WO2024263195A1

WO2024263195A1 - Methods for treatment of liver cancer

Info

Publication number: WO2024263195A1
Application number: PCT/US2023/069032
Authority: WO
Inventors: Stephen Paul HACK
Original assignee: Genentech Inc
Current assignee: Genentech Inc
Priority date: 2023-06-23
Filing date: 2023-06-23
Publication date: 2024-12-26
Anticipated expiration: 2025-12-23
Also published as: WO2024263195A8

Abstract

The present invention relates to the treatment of liver cancer, e.g., hepatocellular carcinoma (HCC), e.g., resectable HCC. More specifically, the invention pertains to the treatment of patients having an HCC by administering (i) a combination of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab); (ii) a combination of a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab); or (iii) a combination of a bispecific antibody that binds to PD-1 and LAGS (e.g., tobemstomig) and a VEGF antagonist (e.g., bevacizumab).

Description

PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO METHODS FOR TREATMENT OF LIVER CANCER SEQUENCE LISTING The instant application contains a Sequence Listing which has been submitted electronically in XML format and is hereby incorporated by reference in its entirety. Said XML copy, created on June 23, 2023, is named 50474-336WO1_Sequence_Listing_6_23_23, and is 68,911 bytes in size. FIELD OF THE INVENTION The present invention relates to the treatment of liver cancer, e.g., hepatocellular carcinoma (HCC), e.g., resectable HCC. More specifically, the invention pertains to the treatment of patients having an HCC by administering (i) a combination of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab); (ii) a combination of a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab); or (iii) a combination of a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) and a VEGF antagonist (e.g., bevacizumab). BACKGROUND OF THE INVENTION Primary liver cancer is the fifth most common cancer and the second most frequent cause of cancer-related death globally, with 854,000 new cases and 810,000 deaths per year. Hepatocellular carcinoma (HCC) accounts for 75%í90% of all primary liver cancers and typically arises in the setting of chronic liver disease, including alcohol consumption, chronic viral hepatitis (B or C), and nonalcoholic fatty liver disease. An estimated 72% of HCC cases arise in Asia, with more than half occurring in China. The incidence and mortality of HCC is rising in the United States and Europe. Surgical resection is a mainstay of curative treatment for patients diagnosed with HCC. However, only 15%í30% of patients are considered candidates for surgery. For patients who undergo potentially curative resection, the risk of post-operative recurrence is unacceptably high (70%í80% within 5 years), even in patients considered optimal candidates for surgery. For high-risk patients with large tumors, multinodular disease, or vascular invasion, the risk of recurrence is further amplified. Globally, approximately 50%í60% of curative-intent liver resections are undertaken in patients at high risk of tumor recurrence. In most cases, HCC recurrence occurs “early,” within 2 years of resection, and post- recurrence survival among patients with early recurrence tends to be worse compared with patients who recur late. The vast majority (approximately 80%) of post-operative HCC recurrences are intrahepatic, and most liver resections result in microscopically negative surgical margins (R0), collectively indicating that HCC recurrence is primarily attributable to intrahepatic micrometastases that persist after surgery. Adjuvant (after surgery), neoadjuvant (before surgery), or perioperative (before and after surgery) therapeutic strategies that can effectively target micrometastatic disease and/or improve resectability through tumor downstaging have the potential to improve outcomes for patients with HCC. Unlike other major cancer types, no effective perioperative treatment is available to patients with HCC. The potential benefit of neoadjuvant therapy in improving HCC resectability and eliminating PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO micrometastases has been recognized for decades, but the development of neoadjuvant therapy for HCC has been hindered by a lack of effective systemic treatments. Until recently, sorafenib was the standard of care for unresectable HCC, but its low response rate (< 10%) and lack of benefit in the adjuvant setting have limited its application as a neoadjuvant therapy. Preoperative locoregional interventions such as transarterial chemoembolization (TACE) have generally failed to show evidence of clinical benefit. High response rates with immunotherapy-based treatment in advanced disease have bolstered interest in their evaluation in the neoadjuvant setting. Therefore, there is a significant need for novel, effective neoadjuvant and adjuvant therapies for patients with HCC. SUMMARY OF THE INVENTION In one aspect, the invention provides a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, one, two, or three dosing cycles are completed prior to the surgery. In some aspects, three dosing cycles are completed prior to the surgery. In some aspects, the atezolizumab is administered at a fixed dose of about 1200 mg every three weeks. In some aspects, the bevacizumab is administered at a dose of about 15 mg/kg every three weeks. In some aspects, the tiragolumab is administered at a fixed dose of about 600 mg every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days. In some aspects, the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the tiragolumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the method comprises administering to the subject atezolizumab before bevacizumab and/or comprises administering to the subject bevacizumab before tiragolumab. In some aspects, the method comprises administering to the subject atezolizumab first, bevacizumab second, and tiragolumab third. In some aspects, the method comprises administering to the subject atezolizumab, bevacizumab, and/or tiragolumab intravenously. In some aspects, the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject (a) one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, one, two, or three dosing cycles of atezolizumab and bevacizumab are completed prior to the surgery. In some aspects, three dosing cycles of atezolizumab and bevacizumab are completed prior to the surgery. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, the atezolizumab is administered at a fixed dose of about 1200 mg every three weeks. In some aspects, the bevacizumab is administered at a dose of about 15 mg/kg every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days. In some aspects, the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the method comprises administering to the subject atezolizumab before bevacizumab. In some aspects, the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously. In some aspects, the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject (a) one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, one, two, or three dosing cycles are completed prior to the surgery. In some aspects, three dosing cycles are completed prior to the surgery. In some aspects, the tobemstomig is administered at a fixed dose of about 600 mg every three weeks. In some aspects, the bevacizumab is administered at a dose of about 15 mg/kg every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days. In some aspects, the tobemstomig is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the method comprises administering to the subject tobemstomig before bevacizumab. In some aspects, the method comprises administering to the subject tobemstomig and/or bevacizumab intravenously. In some aspects, the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject (a) one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, between 1 and 17 dosing cycles of atezolizumab and bevacizumab are administered to the subject as an adjuvant therapy after the surgery. In some aspects, 17 dosing cycles of atezolizumab and bevacizumab are administered to the subject as an adjuvant therapy after the surgery. In some aspects, dosing cycles of atezolizumab and bevacizumab are administered to the subject as an adjuvant therapy for up to 12 months after the surgery. In some aspects, the adjuvant therapy comprises administering the atezolizumab to the subject at a fixed dose of about 1200 mg every three weeks. In some aspects, the adjuvant therapy comprises administering the bevacizumab to the subject at a dose of about 15 mg/kg every three weeks. In some aspects, the length of each of the one or more dosing cycles of the adjuvant therapy is 21 days. In some aspects, the atezolizumab is administered on about Day 1 of each 21-day dosing cycle of the adjuvant therapy. In some aspects, the bevacizumab is administered on about Day 1 of each 21-day dosing cycle of the adjuvant therapy. In some aspects, the method comprises administering to the subject atezolizumab before bevacizumab during each of the one or more dosing cycles of the adjuvant therapy. In some aspects, the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously during each of the one or more dosing cycles of the adjuvant therapy. In another aspect, the invention provides atezolizumab, bevacizumab, and/or tiragolumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, one, two, or three dosing cycles are to be completed prior to the surgery. In some aspects, three dosing cycles are to be completed prior to the surgery. In some aspects, the atezolizumab is to be administered at a fixed dose of about 1200 mg every three weeks. In some aspects, the bevacizumab is to be administered at a dose of about 15 mg/kg every three weeks. In some aspects, the tiragolumab is to be administered at a fixed dose of about 600 mg every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days. In some aspects, the atezolizumab is to be administered on about Day 1 of each 21-day dosing cycle. In some aspects, the bevacizumab to be is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the tiragolumab is to be administered on about Day 1 of each 21-day dosing cycle. In some aspects, the method comprises administering to the subject atezolizumab before bevacizumab. In some aspects, the method comprises administering to the subject bevacizumab before tiragolumab. In some aspects, the method comprises administering to the subject atezolizumab first, bevacizumab second, and tiragolumab third. In some aspects, the method comprises administering to the subject atezolizumab, bevacizumab, and/or tiragolumab intravenously. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides atezolizumab, bevacizumab, and/or tiragolumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject (a) one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides atezolizumab and/or bevacizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, one, two, or three dosing cycles of atezolizumab and bevacizumab are to be completed prior to the surgery. In some aspects, three dosing cycles of atezolizumab and bevacizumab are to be completed prior to the surgery. In some aspects, the atezolizumab is to be administered at a fixed dose of about 1200 mg every three weeks. In some aspects, the bevacizumab is to be administered at a dose of about 15 mg/kg every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days. In some aspects, the atezolizumab is to be administered on about Day 1 of each 21-day dosing cycle. In some aspects, the bevacizumab is to be administered on about Day 1 of each 21-day dosing cycle. In some aspects, the method comprises administering to the subject atezolizumab before bevacizumab. In some aspects, the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously. In some aspects, the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides atezolizumab and/or bevacizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject (a) one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides tobemstomig and/or bevacizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, one, two, or three dosing cycles are to be completed prior to the surgery. In some aspects, three dosing cycles are to be completed prior to the surgery. In some aspects, the tobemstomig is to be administered at a fixed dose of about 600 mg every three weeks. In some aspects, the bevacizumab is to be administered at a dose of about 15 mg/kg every three weeks. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, the length of each of the one or more dosing cycles is 21 days. In some aspects, the tobemstomig is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the bevacizumab is to be administered on about Day 1 of each 21-day dosing cycle. In some aspects, the method comprises administering to the subject tobemstomig before bevacizumab. In some aspects, the method comprises administering to the subject tobemstomig and/or bevacizumab intravenously. In some aspects, the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In another aspect, the invention provides tobemstomig, bevacizumab, and/or atezolizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject (a) one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. In some aspects, between 1 and 17 dosing cycles of atezolizumab and bevacizumab are to be administered to the subject as an adjuvant therapy after the surgery. In some aspects, 17 dosing cycles of atezolizumab and bevacizumab are to be administered to the subject as an adjuvant therapy after the surgery. In some aspects, dosing cycles of atezolizumab and bevacizumab are to be administered to the subject as an adjuvant therapy for up to 12 months after the surgery. In some aspects, the adjuvant therapy comprises administering the atezolizumab to the subject at a fixed dose of about 1200 mg every three weeks. In some aspects, the adjuvant therapy comprises administering the bevacizumab to the subject at a dose of about 15 mg/kg every three weeks. In some aspects, the length of each of the one or more dosing cycles of the adjuvant therapy is 21 days. In some aspects, the atezolizumab is to be administered on about Day 1 of each 21-day dosing cycle of the adjuvant therapy. In some aspects, the bevacizumab is to be administered on about Day 1 of each 21-day dosing cycle of the adjuvant therapy. In some aspects, the method comprises administering to the subject atezolizumab before bevacizumab during each of the one or more dosing cycles of the adjuvant therapy. In some aspects, the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously during each of the one or more dosing cycles of the adjuvant therapy. In some aspects, the HCC is a resectable HCC. In some aspects, the subject has received no prior systemic or locoregional treatment for HCC. In some aspects, the subject does not have extrahepatic disease. In some aspects, the subject does not have macroscopic vascular invasion (MVI). In some aspects, the subject has been determined to have adequate liver function. In some aspects, the adequate liver function is characterized as Child-Pugh class A. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, (a) the subject has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) the subject has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm. In some aspects, the subject is within the Milan criteria. In some aspects, (a) the subject has a single HCC tumor with a longest diameter of > 5 cm; (b) the subject has between two and three HCC tumor nodules, and at least two of the nodules have a longest diameter of >3 cm; or (c) the subject has four or more HCC tumor nodules. In some aspects, the subject is beyond the Milan criteria. In some aspects, the surgery is a liver resection. In some aspects, the surgery is a negative surgical margins (R0) surgical resection. In some aspects, the surgery has curative intent. In some aspects, the surgery is performed at least 28 days after the last day of the one or more dosing cycles. In some aspects, the treating results in an increase in the major pathologic response (MPR) rate as compared to a reference MPR rate. In some aspects, the reference MPR rate is the MPR rate of a population of subjects who have received a control treatment. In some aspects, the treating results in an increase in the pathologic complete response (pCR) rate as compared to a reference pCR rate. In some aspects, the reference pCR rate is the pCR rate of a population of subjects who have received a control treatment. In some aspects, the treating results in an increase in the duration of event-free survival (EFS) as compared to a reference EFS duration. In some aspects, the reference EFS duration is the mean or median EFS duration of a population of subjects who have received a control treatment. In some aspects, the treating results in an increase in the duration of overall survival (OS) as compared to a reference OS duration. In some aspects, the reference OS duration is the mean or median OS duration of a population of subjects who have received a control treatment. In some aspects, the treating results in an increase in the objective response rate (ORR) as compared to a reference ORR. In some aspects, the reference ORR is the ORR of a population of subjects who have received a control treatment. In some aspects, the treating results in an increase in the proportion of patients that are downstaged to within Milan criteria as compared to the proportion in a reference population. In some aspects, the proportion in a reference population is the proportion of patients that are downstaged to within Milan criteria in a population of subjects who have received a control treatment. In some aspects, the treating results in an increase in the R0 resection rate as compared to a reference R0 resection rate. In some aspects, the reference R0 resection rate is the R0 resection rate of a population of subjects who have received a control treatment. In some aspects, the subject is a human. BRIEF DESCRIPTION OF THE DRAWINGS FIG.1 is a schematic diagram showing the overall design of the GO44457 study. HCC= hepatocellular carcinoma; ECOG=Eastern Cooperative Oncology Group; EHS= extrahepatic spread; MVI =macroscopic vascular invasion; PR= partial response; ORR= objective response rate; RFS= relapse-free PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO survival; OS= overall survival; R0= negative surgical margins; R= randomization; atezo = atezolizumab; bev = bevacizumab. FIG.2 is a schematic diagram showing the overall design of the GO44457 study. Tira = tiragolumab; tobe = tobemstomig; RSXN= resection. DETAILED DESCRIPTION OF THE INVENTION I. Definitions The term “about” as used herein refers to the usual error range for the respective value readily known to the skilled person in this technical field. Reference to “about” a value or parameter herein includes (and describes) aspects that are directed to that value or parameter per se. For example, description referring to “about X” includes description of “X.” The term “comparator” or “comparator arm” as used herein refers to a reference (e.g., a reference population of patients) used as a basis of comparison for a treatment or treatment arm in a study, e.g., a clinical trial. For example, a comparator arm may be a control arm in a clinical trial. The comparator arm may include a population of patients who have received a control treatment, such as one or more previously approved treatments or marketed products. A “reference sample,” “reference cell,” “reference tissue,” “control sample,” “control cell,” or “control tissue,” as used herein, refers to a sample, cell, tissue, standard, or level that is used for comparison purposes. In one embodiment, a reference sample, reference cell, reference tissue, control sample, control cell, or control tissue is obtained from a healthy and/or non-diseased part of the body (e.g., tissue or cells) of the same subject. For example, healthy and/or non-diseased cells or tissue adjacent to the diseased cells or tissue (e.g., cells or tissue adjacent to a tumor). In another embodiment, a reference sample is obtained from an untreated tissue and/or cell of the body of the same subject. In yet another embodiment, a reference sample, reference cell, reference tissue, control sample, control cell, or control tissue is obtained from a healthy and/or non-diseased part of the body (e.g., tissues or cells) of a subject who is not the subject. In even another embodiment, a reference sample, reference cell, reference tissue, control sample, control cell, or control tissue is obtained from an untreated tissue and/or cell of the body of an individual who is not the subject. The term “TIGIT” or “T-cell immunoreceptor with Ig and ITIM domains” as used herein refers to any native TIGIT from any vertebrate source, including mammals such as primates (e.g., humans) and rodents (e.g., mice and rats), unless otherwise indicated. TIGIT is also known in the art as DKFZp667A205, FLJ39873, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3, VSIG9, VSTM3, and WUCAM. The term encompasses “full- length,” unprocessed TIGIT (e.g., full-length human TIGIT having the amino acid sequence of SEQ ID NO: 30), as well as any form of TIGIT that results from processing in the cell (e.g., processed human TIGIT without a signal sequence, having the amino acid sequence of SEQ ID NO: 31). The term also encompasses naturally occurring variants of TIGIT, e.g., splice variants or allelic variants. The amino acid sequence of an exemplary human TIGIT may be found under UniProt Accession Number Q495A1. As used herein, “tiragolumab” is a fully human IgG1/kappa MAb-derived in Open Monoclonal Technology (OMT) rats that binds TIGIT and comprises the heavy chain sequence of SEQ ID NO: 33 and PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO the light chain sequence of SEQ ID NO: 34. Tiragolumab comprises two N-linked glycosylation sites (N306) in the Fc domain. Tiragolumab is also described in WHO Drug Information (International Nonproprietary Names for Pharmaceutical Substances), Proposed INN: List 117, Vol.31, No.2, published June 9, 2017 (see page 343). The term “anti-TIGIT antagonist antibody” refers to an antibody or an antigen-binding fragment or variant thereof that is capable of binding TIGIT with sufficient affinity such that it substantially or completely inhibits the biological activity of TIGIT. For example, an anti-TIGIT antagonist antibody may block signaling through PVR, PVRL2, and/or PVRL3 so as to restore a functional response by T-cells (e.g., proliferation, cytokine production, target cell killing) from a dysfunctional state to antigen stimulation. For example, an anti-TIGIT antagonist antibody may block signaling through PVR without impacting PVR- CD226 interaction. It will be understood by one of ordinary skill in the art that in some instances, an anti- TIGIT antagonist antibody may antagonize one TIGIT activity without affecting another TIGIT activity. For example, an anti-TIGIT antagonist antibody for use in certain of the methods or uses described herein is an anti-TIGIT antagonist antibody that antagonizes TIGIT activity in response to one of PVR interaction, PVRL3 interaction, or PVRL2 interaction, e.g., without affecting or minimally affecting any of the other TIGIT interactions. In one aspect, the extent of binding of an anti-TIGIT antagonist antibody to an unrelated, non-TIGIT protein is less than about 10% of the binding of the antibody to TIGIT as measured, e.g., by a radioimmunoassay (RIA). In certain aspects, an anti-TIGIT antagonist antibody that binds to TIGIT has a dissociation constant (K_D) of ^ 1^M, ^ 100 nM, ^ 10 nM, ^ 1 nM, ^ 0.1 nM, ^ 0.01 nM, or ^ 0.001 nM (e.g., 10^-8 M or less, e.g., from 10^-8 M to 10^-13 M, e.g., from 10^-9 M to 10^-13 M). In certain aspects, an anti-TIGIT antagonist antibody binds to an epitope of TIGIT that is conserved among TIGIT from different species or an epitope on TIGIT that allows for cross-species reactivity. In some aspects, the anti-TIGIT binding antibody has intact Fc-mediated effector function (e.g., tiragolumab, vibostolimab, etigilimab, EOS084448, or TJ-T6). In some aspects, the anti-TIGIT binding antibody has enhanced Fc- mediated effector function (e.g., SGN-TGT). In other aspects, the anti-TIGIT binding antibody lacks Fc- mediated effector function (e.g., domvanalimab, BMS-986207, ASP8374, or COM902). In some aspects, the anti-TIGIT binding antibody is an IgG1 class antibody (e.g., tiragolumab, vibostolimab, domvanalimab, BMS-986207, etigilimab, BGB-A1217, SGN-TGT, EOS084448 (EOS-448), TJ-T6, or AB308). In other aspects, the anti-TIGIT binding antibody is an IgG4 class antibody (e.g., ASP8374 or COM902). In one aspect, the anti-TIGIT antagonist antibody is tiragolumab. The terms “programmed death ligand 1” and “PD-L1” refer herein to native sequence human PD- L1 polypeptide. Native sequence PD-L1 polypeptides are provided under Uniprot Accesion No. Q9NZQ7. For example, the native sequence PD-L1 may have the amino acid sequence as set forth in Uniprot Accesion No. Q9NZQ7-1 (isoform 1) (SEQ ID NO: 32). In another example, the native sequence PD-L1 may have the amino acid sequence as set forth in Uniprot Accesion No. Q9NZQ7-2 (isoform 2). In yet another example, the native sequence PD-L1 may have the amino acid sequence as set forth in Uniprot Accesion No. Q9NZQ7-3 (isoform 3). PD-L1 is also referred to in the art as “programmed cell death 1 ligand 1,” “PDCD1LG1,” “CD274,” “B7-H,” and “PDL1.” For the purposes herein, “atezolizumab” is an Fc-engineered, humanized, non-glycosylated IgG1 kappa immunoglobulin that binds PD-L1 and comprises the heavy chain sequence of SEQ ID NO: 1 and PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO the light chain sequence of SEQ ID NO: 2. Atezolizumab comprises a single amino acid substitution (asparagine to alanine) at position 297 on the heavy chain (N297A) using EU numbering of Fc region amino acid residues, which results in a non-glycosylated antibody that has minimal binding to Fc receptors. Atezolizumab is also described in WHO Drug Information (International Nonproprietary Names for Pharmaceutical Substances), Proposed INN: List 112, Vol.28, No.4, published January 16, 2015 (see page 485). The term “PD-1 axis binding antagonist” refers to a molecule that inhibits the interaction of a PD-1 axis binding partner with either one or more of its binding partners, so as to remove T-cell dysfunction resulting from signaling on the PD-1 signaling axis, with a result being to restore or enhance T-cell function (e.g., proliferation, cytokine production, and/or target cell killing). As used herein, a PD-1 axis binding antagonist includes a PD-L1 binding antagonist, a PD-1 binding antagonist, and a PD-L2 binding antagonist. In some instances, the PD-1 axis binding antagonist includes a PD-L1 binding antagonist or a PD-1 binding antagonist. In a preferred aspect, the PD-1 axis binding antagonist is a PD-L1 binding antagonist. The term “PD-L1 binding antagonist” refers to a molecule that decreases, blocks, inhibits, abrogates, or interferes with signal transduction resulting from the interaction of PD-L1 with either one or more of its binding partners, such as PD-1 and/or B7-1. In some instances, a PD-L1 binding antagonist is a molecule that inhibits the binding of PD-L1 to its binding partners. In a specific aspect, the PD-L1 binding antagonist inhibits binding of PD-L1 to PD-1 and/or B7-1. In some instances, the PD-L1 binding antagonists include anti-PD-L1 antibodies, antigen-binding fragments thereof, immunoadhesins, fusion proteins, oligopeptides and other molecules that decrease, block, inhibit, abrogate or interfere with signal transduction resulting from the interaction of PD-L1 with one or more of its binding partners, such as PD-1 and/or B7-1. In one instance, a PD-L1 binding antagonist reduces the negative co-stimulatory signal mediated by or through cell surface proteins expressed on T lymphocytes mediated signaling through PD- L1 so as to render a dysfunctional T-cell less dysfunctional (e.g., enhancing effector responses to antigen recognition). In some instances, the PD-L1 binding antagonist binds to PD-L1. In some instances, a PD- L1 binding antagonist is an anti-PD-L1 antibody (e.g., an anti-PD-L1 antagonist antibody). Exemplary anti-PD-L1 antagonist antibodies include atezolizumab, MDX-1105, MEDI4736 (durvalumab), MSB0010718C (avelumab), SHR-1316, CS1001, envafolimab, TQB2450, ZKAB001, LP-002, CX-072, IMC-001, KL-A167, APL-502, cosibelimab, lodapolimab, FAZ053, TG-1501, BGB-A333, BCD-135, AK- 106, LDP, GR1405, HLX20, MSB2311, RC98, PDL-GEX, KD036, KY1003, YBL-007, and HS-636. In some aspects, the anti-PD-L1 antibody is atezolizumab, MDX-1105, MEDI4736 (durvalumab), or MSB0010718C (avelumab). In one specific aspect, the PD-L1 binding antagonist is MDX-1105. In another specific aspect, the PD-L1 binding antagonist is MEDI4736 (durvalumab). In another specific aspect, the PD-L1 binding antagonist is MSB0010718C (avelumab). In other aspects, the PD-L1 binding antagonist may be a small molecule, e.g., GS-4224, INCB086550, MAX-10181, INCB090244, CA-170, or ABSK041, which in some instances may be administered orally. Other exemplary PD-L1 binding antagonists include AVA-004, MT-6035, VXM10, LYN192, GB7003, and JS-003. In a preferred aspect, the PD-L1 binding antagonist is atezolizumab. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO The term “PD-1 binding antagonist” refers to a molecule that decreases, blocks, inhibits, abrogates or interferes with signal transduction resulting from the interaction of PD-1 with one or more of its binding partners, such as PD-L1 and/or PD-L2. PD-1 (programmed death 1) is also referred to in the art as “programmed cell death 1,” “PDCD1,” “CD279,” and “SLEB2.” An exemplary human PD-1 is shown in UniProtKB/Swiss-Prot Accession No. Q15116. In some instances, the PD-1 binding antagonist is a molecule that inhibits the binding of PD-1 to one or more of its binding partners. In a specific aspect, the PD-1 binding antagonist inhibits the binding of PD-1 to PD-L1 and/or PD-L2. For example, PD-1 binding antagonists include anti-PD-1 antibodies, antigen-binding fragments thereof, immunoadhesins, fusion proteins, oligopeptides, and other molecules that decrease, block, inhibit, abrogate or interfere with signal transduction resulting from the interaction of PD-1 with PD-L1 and/or PD-L2. In one instance, a PD-1 binding antagonist reduces the negative co-stimulatory signal mediated by or through cell surface proteins expressed on T lymphocytes mediated signaling through PD-1 so as render a dysfunctional T-cell less dysfunctional (e.g., enhancing effector responses to antigen recognition). In some instances, the PD-1 binding antagonist binds to PD-1. In some instances, the PD-1 binding antagonist is an anti-PD-1 antibody (e.g., an anti-PD-1 antagonist antibody). Exemplary anti-PD-1 antagonist antibodies include nivolumab, pembrolizumab, MEDI-0680, PDR001 (spartalizumab), REGN2810 (cemiplimab), BGB-108, prolgolimab, camrelizumab, sintilimab, tislelizumab, toripalimab, dostarlimab, retifanlimab, sasanlimab, penpulimab, CS1003, HLX10, SCT-I10A, zimberelimab, balstilimab, genolimzumab, BI 754091, cetrelimab, YBL-006, BAT1306, HX008, budigalimab, AMG 404, CX-188, JTX-4014, 609A, Sym021, LZM009, F520, SG001, AM0001, ENUM 244C8, ENUM 388D4, STI-1110, AK-103, and hAb21. In a specific aspect, a PD-1 binding antagonist is MDX-1106 (nivolumab). In another specific aspect, a PD-1 binding antagonist is MK-3475 (pembrolizumab). In another specific aspect, a PD-1 binding antagonist is a PD-L2 Fc fusion protein, e.g., AMP-224. In another specific aspect, a PD-1 binding antagonist is MED1- 0680. In another specific aspect, a PD-1 binding antagonist is PDR001 (spartalizumab). In another specific aspect, a PD-1 binding antagonist is REGN2810 (cemiplimab). In another specific aspect, a PD-1 binding antagonist is BGB-108. In another specific aspect, a PD-1 binding antagonist is prolgolimab. In another specific aspect, a PD-1 binding antagonist is camrelizumab. In another specific aspect, a PD-1 binding antagonist is sintilimab. In another specific aspect, a PD-1 binding antagonist is tislelizumab. In another specific aspect, a PD-1 binding antagonist is toripalimab. Other additonal exemplary PD-1 binding antagonists include BION-004, CB201, AUNP-012, ADG104, and LBL-006. The term “PD-L2 binding antagonist” refers to a molecule that decreases, blocks, inhibits, abrogates or interferes with signal transduction resulting from the interaction of PD-L2 with either one or more of its binding partners, such as PD-1. PD-L2 (programmed death ligand 2) is also referred to in the art as “programmed cell death 1 ligand 2,” “PDCD1LG2,” “CD273,” “B7-DC,” “Btdc,” and “PDL2.” An exemplary human PD-L2 is shown in UniProtKB/Swiss-Prot Accession No. Q9BQ51. In some instances, a PD-L2 binding antagonist is a molecule that inhibits the binding of PD-L2 to one or more of its binding partners. In a specific aspect, the PD-L2 binding antagonist inhibits binding of PD-L2 to PD-1. Exemplary PD-L2 antagonists include anti-PD-L2 antibodies, antigen binding fragments thereof, immunoadhesins, fusion proteins, oligopeptides and other molecules that decrease, block, inhibit, abrogate or interfere with signal transduction resulting from the interaction of PD-L2 with either one or more of its binding partners, PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO such as PD-1. In one aspect, a PD-L2 binding antagonist reduces the negative co-stimulatory signal mediated by or through cell surface proteins expressed on T lymphocytes mediated signaling through PD-L2 so as render a dysfunctional T-cell less dysfunctional (e.g., enhancing effector responses to antigen recognition). In some aspects, the PD-L2 binding antagonist binds to PD-L2. In some aspects, a PD-L2 binding antagonist is an immunoadhesin. In other aspects, a PD-L2 binding antagonist is an anti- PD-L2 antagonist antibody. A “VEGF antagonist” or “VEGF-specific antagonist” refers to a molecule capable of binding to VEGF, reducing VEGF expression levels, or neutralizing, blocking, inhibiting, abrogating, reducing, or interfering with VEGF biological activities, including, but not limited to, VEGF binding to one or more VEGF receptors, VEGF signaling, and VEGF mediated angiogenesis and endothelial cell survival or proliferation. For example, a molecule capable of neutralizing, blocking, inhibiting, abrogating, reducing, or interfering with VEGF biological activities can exert its effects by binding to one or more VEGF receptor (VEGFR) (e.g., VEGFR1, VEGFR2, VEGFR3, membrane-bound VEGF receptor (mbVEGFR), or soluble VEGF receptor (sVEGFR)). Such antagonists are also referred to herein as “VEGFR inhibitors.” Included as VEGF-specific antagonists useful in the methods of the invention are polypeptides that specifically bind to VEGF, anti-VEGF antibodies and antigen-binding fragments thereof, receptor molecules and derivatives which bind specifically to VEGF thereby sequestering its binding to one or more receptors, fusions proteins (e.g., VEGF-Trap (Regeneron)), and VEGF₁₂₁-gelonin (Peregrine). VEGF-specific antagonists also include antagonist variants of VEGF polypeptides, antisense nucleobase oligomers complementary to at least a fragment of a nucleic acid molecule encoding a VEGF polypeptide; small RNAs complementary to at least a fragment of a nucleic acid molecule encoding a VEGF polypeptide; ribozymes that target VEGF; peptibodies to VEGF; and VEGF aptamers. VEGF antagonists also include polypeptides that bind to VEGFR, anti-VEGFR antibodies, and antigen-binding fragments thereof, and derivatives which bind to VEGFR thereby blocking, inhibiting, abrogating, reducing, or interfering with VEGF biological activities (e.g., VEGF signaling), or fusions proteins. VEGF-specific antagonists also include nonpeptide small molecules that bind to VEGF or VEGFR and are capable of blocking, inhibiting, abrogating, reducing, or interfering with VEGF biological activities. Thus, the term “VEGF biological activities” specifically includes VEGF-mediated biological activities of VEGF. In certain embodiments, the VEGF antagonist reduces or inhibits, by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or more, the expression level or biological activity of VEGF. In some embodiments, the VEGF inhibited by the VEGF-specific antagonist is VEGF (8-109), VEGF (1-109), or VEGF₁₆₅. As used herein VEGF antagonists can include, but are not limited to, anti-VEGFR2 antibodies and related molecules (e.g., ramucirumab, tanibirumab, aflibercept), anti-VEGFR1 antibodies and related molecules (e.g., icrucumab, aflibercept (VEGF Trap-Eye; EYLEA®), and ziv-aflibercept (VEGF Trap; ZALTRAP®)), bispecific VEGF antibodies (e.g., MP-0250, vanucizumab (VEGF-ANG2), and bispecific antibodies disclosed in US 2001/0236388), bispecific antibodies including combinations of two of anti- VEGF, anti-VEGFR1, and anti-VEGFR2 arms, anti-VEGFA antibodies (e.g., bevacizumab, sevacizumab), anti-VEGFB antibodies, anti-VEGFC antibodies (e.g., VGX-100), anti-VEGFD antibodies, and nonpeptide small molecule VEGF antagonists (e.g., pazopanib, axitinib, vandetanib, stivarga, cabozantinib, lenvatinib, nintedanib, orantinib, telatinib, dovitinig, cediranib, motesanib, sulfatinib, apatinib, foretinib, famitinib, and PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO tivozanib). In some examples, the VEGF antagonist may be a tyrosine kinase inhibitor, including a receptor tyrosine kinase inhibitors (e.g., a multi-targeted receptor tyrosine kinase inhibitor such as sunitinib or axitinib). An “anti-VEGF antibody” is an antibody that binds to VEGF with sufficient affinity and specificity. In certain embodiments, the antibody will have a sufficiently high binding affinity for VEGF, for example, the antibody may bind hVEGF with a KD value of between 100 nM and 1 pM. Antibody affinities may be determined, e.g., by a surface plasmon resonance-based assay (such as the BIAcore® assay as described in PCT Application Publication No. WO2005/012359); enzyme-linked immunoabsorbent assay (ELISA); and competition assays (e.g., radioimmunoassays (RIAs)). In certain embodiments, the anti-VEGF antibody can be used as a therapeutic agent in targeting and interfering with diseases or conditions wherein the VEGF activity is involved. Also, the antibody may be subjected to other biological activity assays, e.g., in order to evaluate its effectiveness as a therapeutic. Such assays are known in the art and depend on the target antigen and intended use for the antibody. Examples include the HUVEC inhibition assay; tumor cell growth inhibition assays (as described in WO 89/06692, for example); antibody-dependent cellular cytotoxicity (ADCC) and complement-mediated cytotoxicity (CDC) assays (U.S. Pat. No.5,500,362); and agonistic activity or hematopoiesis assays (see WO 95/27062). An anti-VEGF antibody will usually not bind to other VEGF homologues such as VEGF-B or VEGF-C, nor other growth factors such as PlGF, PDGF, or bFGF. In one embodiment, anti-VEGF antibody is a monoclonal antibody that binds to the same epitope as the monoclonal anti-VEGF antibody A4.6.1 produced by hybridoma ATCC HB 10709. In another embodiment, the anti-VEGF antibody is a recombinant humanized anti-VEGF monoclonal antibody generated according to Presta et al. (Cancer Res.57:4593-4599, 1997), including, but not limited to, the antibody known as bevacizumab (BV; AVASTIN®). The anti-VEGF antibody “bevacizumab (BV),” also known as “rhuMAb VEGF” or “AVASTIN®,” is a recombinant humanized anti-VEGF monoclonal antibody generated according to Presta et al. (Cancer Res.57:4593-4599, 1997). It comprises mutated human IgG1 framework regions and antigen-binding complementarity-determining regions from the murine anti-hVEGF monoclonal antibody A.4.6.1 that blocks binding of human VEGF to its receptors. Approximately 93% of the amino acid sequence of bevacizumab, including most of the framework regions, is derived from human IgG1, and about 7% of the sequence is derived from the murine antibody A4.6.1. Bevacizumab has a molecular mass of about 149,000 daltons and is glycosylated. Bevacizumab and other humanized anti-VEGF antibodies are further described in U.S. Pat. No.6,884,879, issued Feb.26, 2005, the entire disclosure of which is expressly incorporated herein by reference. The term “bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3,” “bispecific antibody that specifically binds PD-1 and LAG3,” “bispecific antigen binding molecule specific for PD-1 and LAG3,” or an “anti-PD-1/anti-LAG3 antibody” are used interchangeably herein and refer to a bispecific antibody that is capable of binding PD-1 and LAG3 with sufficient affinity such that the antibody is useful as a diagnostic and/or therapeutic agent in targeting PD-1 and LAG3. In some aspects, the anti-PD-1/anti-LAG3 antibody is tobemstomig (also known as RO7247669). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Tobemstomig is a bispecific antibody comprising a first heavy chain comprising an amino acid sequence of SEQ ID NO: 51, a first light chain comprising an amino acid sequence of SEQ ID NO: 52, a second heavy chain comprising an amino acid sequence of SEQ ID NO: 53, and a second light chain comprising an amino acid sequence of SEQ ID NO: 54. Tobemstomig is also described in WHO Drug Information (International Nonproprietary Names for Pharmaceutical Substances), Proposed INN: List 127, Vol.36, No.2, published July 22, 2022 (see page 486). The term “PD-1,” also known as Programmed cell death protein 1, is a type I membrane protein of 288 amino acids that was first described in 1992 (Ishida et al., EMBO J., 11 (1992), 3887–3895). PD-1 is a member of the extended CD28/CTLA-4 family of T cell regulators and has two ligands, PD-L1 (B7-H1, CD274) and PD-L2 (B7-DC, CD273). The protein's structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. The intracellular tail contains two phosphorylation sites located in an immunoreceptor tyrosine-based inhibitory motif and an immunoreceptor tyrosine-based switch motif, which suggests that PD-1 negatively regulates TCR signals. This is consistent with binding of SHP-1 and SHP-2 phosphatases to the cytoplasmic tail of PD-1 upon ligand binding. While PD-1 is not expressed on naïve T cells, it is upregulated following T cell receptor (TCR)-mediated activation and is observed on both activated and exhausted T cells (Agata et al., Int. Immunology 8 (1996), 765-772). These exhausted T-cells have a dysfunctional phenotype and are unable to respond appropriately. Although PD-1 has a relatively wide expression pattern its most important role is likely as a coinhibitory receptor on T cells (Chinai et al, Trends in Pharmacological Sciences 36 (2015), 587-595). Current therapeutic approaches thus focus on blocking the interaction of PD-1 with its ligands to enhance T cell response. The terms “Programmed Death 1,” “Programmed Cell Death 1,” “Protein PD-1,” “PD-1,” PD1,” “PDCD1,” “hPD-1” and “hPD-1” can be used interchangeably, and include variants, isoforms, species homologs of human PD-1, and analogs having at least one common epitope with PD-1. The amino acid sequence of human PD-1 is shown in UniProt (www.uniprot.org) accession no. Q15116 (SEQ ID NO: 55). The term “LAG3,” “Lag-3,” “Lymphocyte activation gene-3,” or “CD223” as used herein refers to any native LAG3 from any vertebrate source, including mammals such as primates (e.g., humans) and rodents (e.g., mice and rats), unless otherwise indicated. The term encompasses “full-length,” unprocessed LAG3 as well as any form of LAG3 resulting from processing in the cell. The term also encompasses naturally occurring variants of LAG3, e.g., splice variants or allelic variants. In one preferred embodiment the term “LAG3” refers to human LAG3. The amino acid sequence of an exemplary processed (without signal sequences) LAG3 is shown in SEQ ID NO: 56. The amino acid sequence of an exemplary Extracellular Domain (ECD) LAG3 is shown in SEQ ID NO: 57. The terms “anti-LAG3 antibody” and “an antibody that binds to LAG3” refer to an antibody that is capable of binding LAG3 with sufficient affinity such that the antibody is useful as a diagnostic and/or therapeutic agent in targeting LAG3. In one aspect, the extent of binding of an anti-LAG3 antibody to an unrelated, non-LAG3 protein is less than about 10% of the binding of the antibody to LAG3 as measured, e.g., by a radioimmunoassay (RIA). In certain embodiments, an antibody that binds to LAG3 has a dissociation constant (KD) of ^ 1^M, ^ 100 nM, ^ 10 nM, ^ 1 nM, ^ 0.1 nM, ^ 0.01 nM, or ^ 0.001 nM (e.g., 10^-8 M or less, e.g., from 10^-8 M to 10^-13 M, e.g., from 10^-9 M to 10^-13 M). In certain aspects, an anti- PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO LAG3 antibody binds to an epitope of LAG3 that is conserved among LAG3 from different species. In one preferred embodiment, an “anti-LAG3 antibody,” “an antibody that specifically binds to human LAG3,” and “an antibody that binds to human LAG3” refers to an antibody specifically binding to the human LAG3 antigen or its Extracellular Domain (ECD) with a binding affinity of a K_D-value of 1.0 x 10^-8 mol/l or lower, in one embodiment of a K_D-value of 1.0 x 10^-9 mol/l or lower, in one embodiment of a K_D-value of 1.0 x 10^-9 mol/l to 1.0 x 10^-13 mol/l. In this context the binding affinity is determined with a standard binding assay, such as surface plasmon resonance technique (BIAcore®, GE-Healthcare Uppsala, Sweden) e.g., using the LAG3 extracellular domain. The term “anti-LAG3 antibody” also encompasses bispecific antibodies that are capable of binding LAG3 and a second antigen. The “knob-into-hole” technology is described e.g., in US 5,731,168; US 7,695,936; Ridgway et al., Prot Eng 9, 617-621 (1996) and Carter, J Immunol Meth 248, 7-15 (2001). Generally, the method involves introducing a protuberance (“knob”) at the interface of a first polypeptide and a corresponding cavity (“hole”) in the interface of a second polypeptide, such that the protuberance can be positioned in the cavity so as to promote heterodimer formation and hinder homodimer formation. Protuberances are constructed by replacing small amino acid side chains from the interface of the first polypeptide with larger side chains (e.g., tyrosine or tryptophan). Compensatory cavities of identical or similar size to the protuberances are created in the interface of the second polypeptide by replacing large amino acid side chains with smaller ones (e.g., alanine or threonine). The protuberance and cavity can be made by altering the nucleic acid encoding the polypeptides, e.g., by site-specific mutagenesis, or by peptide synthesis. In a specific embodiment a knob modification comprises the amino acid substitution T366W in one of the two subunits of the Fc domain, and the hole modification comprises the amino acid substitutions T366S, L368A and Y407V in the other one of the two subunits of the Fc domain. In a further specific embodiment, the subunit of the Fc domain comprising the knob modification additionally comprises the amino acid substitution S354C, and the subunit of the Fc domain comprising the hole modification additionally comprises the amino acid substitution Y349C. Introduction of these two cysteine residues results in the formation of a disulfide bridge between the two subunits of the Fc region, thus further stabilizing the dimer (Carter, J Immunol Methods 248, 7-15 (2001)). The term “cancer” refers to a disease caused by an uncontrolled division of abnormal cells in a part of the body. In one instance, the cancer is hepatocellular carcinoma (HCC), e.g., resectable HCC. The term “tumor” refers to all neoplastic cell growth and proliferation, whether malignant or benign, and all pre-cancerous and cancerous cells and tissues. The terms “cancer,” “cancerous,” “cell proliferative disorder,” “proliferative disorder,” and “tumor” are not mutually exclusive as referred to herein. A “tumor cell” as used herein, refers to any tumor cell present in a tumor or a sample thereof. Tumor cells may be distinguished from other cells that may be present in a tumor sample, for example, stromal cells and tumor-infiltrating immune cells, using methods known in the art and/or described herein. As used herein, “treating” comprises effective cancer treatment with an effective amount of a therapeutic agent (e.g., a PD-1 axis binding antagonist (e.g., atezolizumab); a VEGF antagonist (e.g., bevacizumab); an anti-TIGIT antagonist antibody (e.g., tiragolumab); or a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig)) or combination of therapeutic agents (e.g., a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab); a PD-1 axis binding PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab); or a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) and a VEGF antagonist (e.g., bevacizumab)). Treating herein includes, inter alia, adjuvant therapy, neoadjuvant therapy, non-metastatic cancer therapy (e.g., locally advanced cancer therapy), and metastatic cancer therapy. The treatment may be first-line treatment (e.g., the patient may be previously untreated or not have received prior systemic therapy), or second-line or later treatment. An “effective amount” of a compound, for example, a PD-1 axis binding antagonist (e.g., atezolizumab); a VEGF antagonist (e.g., bevacizumab); an anti-TIGIT antagonist antibody (e.g., tiragolumab); a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig), or a composition (e.g., pharmaceutical composition) thereof, is at least the minimum amount required to achieve the desired therapeutic result, such as a measurable increase in overall survival or progression-free survival of a particular disease or disorder (e.g., cancer, e.g., liver cancer (e.g., HCC, e.g., resectable HCC)). An effective amount herein may vary according to factors such as the disease state, age, sex, and weight of the patient, and the ability of the antibody to elicit a desired response in the subject. An effective amount is also one in which any toxic or detrimental effects of the treatment are outweighed by the therapeutically beneficial effects. For prophylactic use, beneficial or desired results include results such as eliminating or reducing the risk, lessening the severity, or delaying the onset of the disease, including biochemical, histological and/or behavioral symptoms of the disease, its complications, and intermediate pathological phenotypes presenting during development of the disease. For therapeutic use, beneficial or desired results include clinical results such as decreasing one or more symptoms resulting from the disease (e.g., reduction or delay in cancer-related pain, symptomatic skeletal-related events (SSE), reduction in symptoms per the European Organization for Research and Treatment of Cancer Quality-of-Life Questionnaire (EORTC QLQ-C30, e.g., fatigue, nausea, vomiting, pain, dyspnea, insomnia, appetite loss, constipation, diarrhea, or general level of physical emotional, cognitive, or social functioning), reduction in pain as measured by, e.g., the 10-point pain severity (measured at its worst) numerical rating scale (NRS), and/or reduction in symptoms associated with lung cancer per the health-related quality of life (HRQoL) questionnaire as assessed by symptoms in lung cancer (SILC) scale (e.g., time to deterioration (TTD) in cough dyspnea and chest pain), increasing the quality of life of those suffering from the disease, decreasing the dose of other medications required to treat the disease, enhancing effect of another medication such as via targeting, delaying the progression of the disease (e.g. progression-free survival or radiographic progression-free survival (rPFS); delay of unequivocal clinical progression (e.g., cancer- related pain progression, symptomatic skeletal-related event, deterioration in Eastern Cooperative Group Oncology Group (ECOG) Performance Status (PS) (e.g., how the disease affects the daily living abilities of the patient), and/or initiation of next systemic anti-cancer therapy), and/or delaying time to lung-specific antigen progression), and/or prolonging survival. In the case of cancer or tumor, an effective amount of the drug may have the effect in reducing the number of cancer cells; reducing the tumor size; inhibiting (i.e., slow to some extent or desirably stop) cancer cell infiltration into peripheral organs; inhibit (i.e., slow to some extent and desirably stop) tumor metastasis; inhibiting to some extent tumor growth; and/or relieving to some extent one or more of the symptoms associated with the disorder. An effective amount can be administered in one or more administrations. For purposes of this invention, an effective amount PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO of drug, compound, or pharmaceutical composition is an amount sufficient to accomplish prophylactic or therapeutic treatment either directly or indirectly. As is understood in the clinical context, an effective amount of a drug, compound, or pharmaceutical composition may or may not be achieved in conjunction with another drug, compound, or pharmaceutical composition. Thus, an “effective amount” may be considered in the context of administering one or more therapeutic agents, and a single agent may be considered to be given in an effective amount if, in conjunction with one or more other agents, a desirable result may be or is achieved. As used herein, “pathologic complete response rate” and “pCR rate” refer interchangeably to the proportion of patients with a pathologic complete response (pCR), wherein a pCR is defined as an absence of residual tumor in a resected tumor specimen (e.g., a tumor specimen that is resected following neoadjuvant treatment). As used herein, “survival” refers to the patient remaining alive, and includes overall survival as well as progression-free survival. As used herein, “relapse-free survival” and “RFS” refer to the length of time after treatment (e.g., after surgery) during which the disease being treated (e.g., cancer, e.g., liver cancer (e.g., HCC, e.g., resectable HCC)) does not relapse. For example, RFS may be defined as the time from surgical resection to the first documented recurrence of disease (e.g., wherein the cancer is an HCC and the recurrence is intrahepatic or extrahepatic) (e.g., as determined according to European Association for the Study of the Liver (EASL) and/or Response Evaluation Criteria in Solid Tumors (RECIST) v1.1) or death from any cause. As used herein, “event-free survival” and “EFS” refer to the length of time during and after treatment during which none of the following events occur: disease progression that precludes surgery (e.g., as assessed by the investigator according RECIST v1.1), local or distant disease recurrence (e.g., as measured by EASL and/or RECIST v1.1), or death from any cause. As used herein, “overall survival” and “OS” refer to the length of time from either the date of diagnosis or the start of treatment for a disease (e.g., cancer) that the patient is still alive. For example, OS may be defined as the time from first study treatment to death from any cause. As used herein, “complete response” and “CR” refers to disappearance of all target lesions. As used herein, “partial response” and “PR” refers to at least a 30% decrease in the sum of the longest diameters (SLD) of target lesions, taking as reference the baseline SLD prior to treatment. As used here, “progressive disease” and “PD” refers to at least a 20% increase in the SLD of target lesions, taking as reference the smallest sum on study (nadir), including baseline. As used herein, “stable disease” and “SD” refers to neither sufficient shrinkage to qualify for PR nor sufficient increase to qualify for PD. As used herein, “R0 resection rate” refers to the proportion of patients for which an R0 resection is obtained. R0 resection is defined as a microscopically margin-negative resection, in which no tumor (gross or microscopic) remains in the primary tumor bed. As used herein, “subject” or “individual” is meant a mammal, including, but not limited to, a human or non-human mammal, such as a bovine, equine, canine, ovine, or feline. In some embodiments, the subject is a human. Patients are also subjects herein. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO As used herein, a “PD-L1-positive tumor cell fraction” is the percentage of viable tumor cells showing partial or complete membrane staining (exclusive of cytoplasmic staining) at any intensity relative to all viable tumor cells present in a sample, following staining of the sample in the context of an immunohistochemical (IHC) assay, e.g., an IHC assay staining for PD-L1 using the antibody SP142, SP263, 22C3, or 28-8. Accordingly, a PD-L1-positive tumor cell fraction may be calculated using the PD- L1 IHC SP142 (Ventana) assay, for example, by the formula PD-L1-positive tumor cell fraction = (number of PD-L1-positive tumor cells)/(total number of PD-L1-positive and PD-L1 negative tumor cells), wherein PD-L1 cytoplasmic staining of tumor cells and all non-tumor cells (e.g., tumor-infiltrating immune cells, normal cells, necrotic cells, and debris) are excluded from evaluation and scoring. It will be appreciated that any given diagnostic PD-L1 antibody may correspond with a particular IHC assay protocol and/or scoring terminology that can be used to derive a PD-L1-positive tumor cell fraction. For example, a PD- L1-positive tumor cell fraction can be derived from a tumor cell sample stained with SP263, 22C3, SP142, or 28-8 using OPTIVIEW® detection on Benchmark ULTRA, EnVision Flex on AutostainerLink 48, OPTIVIEW® detection and amplification on Benchmark ULTRA, or EnVision Flex on AutostainerLink 48, respectively. As used herein, the “Ventana SP142 IHC assay” is conducted according to the Ventana PD-L1 (SP142) Assay package insert (Tucson, AZ: Ventana Medical Systems, Inc.), which is incorporated herein by reference in its entirety. As used herein, the “Ventana SP263 IHC assay” is conducted according to the Ventana PD-L1 (SP263) Assay package insert (Tucson, AZ: Ventana Medical Systems, Inc.), which is incorporated herein by reference in its entirety. As used herein, the “pharmDx 22C3 IHC assay” is conducted according to the PD-L1 IHC 22C3 pharmDx package insert (Carpinteria, CA: Dako, Agilent Pathology Solutions), which is incorporated herein by reference in its entirety. As used herein, the “pharmDx 28-8 IHC assay” is conducted according to the PD-L1 IHC 28-8 pharmDx package insert (Carpinteria, CA: Dako, Agilent Pathology Solutions), which is incorporated herein by reference in its entirety. The term “package insert” is used to refer to instructions customarily included in commercial packages of therapeutic products, that contain information about the indications, usage, dosage, administration, combination therapy, contraindications and/or warnings concerning the use of such therapeutic products. As used herein, “in combination with” refers to administration of one treatment modality in addition to another treatment modality, for example, a treatment regimen that includes administration of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab); a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab); or a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) and a VEGF antagonist (e.g., bevacizumab). As such, “in combination with” refers to administration of one treatment modality before, during, or after administration of the other treatment modality to the patient. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO A drug that is administered “concurrently” with one or more other drugs is administered during the same treatment cycle, on the same day of treatment, as the one or more other drugs, and, optionally, at the same time as the one or more other drugs. For instance, for cancer therapies given every 3 weeks, the concurrently administered drugs are each administered on day 1 of a 3-week cycle. As used herein, the term “adverse event” or “AE” refers to any unfavorable and unintended sign (including an abnormal laboratory finding), symptom, or disease temporally associated with the use of a medical treatment or procedure that may or may not be considered related to the medical treatment or procedure. Adverse events may be classified by “grade,” as defined by the National Cancer Institute Common Terminology Criteria for Adverse Events v4.0 or v5.0 (NIH CTCAE). In some aspects, the AE is a low-grade AE, e.g., a Grade 1 or Grade 2 AE. Grade 1 includes AEs that are asymptomatic or have mild symptoms. Grade 2 includes AEs that are moderate and limit age-appropriate instrumental activities of daily living (e.g., preparing meals, shopping for groceries or clothes) and that indicate local or noninvasive intervention. In other instances, the AE is a high-grade AE, e.g., a Grade 3, Grade 4, or Grade 5 AE. In some instances, the AE is a Grade 3 or a Grade 4 AE. Grade 3 includes AEs that are severe or medically significant, but not immediately life-threatening, and that indicate hospitalization or prolongation of hospitalization. Grade 4 includes AEs that have life-threatening consequences and indicate urgent intervention. Grade 5 includes AEs that result in or relate to death. As used herein, the term “treatment-related AE” refers to an AE that is judged by an investigator to have occurred as a result of a treatment, e.g., a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab); an anti-TIGIT antagonist antibody (e.g., tiragolumab); or a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig). The term “antibody” herein specifically covers monoclonal antibodies (including full-length monoclonal antibodies), polyclonal antibodies, multispecific antibodies (e.g., bispecific antibodies), and antibody fragments so long as they exhibit the desired biological activity. In one instance, the antibody is a full-length monoclonal antibody. The term IgG “isotype” or “subclass” as used herein is meant any of the subclasses of immunoglobulins defined by the chemical and antigenic characteristics of their constant regions. Depending on the amino acid sequences of the constant domains of their heavy chains, antibodies (immunoglobulins) can be assigned to different classes. There are five major classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM, and several of these may be further divided into subclasses (isotypes), e.g., IgG1, IgG2, IgG3, IgG4, IgA1, and IgA2. The heavy chain constant domains that correspond to the different classes of immunoglobulins are called Į, Ȗ, ^, Ȗ, and μ, respectively. The subunit structures and three-dimensional configurations of different classes of immunoglobulins are well known and described generally in, for example, Abbas et al. Cellular and Mol. Immunology, 4th ed. (W.B. Saunders, Co., 2000). An antibody may be part of a larger fusion molecule, formed by covalent or non- covalent association of the antibody with one or more other proteins or peptides. The terms “full-length antibody,” “intact antibody,” and “whole antibody” are used herein interchangeably to refer to an antibody in its substantially intact form, not antibody fragments as defined below. The terms refer to an antibody comprising an Fc region. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO The term “Fc region” herein is used to define a C-terminal region of an immunoglobulin heavy chain that contains at least a portion of the constant region. The term includes native sequence Fc regions and variant Fc regions. In one aspect, a human IgG heavy chain Fc region extends from Cys226, or from Pro230, to the carboxyl-terminus of the heavy chain. However, antibodies produced by host cells may undergo post-translational cleavage of one or more, particularly one or two, amino acids from the C- terminus of the heavy chain. Therefore, an antibody produced by a host cell by expression of a specific nucleic acid molecule encoding a full-length heavy chain may include the full-length heavy chain, or it may include a cleaved variant of the full-length heavy chain. This may be the case where the final two C- terminal amino acids of the heavy chain are glycine (G446) and lysine (K447). Therefore, the C-terminal lysine (Lys447), or the C-terminal glycine (Gly446) and lysine (Lys447), of the Fc region may or may not be present. Amino acid sequences of heavy chains including an Fc region are denoted herein without the C-terminal lysine (Lys447) if not indicated otherwise. In one aspect, a heavy chain including an Fc region as specified herein, comprised in an antibody disclosed herein, comprises an additional C-terminal glycine-lysine dipeptide (G446 and K447). In one aspect, a heavy chain including an Fc region as specified herein, comprised in an antibody disclosed herein, comprises an additional C-terminal glycine residue (G446). In one aspect, a heavy chain including an Fc region as specified herein, comprised in an antibody disclosed herein, comprises an additional C-terminal lysine residue (K447). In one embodiment, the Fc region contains a single amino acid substitution N297A of the heavy chain. Unless otherwise specified herein, numbering of amino acid residues in the Fc region or constant region is according to the EU numbering system, also called the EU index, as described in Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, MD, 1991. The Kabat numbering system is generally used when referring to a residue in the variable domain (approximately residues 1-107 of the light chain and residues 1-113 of the heavy chain) (e.g., Kabat et al., Sequences of Immunological Interest.5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md. (1991)). The “EU numbering system” or “EU index” is generally used when referring to a residue in an immunoglobulin heavy chain constant region (e.g., the EU index reported in Kabat et al., supra). The “EU index as in Kabat” refers to the residue numbering of the human IgG1 EU antibody. A “naked antibody” refers to an antibody that is not conjugated to a heterologous moiety (e.g., a cytotoxic moiety) or radiolabel. The naked antibody may be present in a pharmaceutical composition. The term “monoclonal antibody” as used herein refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the individual antibodies comprising the population are identical and/or bind the same epitope, except for possible variant antibodies, e.g., containing naturally occurring mutations or arising during production of a monoclonal antibody preparation, such variants generally being present in minor amounts. In contrast to polyclonal antibody preparations, which typically include different antibodies directed against different determinants (epitopes), each monoclonal antibody of a monoclonal antibody preparation is directed against a single determinant on an antigen. Thus, the modifier “monoclonal” indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies, and is not to be construed as requiring production of the antibody by any particular method. For example, the monoclonal antibodies in accordance with the present invention may be made by a variety of techniques, including but not limited to the hybridoma method, PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO recombinant DNA methods, phage-display methods, and methods utilizing transgenic animals containing all or part of the human immunoglobulin loci. The term “hypervariable region” or “HVR” as used herein refers to each of the regions of an antibody variable domain which are hypervariable in sequence and which determine antigen binding specificity, for example “complementarity determining regions” (“CDRs”). Generally, antibodies comprise six CDRs: three in the VH (CDR-H1, CDR-H2, CDR-H3), and three in the VL (CDR-L1, CDR-L2, CDR-L3). Exemplary CDRs herein include: (a) hypervariable loops occurring at amino acid residues 26-32 (L1), 50-52 (L2), 91-96 (L3), 26-32 (H1), 53-55 (H2), and 96-101 (H3) (Chothia and Lesk, J. Mol. Biol.196:901-917 (1987)); (b) CDRs occurring at amino acid residues 24-34 (L1), 50-56 (L2), 89-97 (L3), 31-35b (H1), 50-65 (H2), and 95-102 (H3) (Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, MD (1991)); and (c) antigen contacts occurring at amino acid residues 27c-36 (L1), 46-55 (L2), 89-96 (L3), 30-35b (H1), 47-58 (H2), and 93-101 (H3) (MacCallum et al. J. Mol. Biol.262: 732-745 (1996)). Unless otherwise indicated, the CDRs are determined according to Kabat et al., supra. One of skill in the art will understand that the CDR designations can also be determined according to Chothia, supra, McCallum, supra, or any other scientifically accepted nomenclature system. “Framework” or “FR” refers to variable domain residues other than complementary determining regions (CDRs). The FR of a variable domain generally consists of four FR domains: FR1, FR2, FR3, and FR4. Accordingly, the CDR and FR sequences generally appear in the following sequence in VH (or VL): FR1-CDR-H1(CDR-L1)-FR2- CDR-H2(CDR-L2)-FR3- CDR-H3(CDR-L3)-FR4. The term “variable domain residue numbering as in Kabat” or “amino acid position numbering as in Kabat,” and variations thereof, refers to the numbering system used for heavy chain variable domains or light chain variable domains of the compilation of antibodies in Kabat et al., supra. Using this numbering system, the actual linear amino acid sequence may contain fewer or additional amino acids corresponding to a shortening of, or insertion into, a FR or HVR of the variable domain. For example, a heavy chain variable domain may include a single amino acid insert (residue 52a according to Kabat) after residue 52 of H2 and inserted residues (e.g., residues 82a, 82b, and 82c, etc., according to Kabat) after heavy chain FR residue 82. The Kabat numbering of residues may be determined for a given antibody by alignment at regions of homology of the sequence of the antibody with a “standard” Kabat numbered sequence. The term “monospecific” antibody as used herein denotes an antibody that has one or more binding sites each of which bind to the same epitope of the same antigen. The term “bispecific” antibody as used herein means that the antibody is able to specifically bind to at least two distinct antigens, for example two binding sites each formed by a pair of an antibody heavy chain variable domain (VH) and an antibody light chain variable domain (VL) binding to different antigens or to different epitopes on the same antigen. Such a bispecific antibody is an 1+1 format. Other bispecific antibody formats are 2+1 formats (comprising two binding sites for a first antigen or epitope and one binding site for a second antigen or epitope) or 2+2 formats (comprising two binding sites for a first antigen or epitope and two binding sites PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO for a second antigen or epitope). Typically, a bispecific antibody comprises two antigen binding sites, each of which is specific for a different antigen. The term “valent” as used within the current application denotes the presence of a specified number of binding domains in an antigen binding molecule. As such, the terms “bivalent,” “tetravalent,” and “hexavalent” denote the presence of two binding domains, four binding domains, and six binding domains, respectively, in an antigen binding molecule. The bispecific antibodies according to the invention are at least “bivalent” and may be “trivalent” or “multivalent” (e.g., “tetravalent” or “hexavalent”). In a particular aspect, the antibodies of the present invention have two or more binding sites and are bispecific. That is, the antibodies may be bispecific even in cases where there are more than two binding sites (i.e., that the antibody is trivalent or multivalent). An "antibody fragment" refers to a molecule other than an intact antibody that comprises a portion of an intact antibody that binds the antigen to which the intact antibody binds. Examples of antibody fragments include but are not limited to Fv, Fab, Fab', Fab’-SH, F(ab')₂; diabodies, triabodies, tetrabodies, cross-Fab fragments; linear antibodies; single-chain antibody molecules (e.g., scFv); multispecific antibodies formed from antibody fragments and single domain antibodies. For a review of certain antibody fragments, see Hudson et al., Nat Med 9, 129-134 (2003). For a review of scFv fragments, see e.g., Plückthun, in The Pharmacology of Monoclonal Antibodies, vol.113, Rosenburg and Moore eds., Springer-Verlag, New York, pp.269-315 (1994); see also WO 93/16185; and U.S. Patent Nos.5,571,894 and 5,587,458. For discussion of Fab and F(ab')₂ fragments comprising salvage receptor binding epitope residues and having increased in vivo half-life, see U.S. Patent No.5,869,046. Diabodies are antibody fragments with two antigen-binding domains that may be bivalent or bispecific, see, for example, EP 404,097; WO 1993/01161; Hudson et al., Nat Med 9, 129-134 (2003); and Hollinger et al., Proc Natl Acad Sci USA 90, 6444-6448 (1993). Triabodies and tetrabodies are also described in Hudson et al., Nat Med 9, 129-134 (2003). Single-domain antibodies are antibody fragments comprising all or a portion of the heavy chain variable domain or all or a portion of the light chain variable domain of an antibody. In certain embodiments, a single-domain antibody is a human single-domain antibody (Domantis, Inc., Waltham, MA; see e.g., U.S. Patent No.6,248,516 B1). In addition, antibody fragments comprise single chain polypeptides having the characteristics of a VH domain, namely being able to assemble together with a VL domain, or of a VL domain, namely being able to assemble together with a VH domain to a functional antigen binding site and thereby providing the antigen binding property of full-length antibodies. Antibody fragments can be made by various techniques, including but not limited to proteolytic digestion of an intact antibody as well as production by recombinant host cells (e.g., E. coli or phage), as described herein. Papain digestion of intact antibodies produces two identical antigen-binding fragments, called “Fab” fragments containing each the heavy- and light-chain variable domains and also the constant domain of the light chain and the first constant domain (CH1) of the heavy chain. As used herein, Thus, the term “Fab fragment” refers to an antibody fragment comprising a light chain fragment comprising a VL domain and a constant domain of a light chain (CL), and a VH domain and a first constant domain (CH1) of a heavy chain. Fab’ fragments differ from Fab fragments by the addition of a few residues at the carboxy terminus of the heavy chain CH1 domain including one or more cysteins from the antibody hinge region. Fab’-SH are Fab’ fragments wherein the cysteine residue(s) of the constant domains bear a free PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO thiol group. Pepsin treatment yields an F(ab')₂ fragment that has two antigen-combining sites (two Fab fragments) and a part of the Fc region. The term “cross-Fab fragment” or “xFab fragment” or “crossover Fab fragment” refers to a Fab fragment, wherein either the variable regions or the constant regions of the heavy and light chain are exchanged. Two different chain compositions of a crossover Fab molecule are possible and comprised in the bispecific antibodies of the invention: On the one hand, the variable regions of the Fab heavy and light chain are exchanged, i.e., the crossover Fab molecule comprises a peptide chain composed of the light chain variable region (VL) and the heavy chain constant region (CH1), and a peptide chain composed of the heavy chain variable region (VH) and the light chain constant region (CL). This crossover Fab molecule is also referred to as CrossFab _(VLVH). On the other hand, when the constant regions of the Fab heavy and light chain are exchanged, the crossover Fab molecule comprises a peptide chain composed of the heavy chain variable region (VH) and the light chain constant region (CL), and a peptide chain composed of the light chain variable region (VL) and the heavy chain constant region (CH1). This crossover Fab molecule is also referred to as CrossFab _(CLCH1). A “single chain Fab fragment” or “scFab” is a polypeptide consisting of an antibody heavy chain variable domain (VH), an antibody constant domain 1 (CH1), an antibody light chain variable domain (VL), an antibody light chain constant domain (CL) and a linker, wherein said antibody domains and said linker have one of the following orders in N-terminal to C-terminal direction: a) VH-CH1-linker-VL-CL, b) VL-CL- linker-VH-CH1, c) VH-CL-linker-VL-CH1 or d) VL-CH1-linker-VH-CL; and wherein said linker is a polypeptide of at least 30 amino acids, preferably between 32 and 50 amino acids. Said single chain Fab fragments are stabilized via the natural disulfide bond between the CL domain and the CH1 domain. In addition, these single chain Fab molecules might be further stabilized by generation of interchain disulfide bonds via insertion of cysteine residues (e.g., position 44 in the variable heavy chain and position 100 in the variable light chain according to Kabat numbering). A “crossover single chain Fab fragment” or “x-scFab” is a is a polypeptide consisting of an antibody heavy chain variable domain (VH), an antibody constant domain 1 (CH1), an antibody light chain variable domain (VL), an antibody light chain constant domain (CL) and a linker, wherein said antibody domains and said linker have one of the following orders in N-terminal to C-terminal direction: a) VH-CL- linker-VL-CH1 and b) VL-CH1-linker-VH-CL; wherein VH and VL form together an antigen-binding domain which binds specifically to an antigen and wherein said linker is a polypeptide of at least 30 amino acids. In addition, these x-scFab molecules might be further stabilized by generation of interchain disulfide bonds via insertion of cysteine residues (e.g., position 44 in the variable heavy chain and position 100 in the variable light chain according to Kabat numbering). A “single-chain variable fragment (scFv)” is a fusion protein of the variable regions of the heavy (VH) and light chains (VL) of an antibody, connected with a short linker peptide of ten to about 25 amino acids. The linker is usually rich in glycine for flexibility, as well as serine or threonine for solubility, and can either connect the N-terminus of the V_H with the C-terminus of the V_L, or vice versa. This protein retains the specificity of the original antibody, despite removal of the constant regions and the introduction of the linker. scFv antibodies are, e.g., described in Houston, J.S., Methods in Enzymol.203 (1991) 46- 96). In addition, antibody fragments comprise single chain polypeptides having the characteristics of a VH PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO domain, namely being able to assemble together with a VL domain, or of a VL domain, namely being able to assemble together with a VH domain to a functional antigen binding site and thereby providing the antigen binding property of full-length antibodies. The term “effector functions” refers to those biological activities attributable to the Fc region of an antibody, which vary with the antibody isotype. Examples of antibody effector functions include: C1q binding and complement dependent cytotoxicity (CDC), Fc receptor binding, antibody-dependent cell- mediated cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), cytokine secretion, immune complex-mediated antigen uptake by antigen presenting cells, down regulation of cell surface receptors (e.g., B cell receptor), and B cell activation. An “activating Fc receptor” is an Fc receptor that following engagement by an Fc region of an antibody elicits signaling events that stimulate the receptor-bearing cell to perform effector functions. Activating Fc receptors include FcȖRIIIa (CD16a), FcȖRI (CD64), FcȖRIIa (CD32), and FcĮRI (CD89). A particular activating Fc receptor is human FcȖRIIIa (see UniProt accession no. P08637, version 141). “Percent (%) amino acid sequence identity” with respect to a reference polypeptide sequence is defined as the percentage of amino acid residues in a candidate sequence that are identical with the amino acid residues in the reference polypeptide sequence, after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity, and not considering any conservative substitutions as part of the sequence identity. Alignment for purposes of determining percent amino acid sequence identity can be achieved in various ways that are within the skill in the art, for instance, using publicly available computer software such as BLAST, BLAST-2, ALIGN or Megalign (DNASTAR) software. Those skilled in the art can determine appropriate parameters for aligning sequences, including any algorithms needed to achieve maximal alignment over the full length of the sequences being compared. For purposes herein, however, % amino acid sequence identity values are generated using the sequence comparison computer program ALIGN-2. The ALIGN-2 sequence comparison computer program was authored by Genentech, Inc., and the source code has been filed with user documentation in the U.S. Copyright Office, Washington D.C., 20559, where it is registered under U.S. Copyright Registration No. TXU510087. The ALIGN-2 program is publicly available from Genentech, Inc., South San Francisco, California, or may be compiled from the source code. The ALIGN-2 program should be compiled for use on a UNIX operating system, including digital UNIX V4.0D. All sequence comparison parameters are set by the ALIGN-2 program and do not vary. In situations where ALIGN-2 is employed for amino acid sequence comparisons, the % amino acid sequence identity of a given amino acid sequence A to, with, or against a given amino acid sequence B (which can alternatively be phrased as a given amino acid sequence A that has or comprises a certain % amino acid sequence identity to, with, or against a given amino acid sequence B) is calculated as ^follows: 100 times the fraction X/Y where X is the number of amino acid residues scored as identical matches by the sequence alignment program ALIGN-2 in that program’s alignment of A and B, and where Y is the total number of amino acid residues in B. It will be appreciated that where the length of amino acid sequence A is not equal to the PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO length of amino acid sequence B, the % amino acid sequence identity of A to B will not equal the % amino acid sequence identity of B to A. Unless specifically stated otherwise, all % amino acid sequence identity values used herein are obtained as described in the immediately preceding paragraph using the ALIGN-2 computer program. The term “peptide linker” refers to a peptide comprising one or more amino acids, typically about 2 to 20 amino acids. Peptide linkers are known in the art or are described herein. Suitable, non- immunogenic linker peptides are, for example, (G4S)n, (SG4)n or G4(SG4)n peptide linkers, wherein “n” is generally a number between 1 and 10, typically between 2 and 4, in particular 2, i.e. the peptides selected from the group consisting of GGGGS (SEQ ID NO: 58) GGGGSGGGGS (SEQ ID NO: 59), SGGGGSGGGG (SEQ ID NO: 60) and GGGGSGGGGSGGGG (SEQ ID NO: 61), but also include the sequences GSPGSSSSGS (SEQ ID NO: 62), (G4S)3 (SEQ ID NO: 63), (G4S)4 (SEQ ID NO: 64), GSGSGSGS (SEQ ID NO: 65), GSGSGNGS (SEQ ID NO: 66), GGSGSGSG (SEQ ID NO: 67), GGSGSG (SEQ ID NO: 68), GGSG (SEQ ID NO: 69), GGSGNGSG (SEQ ID NO: 70), GGNGSGSG (SEQ ID NO: 71) and GGNGSG (SEQ ID NO: 72). Peptide linkers of particular interest are (G4S) (SEQ ID NO: 58), (G4S)2 or GGGGSGGGGS (SEQ ID NO: 59), (G4S)3 (SEQ ID NO: 63) and (G4S)4 (SEQ ID NO: 65), more particularly (G4S)2 or GGGGSGGGGS (SEQ ID NO: 59). By “fused to” or “connected to” is meant that the components (e.g., an antigen-binding domain and a Fc domain) are linked by peptide bonds, either directly or via one or more peptide linkers. III. THERAPEUTIC AND METHODS AND USES A. Therapeutic methods and uses comprising neoadjuvant therapy with a PD-1 axis binding antagonist, a VEGF antagonist, and an anti-TIGIT antagonist antibody Provided herein are methods of treating a subject (e.g., a human subject) having a hepatocellular carcinoma (HCC), e.g., a resectable HCC, comprising administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab) (e.g., administering one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab) as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, between one and three dosing cycles are completed prior to the surgery (e.g., one dosing cycle, two dosing cycles, or three dosing cycles are completed prior to the surgery). Alternatively, in some aspects, more than three dosing cycles (e.g., 4, 5, 6, 7, 8, 9, 10, or more than 10 dosing cycles) are completed prior to the surgery. In some aspects, the methods further comprise administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., comprise administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Also provided herein are methods of treating a subject having an HCC, e.g., a resectable HCC, comprising administering to the subject: (a) one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab) (e.g., one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab) as a neoadjuvant therapy prior to a surgery for the HCC (e.g., administering one, two, or three dosing cycles as PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO a neoadjuvant therapy); and (b) one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., one or more dosing cycles of atezolizumab and bevacizumab) as an adjuvant therapy after the surgery. Also provided herein are a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and/or an anti-TIGIT antagonist antibody (e.g., tiragolumab) for use in any of the methods provided herein. For example, in one aspect, the invention provides a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and/or an anti-TIGIT antagonist antibody (e.g., tiragolumab) for use in a method of treating a subject having a hepatocellular carcinoma (HCC), e.g., a resectable HCC, comprising administering to the subject one or more dosing cycles of a PD- 1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab) (e.g., administering one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab) as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, the invention further provides use of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery. Further provided herein are uses of a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and/or an anti-TIGIT antagonist antibody (e.g., tiragolumab) in the manufacture of a medicament for treating a patient according to any of the methods provided herein. Cancer type and previous treatment In some aspects, the HCC is a resectable HCC, e.g., is an HCC that is amenable to negative surgical margins (R0) surgical resection with curative intent. In some aspects, the subject does not have extrahepatic disease or extrahepatic spread (EHS) and/or does not have macroscopic vascular invasion (MVI). The subject may have been determined to have adequate liver function, e.g., as determined by assessment of bilirubin levels, albumin levels, prothrombin time, presence of ascites, and/or encephalopathy and/or as determined according to the Child-Pugh classification system (Child and Turcotte: Surgery and portal hypertension. In: Child CG, editor. The liver and portal hypertension. Philadelphia, Saunders, 50-64, 1964; Pugh et al., J Hepatol, 69: 182-236, 2018). For example, in some aspects, the subject has been determined to be Class A according to the Child-Pugh classification system. The subject may fall within the Milan criteria, or may be beyond the Milan criteria. A subject is defined as within the Milan criteria if (a) the subject has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) the subject has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm. A subject is defined as beyond the Milan criteria if (a) the subject has a single HCC tumor with a longest diameter of > 5 cm; (b) the subject has between two and three HCC tumor nodules, and at least two of the nodules have a longest diameter of >3 cm; or (c) the subject has four or more HCC tumor nodules. In some aspects, the subject is beyond the Milan criteria at baseline, and is downstaged to within the Milan criteria during or following the neoadjuvant treatment (e.g., is downstaged to within the Milan criteria before the surgery). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, the subject has received no prior systemic or locoregional treatment for HCC, e.g., is chemotherapy-naïve and/or is treatment-naïve. Surgery In some aspects, the surgery that follows the one or more neoadjuvant dosing cycles is a liver resection (e.g., surgical removal of a portion of the liver or all of the liver). In some aspects, the surgery is a negative surgical margins (R0) surgical resection, e.g., negative surgical margins are achieved by the surgery. R0 resection is defined as a microscopically margin-negative resection, in which no tumor (gross or microscopic) remains in the primary tumor bed. The surgery may have curative intent. In some aspects, the sugery is performed at least 28 days after the neoadjuvant dosing cycles (e.g., is performed at least 28 days after the last day of the one or more dosing cycles). Dosing and administration order for neoadjuvant therapy PD-1 axis binding antagonist In some aspects, in each of the one or more dosing cycles administered as a neoadjuvant therapy, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary PD-1 axis binding antagonists, and dosing regimens for the same, are provided in Section V, below. In some aspects, the PD-1 axis binding antagonist is atezolizumab, and the atezolizumab is administered at a fixed dose of about 1200 mg (e.g., a fixed dose of 1200 mg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered intravenously. In other aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered subcutaneously. VEGF antagonist In some aspects, in each of the one or more dosing cycles administered as a neoadjuvant therapy, the VEGF antagonist (e.g., bevacizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary VEGF antagonists are provided in Section VII, below. In some aspects, the VEGF antagonist is bevacizumab, and the bevacizumab is administered at a dose of about 15 mg/kg (e.g., a dose of 15 mg/kg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the VEGF antagonist (e.g., bevacizumab) is administered intravenously. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Anti-TIGIT antagonist antibody In some aspects, in each of the one or more dosing cycles administered as a neoadjuvant therapy, the anti-TIGIT antagonist antibody (e.g., tiragolumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary anti-TIGIT antagonist antibodies, and dosing regimens for the same, are provided in Section IV, below. In some aspects, the anti-TIGIT antagonist antibody is tiragolumab, and the tiragolumab is administered at a fixed dose of about 600 mg (e.g., a dose of 600 mg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the anti-TIGIT antagonist antibody (e.g., tiragolumab) is administered intravenously. In other aspects, the anti-TIGIT antagonist antibody (e.g., tiragolumab) is administered subcutaneously. Atezolizumab, bevacizumab, and tiragolumab Accordingly, in some aspects, provided herein are methods of treating a subject (e.g., a human subject) having an HCC (e.g., a resectable HCC) comprising administering to the subject one or more (e.g., one, two, or three) 21-day dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC, wherein each of atezolizumab, bevacizumab, and tiragolumab are administered intravenously on Day 1 of each 21-day cycle, and wherein the atezolizumab is administered at a fixed dose of 1200 mg; the bevacizumab is administered at a dose of 15 mg/kg; and the tiragolumab is administered at a fixed dose of 600 mg. Administration order In some aspects, the method comprises administering to the subject the PD-1 axis binding antagonist before the VEGF antagonist (e.g., atezolizumab before bevacizumab). In some aspects, the method comprises administering to the subject the VEGF antagonist before the anti-TIGIT antagonist antibody (e.g., bevacizumab before tiragolumab). Thus, in some aspects, the method comprises administering to the subject the PD-1 axis binding antagonist first, the VEGF antagonist second, and the anti-TIGIT antagonist antibody third (e.g., comprises administering atezolizumab first, bevacizumab second, and tiragolumab third). Alternatively, the method may comprise administering PD-1 axis binding antagonist first, the anti-TIGIT antagonist antibody second, and the VEGF antagonist third; administering the VEGF antagonist first, the PD-1 axis binding antagonist second, and the anti-TIGIT antagonist antibody third; administering the VEGF antagonist first, the anti-TIGIT antagonist antibody second, and the PD-1 axis binding antagonist third; administering the anti-TIGIT antagonist antibody first, the PD-1 axis binding antagonist second, and the VEGF antagonist third; or administering the VEGF antagonist first, the the anti-TIGIT antagonist antibody second, and the PD-1 axis binding antagonist third. In some aspects in which the PD-1 axis binding antagonist is administered before the VEGF antagonist (e.g., atezolizumab is administered before bevacizumab), the VEGF antagonist is administered at least 5 minutes after completion of the PD-1 axis binding antagonist administration. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects in which the VEGF antagonist is administered before the anti-TIGIT antagonist antibody (e.g., bevacizumab is administered before tiragolumab), the anti-TIGIT antagonist antibody is administered at least 60 minutes after completion of the VEGF antagonist administration. In some aspects, the anti-TIGIT antagonist antibody is administered at least 60 minutes after completion of the VEGF antagonist administration in a first administration (e.g., first dosing cycle), and is administered at least 30 minutes after completion of the VEGF antagonist administration in a second or subsequent administration (e.g., second or subsequent dosing cycle) (e.g., if the VEGF antagonist administration was given without premedication and tolerated without an infusion-related reaction (IRR)).

Alternatively, in some aspects, the method comprises co-administering the PD-1 axis binding antagonist and the anti-TIGIT antagonist antibody (e.g., comprises co-administering tiragolumab and atezolizumab). For example, in some aspects, the method comprises IV co-infusion of tiragolumab and atezolizumab. In some aspects, the co-infused tiragolumab and atezolizumab are mixed prior to infusion (e.g., are formulated separately and are mixed by the physician administering the drugs), e.g., are combined in an IV bag prior to administration. In other aspects, the co-infused tiragolumab and atezolizumab are formulated together (i.e., are not mixed by the physician administering the drugs) and are administered as an IV-administered fixed dose combination (FDC). In some aspects, the IV- administered co-infusion of tiragolumab and atezolizumab (e.g., FDC) comprises atezolizumab at a dose of 1200 mg and tiragolumab at a dose of 600 mg. In some aspects, the method comprises SC co-infusion of tiragolumab and atezolizumab. In some aspects, the co-infused tiragolumab and atezolizumab are mixed prior to infusion (e.g., are formulated separately and are mixed by the physician administering the drugs). In other aspects, the co- infused tiragolumab and atezolizumab are formulated together (i.e., are not mixed by the physician administering the drugs) and are administered as an SC-administered FDC. In some aspects, the SC- administered co-infusion of tiragolumab and atezolizumab (e.g., FDC) comprises atezolizumab at a dose of 1875 mg or 2000 mg and tiragolumab at a dose of 880 mg. In other aspects, the SC-administered co- infusion of tiragolumab and atezolizumab (e.g., FDC) comprises atezolizumab at a dose of 1875 mg or 2000 mg and tiragolumab at a dose of 1000 mg. In some aspects, the method comprises both IV and SC administration of tiragolumab and/or atezolizumab, e.g., comprises one or more IV-administered doses and one or more SC-administered doses of tiragolumab and/or atezolizumab. For example, in some aspects, the method comprises administering at least one dose of tiragolumab and atezolizumab as an IV-administered FDC and comprises administering at least one dose of tiragolumab and atezolizumab as an SC-administered FDC. Exemplary IV and SC FDC doses and formulations of tiragolumab and atezolizumab are provided in PCT/US2022/082139 and in U.S. Provisional Patent Application Nos.63/493,691 (filed March 31, 2023) and 63/494,983 (filed April 7, 2023) (both titled “Methods of Treating Tumors with Anti-TIGIT Antibodies”), each of which is incorporated herein by reference in its entirety. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Adjuvant dosing cycles In some aspects, the methods provided herein further comprise administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., comprise administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). For example, in some aspects, between 1 and 17 dosing cycles (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, or 17 cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy after the surgery. In one aspect, 17 cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy after the surgery. In some aspects, dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy for up to 12 months after the surgery Dosing and administration order for adjuvant therapy PD-1 axis binding antagonist In some aspects, in each of the one or more dosing cycles administered as an adjuvant therapy, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary PD-1 axis binding antagonists, and dosing regimens for the same, are provided in Section V, below. In some aspects, the PD-1 axis binding antagonist is atezolizumab, and the atezolizumab is administered at a fixed dose of about 1200 mg (e.g., a fixed dose of 1200 mg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered intravenously. In other aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered subcutaneously. VEGF antagonist In some aspects, in each of the one or more dosing cycles administered as an adjuvant therapy, the VEGF antagonist (e.g., bevacizumab) is administered every three weeks (e.g., is administered in 21- day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary VEGF antagonists are provided in Section VII, below. In some aspects, the VEGF antagonist is bevacizumab, and the bevacizumab is administered at a dose of about 15 mg/kg (e.g., a dose of 15 mg/kg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the VEGF antagonist (e.g., bevacizumab) is administered intravenously. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Administration order In some aspects, the method comprises administering to the subject the PD-1 axis binding antagonist before the VEGF antagonist (e.g., atezolizumab before bevacizumab). In other aspects, the method comprises administering to the subject the VEGF antagonist before the PD-1 axis binding antagonist (e.g., bevacizumab before atezolizumab). In some aspects in which the PD-1 axis binding antagonist is administered before the VEGF antagonist (e.g., atezolizumab is administered before bevacizumab), the VEGF antagonist is administered at least 5 minutes after completion of the PD-1 axis binding antagonist administration. Atezolizumab, bevacizumab, and tiragolumab Accordingly, in some aspects, provided herein are methods of treating a subject (e.g., a human subject) having an HCC (e.g., a resectable HCC) comprising administering to the subject (a) one or more (e.g., one, two, or three) 21-day dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC, wherein each of atezolizumab, bevacizumab, and tiragolumab are administered intravenously on Day 1 of each 21-day cycle, and wherein the atezolizumab is administered at a fixed dose of 1200 mg; the bevacizumab is administered at a dose of 15 mg/kg; and the tiragolumab is administered at a fixed dose of 600 mg; and (b) one or more 21-day dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery, wherein each of atezolizumab and bevacizumab are administered intravenously on Day 1 of each 21-day cycle, and wherein the atezolizumab is administered at a fixed dose of 1200 mg and the bevacizumab is administered at a dose of 15 mg/kg. Benefit from treatment Increased MPR rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the major pathologic response (MPR) rate as compared to a reference MPR rate. MPR rate may be defined, e.g., as the proportion of subjects in a population of subjects treated according to the method with an MPR of less than or equal to 10% (residual viable tumor in the tumor bed). In some aspects, the reference MPR rate is an MPR rate in a population of subjects (e.g., is the mean or median MPR rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an MPR rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the MPR rate of a population of subjects treated according to the method compared to a reference MPR rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO or more than 100%, e.g., increases the MPR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%- 50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference MPR rate. In some aspects, the reference MPR rate is an MPR rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tiragolumab. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased pCR rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the pathologic complete response (pCR) rate as compared to a reference pCR rate. pCR rate may be defined as the proportion of subjects in a population of subjects treated according to the method who achieve a pCR, e.g., have an absence of residual tumor in a resected tumor specimen. In some aspects, the reference pCR rate is a pCR rate in a population of subjects (e.g., is the mean or median pCR rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in a pCR rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the pCR rate of a population of subjects treated according to the method compared to a reference pCR rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the pCR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference pCR rate. In some aspects, the reference pCR rate is a pCR rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tiragolumab. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased duration of EFS In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in event-free survival (EFS) as compared to a reference EFS. In some aspects, the reference EFS is an EFS in a population of subjects (e.g., is the mean or median EFS of a population of subjects) who have received a control treatment. In some embodiments, a treatment described herein extends the EFS of the subject compared to a reference EFS by at least about 2 months (e.g., by 2-120 months, by 2.5-100 months, by 3.0-80 months, by 4.0-60 months, by 5.0-48 months, by 6.0-36 months, by 8.0-24 months, or by 10-12 months, e.g., by at least about 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some embodiments, the treatment extends the EFS of the subject by at least about 4 months (e.g., by 4-120 months, by 5-100 months, by 6-80 months, by 7-60 months, by 8-48 months, by 9-36 months, or by 10-24 months, e.g., by at least about 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some embodiments, the treatment extends the EFS of the subject by at least about 2 months (e.g., by 2-120 months, by 3-100 months, by 4-80 months, by 6-60 months, by 8-48 months, by 9-36 months, or by 10-24 months, e.g., by at least about 2.0 months, 2.1 months, 2.2 months, 2.3 months, 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some aspects, the reference EFS is an EFS (e.g., a mean or median duration of EFS) in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tiragolumab. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased duration of OS In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in overall survival (OS) as compared to a reference OS. In some aspects, the reference OS is an OS in a population of subjects (e.g., is the mean or median OS of a population of subjects) who have received a control treatment. In some embodiments, OS is measured as the period of time from the start of treatment to death. In some instances, the treatment extends the OS of the subject by at least about 2 months as compared to a reference OS (e.g., by 2-120 months, by 3-110 months, by 4-100 months, by 5-80 months, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 2 months, 2.1 months, 2.2 months, 2.3 months, 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some instances, the treatment extends the OS of the subject by at least about 3.3 months (e.g., by 3.3-120 months, by 4-100 months, by 5-80 months, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some instances, the treatment extends the OS of the subject by at least about 5.3 months (e.g., by 5.3-120, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 5.3 months, 5.5 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in objective response rate (ORR) as compared to a reference ORR. In some aspects, the reference ORR is an ORR in a population of subjects (e.g., is the mean or median ORR of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an ORR of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the ORR of a population of subjects treated according to the method compared to a reference ORR by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the ORR by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%- 60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference ORR. In some aspects, the reference OS is an OS (e.g., a mean or median duration of OS) in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tiragolumab. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Downstaging to within Milan criteria In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the proportion of patients that are downstaged to within Milan criteria (e.g., are downstaged to within Milan criteria during or after PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO neoadjuvant therapy, and before a surgery) as compared to the proportion in a reference population. A patient who is downstaged to within Milan criteria may be one who is beyond the Milan criteria at baseline (e.g., (a) has a single HCC tumor with a longest diameter of > 5 cm; (b) has between two and three HCC tumor nodules, wherein at least two of the nodules have a longest diameter of >3 cm; or (c) has four or more HCC tumor nodules) and is within the Milan criteria during or following the neoadjuvant treatment (e.g., (a) has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm). In some aspects, the proportion in a reference population is the proportion of patients that are downstaged to within Milan criteria in a population of subjects who have received a control treatment. In some embodiments, the treatment results in a downstaging rate in the population of subjects that are initially beyond the Milan criteria of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases downstaging rate of a population of subjects that are initially beyond the Milan criteria treated according to the method compared to a reference downstaging rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the pCR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference downstaging rate. In some aspects, the reference downstaging rate is a downstaging rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tiragolumab. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased R0 resection rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the R0 resection rate as compared to a reference R0 resection rate. R0 resection rate may be defined as the proportion of patients for which an R0 resection (e.g., microscopically margin-negative resection, e.g., in which no tumor (gross or microscopic) remains in the primary tumor bed) is obtained. In some aspects, the reference R0 resection rate is an R0 resection rate in a population of subjects (e.g., is the mean or median R0 resection rate of a population of subjects) who have received a control treatment. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some embodiments, the treatment results in an R0 resection rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the R0 resection rate of a population of subjects treated according to the method compared to a reference R0 resection rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the R0 resection rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference R0 resection rate. In some aspects, the reference R0 resection rate is an R0 resection rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tiragolumab. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). B. Therapeutic methods and uses comprising neoadjuvant therapy with a PD-1 axis binding antagonist and a VEGF antagonist Provided herein are methods of treating a subject (e.g., a human subject) having a hepatocellular carcinoma (HCC), e.g., a resectable HCC, comprising administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, between one and three dosing cycles are completed prior to the surgery (e.g., one dosing cycle, two dosing cycles, or three dosing cycles are completed prior to the surgery). Alternatively, in some aspects, more than three dosing cycles (e.g., 4, 5, 6, 7, 8, 9, 10, or more than 10 dosing cycles) are completed prior to the surgery. In some aspects, the methods further comprise administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., comprise administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Also provided herein are methods of treating a subject having an HCC, e.g., a resectable HCC, comprising administering to the subject: (a) one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC (e.g., PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO administering one, two, or three dosing cycles as a neoadjuvant therapy); and (b) one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., one or more dosing cycles of atezolizumab and bevacizumab) as an adjuvant therapy after the surgery. Also provided herein are a PD-1 axis binding antagonist (e.g., atezolizumab) and/or a VEGF antagonist (e.g., bevacizumab) for use in any of the methods provided herein. For example, in one aspect, the invention provides a PD-1 axis binding antagonist (e.g., atezolizumab) and/or a VEGF antagonist (e.g., bevacizumab) for use in a method of treating a subject having a hepatocellular carcinoma (HCC), e.g., a resectable HCC, comprising administering to the subject one or more dosing cycles of a PD- 1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, the invention further provides use of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery. Further provided herein are uses of a PD-1 axis binding antagonist (e.g., atezolizumab) and/or a VEGF antagonist (e.g., bevacizumab) in the manufacture of a medicament for treating a patient according to any of the methods provided herein. Cancer type and previous treatment In some aspects, the HCC is a resectable HCC, e.g., is an HCC that is amenable to negative surgical margins (R0) surgical resection with curative intent. In some aspects, the subject does not have extrahepatic disease or extrahepatic spread (EHS) and/or does not have macroscopic vascular invasion (MVI). The subject may have been determined to have adequate liver function, e.g., as determined by assessment of bilirubin levels, albumin levels, prothrombin time, presence of ascites, and/or encephalopathy and/or as determined according to the Child-Pugh classification system (Child and Turcotte: Surgery and portal hypertension. In: Child CG, editor. The liver and portal hypertension. Philadelphia, Saunders, 50-64, 1964; Pugh et al., J Hepatol, 69: 182-236, 2018). For example, in some aspects, the subject has been determined to be Class A according to the Child-Pugh classification system. The subject may fall within the Milan criteria, or may be beyond the Milan criteria. A subject is defined as within the Milan criteria if (a) the subject has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) the subject has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm. A subject is defined as beyond the Milan criteria if (a) the subject has a single HCC tumor with a longest diameter of > 5 cm; (b) the subject has between two and three HCC tumor nodules, and at least two of the nodules have a longest diameter of >3 cm; or (c) the subject has four or more HCC tumor nodules. In some aspects, the subject is beyond the Milan criteria at baseline, and is downstaged to within the Milan criteria during or following the neoadjuvant treatment (e.g., is downstaged to within the Milan criteria before the surgery). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, the subject has received no prior systemic or locoregional treatment for HCC, e.g., is chemotherapy-naïve and/or is treatment-naïve. Surgery In some aspects, the surgery that follows the one or more neoadjuvant dosing cycles is a liver resection (e.g., surgical removal of a portion of the liver or all of the liver). In some aspects, the surgery is a negative surgical margins (R0) surgical resection, e.g., negative surgical margins are achieved by the surgery. R0 resection is defined as a microscopically margin-negative resection, in which no tumor (gross or microscopic) remains in the primary tumor bed. The surgery may have curative intent. In some aspects, the sugery is performed at least 28 days after the neoadjuvant dosing cycles (e.g., is performed at least 28 days after the last day of the one or more dosing cycles). Dosing and administration order for neoadjuvant therapy PD-1 axis binding antagonist In some aspects, in each of the one or more dosing cycles administered as a neoadjuvant therapy, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary PD-1 axis binding antagonists, and dosing regimens for the same, are provided in Section V, below. In some aspects, the PD-1 axis binding antagonist is atezolizumab, and the atezolizumab is administered at a fixed dose of about 1200 mg (e.g., a fixed dose of 1200 mg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered intravenously. In other aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered subcutaneously. VEGF antagonist In some aspects, in each of the one or more dosing cycles administered as a neoadjuvant therapy, the VEGF antagonist (e.g., bevacizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary VEGF antagonists are provided in Section VII, below. In some aspects, the VEGF antagonist is bevacizumab, and the bevacizumab is administered at a dose of about 15 mg/kg (e.g., a dose of 15 mg/kg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the VEGF antagonist (e.g., bevacizumab) is administered intravenously. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Atezolizumab and bevacizumab Accordingly, in some aspects, provided herein are methods of treating a subject (e.g., a human subject) having an HCC (e.g., a resectable HCC) comprising administering to the subject one or more (e.g., one, two, or three) 21-day dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC, wherein each of atezolizumab and bevacizumab are administered intravenously on Day 1 of each 21-day cycle, and wherein the atezolizumab is administered at a fixed dose of 1200 mg and the bevacizumab is administered at a dose of 15 mg/kg. Administration order In some aspects, the method comprises administering to the subject the PD-1 axis binding antagonist before the VEGF antagonist (e.g., atezolizumab before bevacizumab). In other aspects, the method comprises administering to the subject the VEGF antagonist before the PD-1 axis binding antagonist (e.g., bevacizumab before atezolizumab). In some aspects in which the PD-1 axis binding antagonist is administered before the VEGF antagonist (e.g., atezolizumab is administered before bevacizumab), the VEGF antagonist is administered at least 5 minutes after completion of the PD-1 axis binding antagonist administration. Adjuvant dosing cycles In some aspects, the methods provided herein further comprise administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., comprise administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). For example, in some aspects, between 1 and 17 dosing cycles (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, or 17 cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy after the surgery. In one aspect, 17 cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy after the surgery. In some aspects, dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy for up to 12 months after the surgery Dosing and administration order for adjuvant therapy PD-1 axis binding antagonist In some aspects, in each of the one or more dosing cycles administered as an adjuvant therapy, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary PD-1 axis binding antagonists, and dosing regimens for the same, are provided in Section V, below. In some aspects, the PD-1 axis binding antagonist is atezolizumab, and the atezolizumab is administered at a fixed dose of about 1200 mg (e.g., a fixed dose of 1200 mg) every three weeks. In some PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO aspects, the length of each of the one or more dosing cycles is 21 days, and the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered intravenously. In other aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered subcutaneously. VEGF antagonist In some aspects, in each of the one or more dosing cycles administered as an adjuvant therapy, the VEGF antagonist (e.g., bevacizumab) is administered every three weeks (e.g., is administered in 21- day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary VEGF antagonists are provided in Section VII, below. In some aspects, the VEGF antagonist is bevacizumab, and the bevacizumab is administered at a dose of about 15 mg/kg (e.g., a dose of 15 mg/kg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the VEGF antagonist (e.g., bevacizumab) is administered intravenously. . Administration order In some aspects, the method comprises administering to the subject the PD-1 axis binding antagonist before the VEGF antagonist (e.g., atezolizumab before bevacizumab). In other aspects, the method comprises administering to the subject the VEGF antagonist before the PD-1 axis binding antagonist (e.g., bevacizumab before atezolizumab). In some aspects in which the PD-1 axis binding antagonist is administered before the VEGF antagonist (e.g., atezolizumab is administered before bevacizumab), the VEGF antagonist is administered at least 5 minutes after completion of the PD-1 axis binding antagonist administration. Atezolizumab and bevacizumab Accordingly, in some aspects, provided herein are methods of treating a subject (e.g., a human subject) having an HCC (e.g., a resectable HCC) comprising administering to the subject (a) one or more (e.g., one, two, or three) 21-day dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC, wherein each of atezolizumab and bevacizumab are administered intravenously on Day 1 of each 21-day cycle, and wherein the atezolizumab is administered at a fixed dose of 1200 mg and the bevacizumab is administered at a dose of 15 mg/kg; and (b) one or more 21-day dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery, wherein each of atezolizumab and bevacizumab are administered intravenously on Day 1 of each 21-day cycle, and wherein the atezolizumab is administered at a fixed dose of 1200 mg and the bevacizumab is administered at a dose of 15 mg/kg. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Benefit from treatment Increased MPR rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the major pathologic response (MPR) rate as compared to a reference MPR rate. MPR rate may be defined, e.g., as the proportion of subjects in a population of subjects treated according to the method with an MPR of less than or equal to 10% (residual viable tumor in the tumor bed). In some aspects, the reference MPR rate is an MPR rate in a population of subjects (e.g., is the mean or median MPR rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an MPR rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the MPR rate of a population of subjects treated according to the method compared to a reference MPR rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the MPR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%- 50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference MPR rate. Increased pCR rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the pathologic complete response (pCR) rate as compared to a reference pCR rate. pCR rate may be defined as the proportion of subjects in a population of subjects treated according to the method who achieve a pCR, e.g., have an absence of residual tumor in a resected tumor specimen. In some aspects, the reference pCR rate is a pCR rate in a population of subjects (e.g., is the mean or median pCR rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in a pCR rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the pCR rate of a population of subjects treated according to the method compared to a reference pCR rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the pCR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference pCR rate. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Increased duration of EFS In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in event-free survival (EFS) as compared to a reference EFS. In some aspects, the reference EFS is an EFS in a population of subjects (e.g., is the mean or median EFS of a population of subjects) who have received a control treatment. In some embodiments, a treatment described herein extends the EFS of the subject compared to a reference EFS by at least about 2 months (e.g., by 2-120 months, by 2.5-100 months, by 3.0-80 months, by 4.0-60 months, by 5.0-48 months, by 6.0-36 months, by 8.0-24 months, or by 10-12 months, e.g., by at least about 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some embodiments, the treatment extends the EFS of the subject by at least about 4 months (e.g., by 4-120 months, by 5-100 months, by 6-80 months, by 7-60 months, by 8-48 months, by 9-36 months, or by 10-24 months, e.g., by at least about 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some embodiments, the treatment extends the EFS of the subject by at least about 2 months (e.g., by 2-120 months, by 3-100 months, by 4-80 months, by 6-60 months, by 8-48 months, by 9-36 months, or by 10-24 months, e.g., by at least about 2.0 months, 2.1 months, 2.2 months, 2.3 months, 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Increased duration of OS In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in overall survival (OS) as compared to a reference OS. In some aspects, the reference OS is an OS in a population of subjects (e.g., is the mean or median OS of a population of subjects) who have received a control treatment. In some embodiments, OS is measured as the period of time from the start of treatment to death. In some instances, the treatment extends the OS of the subject by at least about 2 months as compared to a reference OS (e.g., by 2-120 months, by 3-110 months, by 4-100 months, by 5-80 months, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 2 months, 2.1 months, 2.2 months, 2.3 months, 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some instances, the treatment extends the OS of the subject by at least about 3.3 months (e.g., by 3.3-120 months, by 4-100 months, by 5-80 months, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some instances, the treatment extends the OS of the subject by at least about 5.3 months (e.g., by 5.3-120, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 5.3 months, 5.5 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in objective response rate (ORR) as compared PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO to a reference ORR. In some aspects, the reference ORR is an ORR in a population of subjects (e.g., is the mean or median ORR of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an ORR of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the ORR of a population of subjects treated according to the method compared to a reference ORR by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the ORR by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%- 60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference ORR. Downstaging to within Milan criteria In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the proportion of patients that are downstaged to within Milan criteria (e.g., are downstaged to within Milan criteria during or after neoadjuvant therapy, and before a surgery) as compared to the proportion in a reference population. A patient who is downstaged to within Milan criteria may be one who is beyond the Milan criteria at baseline (e.g., (a) has a single HCC tumor with a longest diameter of > 5 cm; (b) has between two and three HCC tumor nodules, wherein at least two of the nodules have a longest diameter of >3 cm; or (c) has four or more HCC tumor nodules) and is within the Milan criteria during or following the neoadjuvant treatment (e.g., (a) has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm). In some aspects, the proportion in a reference population is the proportion of patients that are downstaged to within Milan criteria in a population of subjects who have received a control treatment. In some embodiments, the treatment results in a downstaging rate in the population of subjects that are initially beyond the Milan criteria of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases downstaging rate of a population of subjects that are initially beyond the Milan criteria treated according to the method compared to a reference downstaging rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the pCR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference downstaging rate. Increased R0 resection rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO adjuvant therapy as provided herein) results in an increase in the R0 resection rate as compared to a reference R0 resection rate. R0 resection rate may be defined as the proportion of patients for which an R0 resection (e.g., microscopically margin-negative resection, e.g., in which no tumor (gross or microscopic) remains in the primary tumor bed) is obtained. In some aspects, the reference R0 resection rate is an R0 resection rate in a population of subjects (e.g., is the mean or median R0 resection rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an R0 resection rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the R0 resection rate of a population of subjects treated according to the method compared to a reference R0 resection rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the R0 resection rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference R0 resection rate. C. Therapeutic methods and uses comprising neoadjuvant therapy with a VEGF antagonist and a bispecific antibody that binds to PD-1 and LAG3 Provided herein are methods of treating a subject (e.g., a human subject) having a hepatocellular carcinoma (HCC), e.g., a resectable HCC, comprising administering to the subject one or more dosing cycles of a VEGF antagonist (e.g., bevacizumab) and a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) (e.g., administering one or more dosing cycles of bevacizumab and tobemstomig) as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, between one and three dosing cycles are completed prior to the surgery (e.g., one dosing cycle, two dosing cycles, or three dosing cycles are completed prior to the surgery). Alternatively, in some aspects, more than three dosing cycles (e.g., 4, 5, 6, 7, 8, 9, 10, or more than 10 dosing cycles) are completed prior to the surgery. In some aspects, the methods further comprise administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., comprise administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Also provided herein are methods of treating a subject having an HCC, e.g., a resectable HCC, comprising administering to the subject: (a) one or more dosing cycles of a VEGF antagonist (e.g., bevacizumab) and a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) (e.g., one or more dosing cycles of bevacizumab and tobemstomig) as a neoadjuvant therapy prior to a surgery for the HCC (e.g., administering one, two, or three dosing cycles as a neoadjuvant therapy); and (b) one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO bevacizumab) (e.g., one or more dosing cycles of atezolizumab and bevacizumab) as an adjuvant therapy after the surgery. Also provided herein are a VEGF antagonist (e.g., bevacizumab) and/or a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) for use in any of the methods provided herein. For example, in one aspect, the invention provides a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) and/or a VEGF antagonist (e.g., bevacizumab) for use in a method of treating a subject having a hepatocellular carcinoma (HCC), e.g., a resectable HCC, comprising administering to the subject one or more dosing cycles of a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of tobemstomig and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC. In some aspects, the invention further provides use of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery. Further provided herein are uses of a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) and/or a VEGF antagonist (e.g., bevacizumab) in the manufacture of a medicament for treating a patient according to any of the methods provided herein. Cancer type and previous treatment In some aspects, the HCC is a resectable HCC, e.g., is an HCC that is amenable to negative surgical margins (R0) surgical resection with curative intent. In some aspects, the subject does not have extrahepatic disease or extrahepatic spread (EHS) and/or does not have macroscopic vascular invasion (MVI). The subject may have been determined to have adequate liver function, e.g., as determined by assessment of bilirubin levels, albumin levels, prothrombin time, presence of ascites, and/or encephalopathy and/or as determined according to the Child-Pugh classification system (Child and Turcotte: Surgery and portal hypertension. In: Child CG, editor. The liver and portal hypertension. Philadelphia, Saunders, 50-64, 1964; Pugh et al., J Hepatol, 69: 182-236, 2018). For example, in some aspects, the subject has been determined to be Class A according to the Child-Pugh classification system. The subject may fall within the Milan criteria, or may be beyond the Milan criteria. A subject is defined as within the Milan criteria if (a) the subject has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) the subject has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm. A subject is defined as beyond the Milan criteria if (a) the subject has a single HCC tumor with a longest diameter of > 5 cm; (b) the subject has between two and three HCC tumor nodules, and at least two of the nodules have a longest diameter of >3 cm; or (c) the subject has four or more HCC tumor nodules. In some aspects, the subject is beyond the Milan criteria at baseline, and is downstaged to within the Milan criteria during or following the neoadjuvant treatment (e.g., is downstaged to within the Milan criteria before the surgery). In some aspects, the subject has received no prior systemic or locoregional treatment for HCC, e.g., is chemotherapy-naïve and/or is treatment-naïve. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Surgery In some aspects, the surgery that follows the one or more neoadjuvant dosing cycles is a liver resection (e.g., surgical removal of a portion of the liver or all of the liver). In some aspects, the surgery is a negative surgical margins (R0) surgical resection, e.g., negative surgical margins are achieved by the surgery. R0 resection is defined as a microscopically margin-negative resection, in which no tumor (gross or microscopic) remains in the primary tumor bed. The surgery may have curative intent. In some aspects, the sugery is performed at least 28 days after the neoadjuvant dosing cycles (e.g., is performed at least 28 days after the last day of the one or more dosing cycles). Dosing and administration order for neoadjuvant therapy Bispecific antibody that binds to PD-1 and LAG3 In some aspects, in each of the one or more dosing cycles administered as a neoadjuvant therapy, the bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary bispecific antibodies that bind to PD-1 and LAG3, and dosing regimens for the same, are provided in Section VI, below. In some aspects, the bispecific antibody that binds to PD-1 and LAG3 is tobemstomig, and the tobemstomig is administered at a fixed dose of about 600 mg (e.g., a fixed dose of 600 mg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the tobemstomig is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) is administered intravenously. VEGF antagonist In some aspects, in each of the one or more dosing cycles administered as a neoadjuvant therapy, the VEGF antagonist (e.g., bevacizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary VEGF antagonists are provided in Section VII, below. In some aspects, the VEGF antagonist is bevacizumab, and the bevacizumab is administered at a dose of about 15 mg/kg (e.g., a dose of 15 mg/kg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the VEGF antagonist (e.g., bevacizumab) is administered intravenously. Tobemstomig and bevacizumab Accordingly, in some aspects, provided herein are methods of treating a subject (e.g., a human subject) having an HCC (e.g., a resectable HCC) comprising administering to the subject one or more (e.g., one, two, or three) 21-day dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC, wherein each of tobemstomig and bevacizumab are administered intravenously PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO on Day 1 of each 21-day cycle, and wherein the tobemstomig is administered at a fixed dose of 600 mg and the bevacizumab is administered at a dose of 15 mg/kg. Administration order In some aspects, the method comprises administering to the subject the bispecific antibody that binds to PD-1 and LAG3 before the VEGF antagonist (e.g., tobemstomig before bevacizumab). In other aspects, the method comprises administering to the subject the VEGF antagonist before the bispecific antibody that binds to PD-1 and LAG3 (e.g., bevacizumab before tobemstomig). In some aspects in which the bispecific antibody that binds to PD-1 and LAG3 is administered before the VEGF antagonist (e.g., tobemstomig is administered before bevacizumab), the VEGF antagonist is administered at least 90 minutes after completion of the administration of the bispecific antibody that binds to PD-1 and LAG3. In some aspects, the VEGF antagonist is administered at least 90 minutes after completion of the administration of the bispecific antibody that binds to PD-1 and LAG3 in a first administration (e.g., first dosing cycle); is administered at least 60 minutes after completion of the administration of the bispecific antibody that binds to PD-1 and LAG3 in a second administration (e.g., second dosing cycle) if the first infusion was tolerated without an IRR; and/or is administered at least 30 minutes after completion of the administration of the bispecific antibody that binds to PD-1 and LAG3 in a third or further administration (e.g., third or further dosing cycle) if the first and second infusions were tolerated without an IRR. Adjuvant dosing cycles In some aspects, the methods provided herein further comprise administering to the subject one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., comprise administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). For example, in some aspects, between 1 and 17 dosing cycles (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, or 17 cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy after the surgery. In one aspect, 17 cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy after the surgery. In some aspects, dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) are administered to the subject as an adjuvant therapy for up to 12 months after the surgery Dosing and administration order for adjuvant therapy PD-1 axis binding antagonist In some aspects, in each of the one or more dosing cycles administered as an adjuvant therapy, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered every three weeks (e.g., is administered in 21-day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO cycles). Exemplary PD-1 axis binding antagonists, and dosing regimens for the same, are provided in Section V, below. In some aspects, the PD-1 axis binding antagonist is atezolizumab, and the atezolizumab is administered at a fixed dose of about 1200 mg (e.g., a fixed dose of 1200 mg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered intravenously. In other aspects, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered subcutaneously. VEGF antagonist In some aspects, in each of the one or more dosing cycles administered as an adjuvant therapy, the VEGF antagonist (e.g., bevacizumab) is administered every three weeks (e.g., is administered in 21- day dosing cycles, e.g., is administered on Day 1 of each of one or more dosing cycles). Exemplary VEGF antagonists are provided in Section VII, below. In some aspects, the VEGF antagonist is bevacizumab, and the bevacizumab is administered at a dose of about 15 mg/kg (e.g., a dose of 15 mg/kg) every three weeks. In some aspects, the length of each of the one or more dosing cycles is 21 days, and the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. In some aspects, the VEGF antagonist (e.g., bevacizumab) is administered intravenously. Administration order In some aspects, the method comprises administering to the subject the PD-1 axis binding antagonist before the VEGF antagonist (e.g., atezolizumab before bevacizumab). In other aspects, the method comprises administering to the subject the VEGF antagonist before the PD-1 axis binding antagonist (e.g., bevacizumab before atezolizumab). In some aspects in which the PD-1 axis binding antagonist is administered before the VEGF antagonist (e.g., atezolizumab is administered before bevacizumab), the VEGF antagonist is administered at least 5 minutes after completion of the PD-1 axis binding antagonist administration. Atezolizumab and bevacizumab Accordingly, in some aspects, provided herein are methods of treating a subject (e.g., a human subject) having an HCC (e.g., a resectable HCC) comprising administering to the subject (a) one or more (e.g., one, two, or three) 21-day dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC, wherein each of tobemstomig and bevacizumab are administered intravenously on Day 1 of each 21-day cycle, and wherein the tobemstomig is administered at a fixed dose of 1200 mg and the bevacizumab is administered at a dose of 15 mg/kg; and (b) one or more 21-day dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery, wherein each of atezolizumab and bevacizumab are administered intravenously on Day 1 of each 21-day cycle, and PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO wherein the atezolizumab is administered at a fixed dose of 1200 mg and the bevacizumab is administered at a dose of 15 mg/kg. Benefit from treatment Increased MPR rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the major pathologic response (MPR) rate as compared to a reference MPR rate. MPR rate may be defined, e.g., as the proportion of subjects in a population of subjects treated according to the method with an MPR of less than or equal to 10% (residual viable tumor in the tumor bed). In some aspects, the reference MPR rate is an MPR rate in a population of subjects (e.g., is the mean or median MPR rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an MPR rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the MPR rate of a population of subjects treated according to the method compared to a reference MPR rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the MPR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%- 50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference MPR rate. In some aspects, the reference MPR rate is an MPR rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tobemstomig. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased pCR rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the pathologic complete response (pCR) rate as compared to a reference pCR rate. pCR rate may be defined as the proportion of subjects in a population of subjects treated according to the method who achieve a pCR, e.g., have an absence of residual tumor in a resected tumor specimen. In some aspects, the reference pCR rate is a pCR rate in a PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO population of subjects (e.g., is the mean or median pCR rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in a pCR rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the pCR rate of a population of subjects treated according to the method compared to a reference pCR rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the pCR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference pCR rate. In some aspects, the reference pCR rate is a pCR rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tobemstomig. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased duration of EFS In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in event-free survival (EFS) as compared to a reference EFS. In some aspects, the reference EFS is an EFS in a population of subjects (e.g., is the mean or median EFS of a population of subjects) who have received a control treatment. In some embodiments, a treatment described herein extends the EFS of the subject compared to a reference EFS by at least about 2 months (e.g., by 2-120 months, by 2.5-100 months, by 3.0-80 months, by 4.0-60 months, by 5.0-48 months, by 6.0-36 months, by 8.0-24 months, or by 10-12 months, e.g., by at least about 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO months). In some embodiments, the treatment extends the EFS of the subject by at least about 4 months (e.g., by 4-120 months, by 5-100 months, by 6-80 months, by 7-60 months, by 8-48 months, by 9-36 months, or by 10-24 months, e.g., by at least about 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some embodiments, the treatment extends the EFS of the subject by at least about 2 months (e.g., by 2-120 months, by 3-100 months, by 4-80 months, by 6-60 months, by 8-48 months, by 9-36 months, or by 10-24 months, e.g., by at least about 2.0 months, 2.1 months, 2.2 months, 2.3 months, 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some aspects, the reference EFS is an EFS (e.g., a mean or median duration of EFS) in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tobemstomig. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased duration of OS In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in overall survival (OS) as compared to a reference OS. In some aspects, the reference OS is an OS in a population of subjects (e.g., is the mean or median OS of a population of subjects) who have received a control treatment. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some embodiments, OS is measured as the period of time from the start of treatment to death. In some instances, the treatment extends the OS of the subject by at least about 2 months as compared to a reference OS (e.g., by 2-120 months, by 3-110 months, by 4-100 months, by 5-80 months, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 2 months, 2.1 months, 2.2 months, 2.3 months, 2.4 months, 2.5 months, 2.6 months, 2.7 months, 2.8 months, 2.9 months, 3.0 months, 3.1 months, 3.2 months, 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some instances, the treatment extends the OS of the subject by at least about 3.3 months (e.g., by 3.3-120 months, by 4-100 months, by 5-80 months, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 3.3 months, 3.4 months, 3.5 months, 3.6 months, 3.7 months, 3.8 months, 3.9 months, 4.0 months, 4.1 months, 4.2 months, 4.3 months, 4.4 months, 4.5 months, 4.6 months, 4.7 months, 4.8 months, 4.9 months, 5.0 months, 5.1 months, 5.2 months, 5.3 months, 5.4 months, 5.5 months, 5.6 months, 5.7 months, 5.8 months, 5.9 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some instances, the treatment extends the OS of the subject by at least about 5.3 months (e.g., by 5.3-120, by 6-60 months, by 7-48 months, by 8-36 months, or by 10-24 months, e.g., by at least about 5.3 months, 5.5 months, 6.0 months, 6.5 months, 7.0 months, 7.5 months, 8.0 months, 8.5 months, 9.0 months, 9.5 months, 10 months, 10.5 months, 11 months, 11.5 months, 12 months, 13 months, 14 months, 15 months, 16 months, 17 months, 18 months, 19 months, 20 months, 21 months, 22 months, 23 months, 24 months, 25 months, 26 months, 27 months, 28 months, 29 months, 30 months, 31 months, 32 months, 33 months, 34 months, 35 months, or 36 months). In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in objective response rate (ORR) as compared to a reference ORR. In some aspects, the reference ORR is an ORR in a population of subjects (e.g., is the mean or median ORR of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an ORR of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some embodiments, a treatment described herein increases the ORR of a population of subjects treated according to the method compared to a reference ORR by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the ORR by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%- 60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference ORR. In some aspects, the reference OS is an OS (e.g., a mean or median duration of OS) in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tobemstomig. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Downstaging to within Milan criteria In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the proportion of patients that are downstaged to within Milan criteria (e.g., are downstaged to within Milan criteria during or after neoadjuvant therapy, and before a surgery) as compared to the proportion in a reference population. A patient who is downstaged to within Milan criteria may be one who is beyond the Milan criteria at baseline (e.g., (a) has a single HCC tumor with a longest diameter of > 5 cm; (b) has between two and three HCC tumor nodules, wherein at least two of the nodules have a longest diameter of >3 cm; or (c) has four or more HCC tumor nodules) and is within the Milan criteria during or following the neoadjuvant treatment (e.g., (a) has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm). In some aspects, the proportion in a reference population is the proportion of patients that are downstaged to within Milan criteria in a population of subjects who have received a control treatment. In some embodiments, the treatment results in a downstaging rate in the population of subjects that are initially beyond the Milan criteria of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases downstaging rate of a population of subjects that are initially beyond the Milan criteria treated according to the method compared to a reference downstaging rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the pCR rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference downstaging rate. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some aspects, the reference downstaging rate is a downstaging rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tobemstomig. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). Increased R0 resection rate In some aspects, treating a subject according to any one of the methods provided herein (e.g., treating with a neoadjuvant therapy as provided herein or treating with a neoadjuvant therapy and an adjuvant therapy as provided herein) results in an increase in the R0 resection rate as compared to a reference R0 resection rate. R0 resection rate may be defined as the proportion of patients for which an R0 resection (e.g., microscopically margin-negative resection, e.g., in which no tumor (gross or microscopic) remains in the primary tumor bed) is obtained. In some aspects, the reference R0 resection rate is an R0 resection rate in a population of subjects (e.g., is the mean or median R0 resection rate of a population of subjects) who have received a control treatment. In some embodiments, the treatment results in an R0 resection rate of the population of subjects of at least about 50% (e.g., about 50% to about 100% (e.g., about 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%)). In some embodiments, a treatment described herein increases the R0 resection rate of a population of subjects treated according to the method compared to a reference R0 resection rate by at least about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 85%, 100%, or more than 100%, e.g., increases the R0 resection rate by 5%-10%, 10%-20%, 20%-30%, 30%-40%, 40%-50%, 50%-60%, 60%-70%, 70%-80%, 80%-90%, or 90%-100% relative to a reference R0 resection rate. In some aspects, the reference R0 resection rate is an R0 resection rate in a population of subjects having an HCC, e.g., a resectable HCC, who have been treated according to a method comprising administering to each subject one or more dosing cycles (e.g., 1-3 dosing cycles) of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) (e.g., administering one or more dosing cycles of atezolizumab and bevacizumab) as a neoadjuvant therapy prior to a surgery for the HCC, wherein the treatment does not comprise administration of tobemstomig. In some aspects, the subjects in the reference population have further been administered one or more dosing cycles of a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab) as an adjuvant therapy after the surgery (e.g., one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO IV. ANTI-TIGIT ANTAGONIST ANTIBODIES The invention provides anti-TIGIT antagonist antibodies useful for treating cancer in a subject (e.g., a human) having a cancer (e.g., a hepatocellular carcinoma (HCC), e.g., a resectable HCC). In some instances, the anti-TIGIT antagonist antibody is tiragolumab (CAS Registry Number: 1918185-84-8). Tiragolumab (Genentech) is also known as MTIG7192A. In certain instances, the anti-TIGIT antagonist antibody includes at least one, two, three, four, five, or six HVRs selected from: (a) an HVR-H1 comprising the amino acid sequence of SNSAAWN (SEQ ID NO: 11); (b) an HVR-H2 comprising the amino acid sequence of KTYYRFKWYSDYAVSVKG (SEQ ID NO: 12); (c) an HVR-H3 comprising the amino acid sequence of ESTTYDLLAGPFDY (SEQ ID NO: 13); (d) an HVR-L1 comprising the amino acid sequence of KSSQTVLYSSNNKKYLA (SEQ ID NO: 14), (e) an HVR-L2 comprising the amino acid sequence of WASTRES (SEQ ID NO: 15); and/or (f) an HVR-L3 comprising the amino acid sequence of QQYYSTPFT (SEQ ID NO: 16), or a combination of one or more of the above HVRs and one or more variants thereof having at least about 90% sequence identity (e.g., 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity) to any one of SEQ ID NOs: 11-16. In some instances, anti-TIGIT antagonist antibodies may include (a) an HVR-H1 comprising the amino acid sequence of SNSAAWN (SEQ ID NO: 11); (b) an HVR-H2 comprising the amino acid sequence of KTYYRFKWYSDYAVSVKG (SEQ ID NO: 12); (c) an HVR-H3 comprising the amino acid sequence of ESTTYDLLAGPFDY (SEQ ID NO: 13); (d) an HVR-L1 comprising the amino acid sequence of KSSQTVLYSSNNKKYLA (SEQ ID NO: 14); (e) an HVR-L2 comprising the amino acid sequence of WASTRES (SEQ ID NO: 15); and (f) an HVR-L3 comprising the amino acid sequence of QQYYSTPFT (SEQ ID NO: 16). In some instances, the anti-TIGIT antagonist antibody has a VH domain comprising an amino acid sequence having at least 90% sequence identity (e.g., at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of, EVQLQQSGPGLVKPSQTLSLTCAISGDSVSSNSAAWNWIRQSPSRGLEWLGKTYYRFKWYSDYAVSVK GRITINPDTSKNQFSLQLNSVTPEDTAVFYCTRESTTYDLLAGPFDYWGQGTLVTVSS (SEQ ID NO: 27) or an amino acid sequence having at least 90% sequence identity (e.g., at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of, QVQLQQSGPGLVKPSQTLSLTCAISGDSVSSNSAAWNWIRQSPSRGLEWLGKTYYRFKWYSDYAVSVK GRITINPDTSKNQFSLQLNSVTPEDTAVFYCTRESTTYDLLAGPFDYWGQGTLVTVSS (SEQ ID NO: 28); and/or a VL domain comprising an amino acid sequence having at least 90% sequence identity (e.g., at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of, DIVMTQSPDSLAVSLGERATINCKSSQTVLYSSNNKKYLAWYQQKPGQPPNLLIYWASTRESGVPDRFSG SGSGTDFTLTISSLQAEDVAVYYCQQYYSTPFTFGPGTKVEIK (SEQ ID NO: 29). In some instances, the anti-TIGIT antagonist antibody has a VH domain comprising an amino acid sequence having at least 90% sequence identity (e.g., at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of, SEQ ID NO: 27 and/or a VL domain comprising an amino acid sequence having at least 90% sequence identity (e.g., at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of, SEQ ID NO: 29. In some instances, the anti-TIGIT antagonist antibody has a VH domain comprising the amino acid sequence of SEQ ID NO: 27 and a VL domain PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO comprising the amino acid sequence of SEQ ID NO: 29. In some instances, the anti-TIGIT antagonist antibody has a VH domain comprising an amino acid sequence having at least 90% sequence identity (e.g., at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of, SEQ ID NO: 28 and/or a VL domain comprising an amino acid sequence having at least 90% sequence identity (e.g., at least 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of, SEQ ID NO: 29. In some instances, the anti-TIGIT antagonist antibody has a VH domain comprising the amino acid sequence of SEQ ID NO: 28 and a VL domain comprising the amino acid sequence of SEQ ID NO: 29. In some instances, the anti-TIGIT antagonist antibody includes a heavy chain and a light chain sequence, wherein: (a) the heavy chain comprises the amino acid sequence: EVQLQQSGPGLVKPSQTLSLTCAISGDSVSSNSAAWNWIRQSPSRGLEWLGKTYYRFKWYSDYAVSVK GRITINPDTSKNQFSLQLNSVTPEDTAVFYCTRESTTYDLLAGPFDYWGQGTLVTVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC NVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHED PEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAK GQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSK LTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK (SEQ ID NO: 33); and (b) the light chain comprises the amino acid sequence: DIVMTQSPDSLAVSLGERATINCKSSQTVLYSSNNKKYLAWYQQKPGQPPNLLIYWASTRESGVPDRFSG SGSGTDFTLTISSLQAEDVAVYYCQQYYSTPFTFGPGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLL NNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPV TKSFNRGEC (SEQ ID NO: 34). In some instances, the anti-TIGIT antagonist antibody further comprises at least one, two, three, or four of the following light chain variable region framework regions (FRs): an FR-L1 comprising the amino acid sequence of DIVMTQSPDSLAVSLGERATINC (SEQ ID NO: 17); an FR-L2 comprising the amino acid sequence of WYQQKPGQPPNLLIY (SEQ ID NO: 18); an FR-L3 comprising the amino acid sequence of GVPDRFSGSGSGTDFTLTISSLQAEDVAVYYC (SEQ ID NO: 19); and/or an FR-L4 comprising the amino acid sequence of FGPGTKVEIK (SEQ ID NO: 20), or a combination of one or more of the above FRs and one or more variants thereof having at least about 90% sequence identity (e.g., 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity) to any one of SEQ ID NOs: 17-20. In some instances, for example, the antibody further comprises an FR-L1 comprising the amino acid sequence of DIVMTQSPDSLAVSLGERATINC (SEQ ID NO: 17); an FR-L2 comprising the amino acid sequence of WYQQKPGQPPNLLIY (SEQ ID NO: 18); an FR-L3 comprising the amino acid sequence of GVPDRFSGSGSGTDFTLTISSLQAEDVAVYYC (SEQ ID NO: 19); and an FR-L4 comprising the amino acid sequence of FGPGTKVEIK (SEQ ID NO: 20). In some instances, the anti-TIGIT antagonist antibody further comprises at least one, two, three, or four of the following heavy chain variable region FRs: an FR-H1 comprising the amino acid sequence of X1VQLQQSGPGLVKPSQTLSLTCAISGDSVS (SEQ ID NO: 21), wherein X1 is E or Q; an FR-H2 comprising the amino acid sequence of WIRQSPSRGLEWLG (SEQ ID NO: 22); an FR-H3 comprising the amino acid sequence of RITINPDTSKNQFSLQLNSVTPEDTAVFYCTR (SEQ ID NO: 23); and/or an FR- PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO H4 comprising the amino acid sequence of WGQGTLVTVSS (SEQ ID NO: 24), or a combination of one or more of the above FRs and one or more variants thereof having at least about 90% sequence identity (e.g., 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity) to any one of SEQ ID NOs: 21- 24. The anti-TIGIT antagonist antibody may further include, for example, at least one, two, three, or four of the following heavy chain variable region FRs: an FR-H1 comprising the amino acid sequence of EVQLQQSGPGLVKPSQTLSLTCAISGDSVS (SEQ ID NO: 25); an FR-H2 comprising the amino acid sequence of WIRQSPSRGLEWLG (SEQ ID NO: 22); an FR-H3 comprising the amino acid sequence of RITINPDTSKNQFSLQLNSVTPEDTAVFYCTR (SEQ ID NO: 23); and/or an FR-H4 comprising the amino acid sequence of WGQGTLVTVSS (SEQ ID NO: 24), or a combination of one or more of the above FRs and one or more variants thereof having at least about 90% sequence identity (e.g., 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity) to any one of SEQ ID NOs: 22-25. In some instances, the anti-TIGIT antagonist antibody includes an FR-H1 comprising the amino acid sequence of EVQLQQSGPGLVKPSQTLSLTCAISGDSVS (SEQ ID NO: 25); an FR-H2 comprising the amino acid sequence of WIRQSPSRGLEWLG (SEQ ID NO: 22); an FR-H3 comprising the amino acid sequence of RITINPDTSKNQFSLQLNSVTPEDTAVFYCTR (SEQ ID NO: 23); and an FR-H4 comprising the amino acid sequence of WGQGTLVTVSS (SEQ ID NO: 24). In another instance, for example, the anti-TIGIT antagonist antibody may further include at least one, two, three, or four of the following heavy chain variable region FRs: an FR-H1 comprising the amino acid sequence of QVQLQQSGPGLVKPSQTLSLTCAISGDSVS (SEQ ID NO: 26); an FR-H2 comprising the amino acid sequence of WIRQSPSRGLEWLG (SEQ ID NO: 22); an FR-H3 comprising the amino acid sequence of RITINPDTSKNQFSLQLNSVTPEDTAVFYCTR (SEQ ID NO: 23); and/or an FR-H4 comprising the amino acid sequence of WGQGTLVTVSS (SEQ ID NO: 24), or a combination of one or more of the above FRs and one or more variants thereof having at least about 90% sequence identity (e.g., 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity) to any one of SEQ ID NOs: 22-24 and 26. In some instances, the anti-TIGIT antagonist antibody includes an FR-H1 comprising the amino acid sequence of QVQLQQSGPGLVKPSQTLSLTCAISGDSVS (SEQ ID NO: 26); an FR-H2 comprising the amino acid sequence of WIRQSPSRGLEWLG (SEQ ID NO: 22); an FR-H3 comprising the amino acid sequence of RITINPDTSKNQFSLQLNSVTPEDTAVFYCTR (SEQ ID NO: 23); and an FR-H4 comprising the amino acid sequence of WGQGTLVTVSS (SEQ ID NO: 24). In another aspect, an anti-TIGIT antagonist antibody is provided, wherein the antibody comprises a VH as in any of the instances provided above, and a VL as in any of the instances provided above, wherein one or both of the variable domain sequences include post-translational modifications. In some instances, any one of the anti-TIGIT antagonist antibodies described above is capable of binding to rabbit TIGIT, in addition to human TIGIT. In some instances, any one of the anti-TIGIT antagonist antibodies described above is capable of binding to both human TIGIT and cynomolgus monkey (cyno) TIGIT. In some instances, any one of the anti-TIGIT antagonist antibodies described above is capable of binding to human TIGIT, cyno TIGIT, and rabbit TIGIT. In some instances, any one of the anti-TIGIT antagonist antibodies described above is capable of binding to human TIGIT, cyno TIGIT, and rabbit TIGIT, but not murine TIGIT. In some instances, the anti-TIGIT antagonist antibody binds human TIGIT with a KD of about 10 PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO nM or lower and cyno TIGIT with a KD of about 10 nM or lower (e.g., binds human TIGIT with a KD of about 0.1 nM to about 1 nM and cyno TIGIT with a KD of about 0.5 nM to about 1 nM, e.g., binds human TIGIT with a KD of about 0.1 nM or lower and cyno TIGIT with a KD of about 0.5 nM or lower). In some instances, the anti-TIGIT antagonist antibody specifically binds TIGIT and inhibits or blocks TIGIT interaction with poliovirus receptor (PVR) (e.g., the antagonist antibody inhibits intracellular signaling mediated by TIGIT binding to PVR). In some instances, the antagonist antibody inhibits or blocks binding of human TIGIT to human PVR with an IC50 value of 10 nM or lower (e.g., 1 nM to about 10 nM). In some instances, the anti-TIGIT antagonist antibody specifically binds TIGIT and inhibits or blocks TIGIT interaction with PVR, without impacting PVR-CD226 interaction. In some instances, the antagonist antibody inhibits or blocks binding of cyno TIGIT to cyno PVR with an IC50 value of 50 nM or lower (e.g., 1 nM to about 50 nM, e.g., 1 nM to about 5 nM). In some instances, the anti-TIGIT antagonist antibody inhibits and/or blocks the interaction of CD226 with TIGIT. In some instances, the anti-TIGIT antagonist antibody inhibits and/or blocks the ability of TIGIT to disrupt CD226 homodimerization. In some instances, the methods or uses described herein may include using or administering an isolated anti-TIGIT antagonist antibody that competes for binding to TIGIT with any of the anti-TIGIT antagonist antibodies described above. For example, the method may include administering an isolated anti-TIGIT antagonist antibody that competes for binding to TIGIT with an anti-TIGIT antagonist antibody having the following six HVRs: (a) an HVR-H1 comprising the amino acid sequence of SNSAAWN (SEQ ID NO: 11); (b) an HVR-H2 comprising the amino acid sequence of KTYYRFKWYSDYAVSVKG (SEQ ID NO: 12); (c) an HVR-H3 comprising the amino acid sequence of ESTTYDLLAGPFDY (SEQ ID NO: 13); (d) an HVR-L1 comprising the amino acid sequence of KSSQTVLYSSNNKKYLA (SEQ ID NO: 14), (e) an HVR-L2 comprising the amino acid sequence of WASTRES (SEQ ID NO: 15); and (f) an HVR-L3 comprising the amino acid sequence of QQYYSTPFT (SEQ ID NO: 16). The methods described herein may also include administering an isolated anti-TIGIT antagonist antibody that binds to the same epitope as an anti-TIGIT antagonist antibody described above. In some aspects, the anti-TIGIT antagonist antibody exhibits Fc-mediated effector function, e.g., participates in antibody-dependent cellular cytotoxicity (ADCC). In some aspects, the anti-TIGIT antagonist antibody is an antibody having intact Fc-mediated effector function (e.g., tiragolumab, vibostolimab, etigilimab, EOS084448, or TJ-T6) or enhanced effector function (e.g., SGN-TGT). In other aspects, the anti-TIGIT antagonist antibody is an antibody that lacks Fc-mediated effector function (e.g., domvanalimab, BMS-986207, ASP8374, or COM902). In some aspects, the anti-TIGIT antagonist antibody is an IgG class antibody. In some aspects, the anti-TIGIT antagonist antibody is an IgG1 class antibody, e.g., tiragolumab, vibostolimab, domvanalimab, BMS-986207, etigilimab, BGB-A1217, SGN-TGT, EOS084448 (EOS-448), TJ-T6, or AB308. In some aspects, the antibody is a human monoclonal full-length IgG1 class antibody comprising an Fc region. In some aspects, the anti-TIGIT antagonist antibody is a human, monoclonal full-length IgG1 subclass antibody comprising a human IgG1 Fc region, a heavy chain variable region (VH) comprising the amino acid sequence of SEQ ID NO: 27, and a light chain variable region (VL) comprising the amino acid PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO sequence of SEQ ID NO: 29. In other aspects, the anti-TIGIT antagonist antibody is an IgG4 class antibody, e.g., ASP8374 or COM902. The anti-TIGIT antagonist antibodies (e.g., tiragolumab) useful in this invention, including compositions containing such antibodies, may be used in combination with a PD-1 axis binding antagonist (e.g., PD-L1 binding antagonists (e.g., anti-PD-L1 antagonist antibodies, e.g., atezolizumab), PD-1 binding antagonists (e.g., anti-PD-1 antagonist antibodies, e.g., pembrolizumab), and PD-L2 binding antagonists (e.g., anti-PD-L2 antagonist antibodies)). In some embodiments, the anti-TIGIT antagonist antibody functions to inhibit TIGIT signaling. In some embodiments, the anti-TIGIT antagonist antibody inhibits the binding of TIGIT to its binding partners. Exemplary TIGIT binding partners include CD155 (PVR), CD112 (PVRL2 or Nectin-2), and CD113 (PVRL3 or Nectin-3). In some embodiments, the anti-TIGIT antagonist antibody is capable of inhibiting binding between TIGIT and CD155. In some embodiments, the anti-TIGIT antagonist antibody may inhibit binding between TIGIT and CD112. In some embodiments, the anti-TIGIT antagonist antibody inhibits binding between TIGIT and CD113. In some embodiments, the anti-TIGIT antagonist antibody inhibits TIGIT-mediated cellular signaling in immune cells. In some embodiments, the anti-TIGIT antagonist antibody inhibits TIGIT by depleting regulatory T cells (e.g., when engaging a FcȖR). In some embodiments, the anti-TIGIT antibody is a monoclonal antibody. In some embodiments, the anti-TIGIT antibody is an antibody fragment selected from the group consisting of Fab, Fab’-SH, Fv, scFv, and (Fab’)2 fragments. In some embodiments, the anti-TIGIT antibody is a humanized antibody. In some embodiments, the anti-TIGIT antibody is a human antibody. In some embodiments, the anti-TIGIT antibody described herein binds to human TIGIT. In some embodiments, the anti-TIGIT antibody is an Fc fusion protein. In some embodiments, the anti-TIGIT antibody is selected from the group consisting of tiragolumab (MTIG7192A, RG6058 or RO7092284), vibostolimab (MK-7684), ASP8374 (PTZ-201), EOS884448 (EOS-448), SEA-TGT (SGN-TGT)), BGB-A1217, BMS-986207 (ONO-4686), COM902 (CGEN-15137), IBI939, domvanalimab (AB154), M6223, AB308, AB154, TJ-T6, MG1131, NB6253, HLX301, HLX53, SL-9258 (TIGIT-Fc-LIGHT), STW264, and YBL-012. In some embodiments, the anti- TIGIT antibody is selected from the group consisting of tiragolumab (MTIG7192A, RG6058 or RO7092284), vibostolimab (MK-7684), ASP8374 (PTZ-201), EOS-448, and SEA-TGT (SGN-TGT). The anti-TIGIT antibody may be tiragolumab (MTIG7192A, RG6058 or RO7092284). In some embodiments, the anti-TIGIT antibody comprises at least one, two, three, four, five, or six complementarity determining regions (CDRs) of any of the anti-TIGIT antibodies disclosed herein. In some embodiments, the anti-TIGIT antibody comprises the six CDRs of any of the anti-TIGIT antibodies disclosed herein. In some embodiments, the anti-TIGIT antibody comprises the six CDRs of any one of the antibodies selected from the group consisting of tiragolumab, ASP8374 (PTZ-201), BGB-A1217, BMS- 986207 (ONO-4686), COM902 (CGEN-15137), M6223, IBI939, EOS884448 (EOS-448), domvanalimab (AB154), vibostolimab (MK-7684), and SEA-TGT (SGN-TGT). In some embodiments, the anti-TIGIT antibody comprises a heavy chain and a light chain, wherein the heavy chain comprises a heavy chain variable region (VH) sequence of any one of the anti- PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO TIGIT antibodies disclosed herein and the light chain comprises a light chain variable region (VL) of the same antibody. In some embodiments, the anti-TIGIT antibody comprises the VH and VL of an anti-TIGIT antibody selected from the group consisting of tiragolumab, ASP8374 (PTZ-201), BGB-A1217, BMS- 986207 (ONO-4686), COM902 (CGEN-15137), M6223, IBI939, EOS884448 (EOS-448), domvanalimab (AB154), vibostolimab (MK-7684), and SEA-TGT (SGN-TGT). In some embodiments, the anti-TIGIT antibody comprises the heavy chain and the light chain of any of the anti-TIGIT antibodies disclosed herein. In some embodiments, the anti-TIGIT antibody comprises the heavy chain and the light chain of an anti-TIGIT antibody selected from the group consisting of tiragolumab, ASP8374 (PTZ-201), BGB-A1217, BMS-986207 (ONO-4686), COM902 (CGEN-15137), M6223, IBI939, EOS884448 (EOS-448), domvanalimab (AB154), vibostolimab (MK- 7684), and SEA-TGT (SGN-TGT). A. Dosing of anti-TIGIT antagonist antibodies As a general proposition, the therapeutically effective amount of an anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) administered to a subject having a cancer (e.g., HCC) will be in the range of about 0.01 to about 50 mg/kg of subject body weight, whether by one or more administrations. In some embodiments, the therapeutically effective amount of an anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) administered to a subject is in the range of 0.01 to 50 mg/kg of subject body weight, whether by one or more administrations. In some exemplary embodiments, the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is administered in a dose of about 0.01 to about 45 mg/kg, about 0.01 to about 40 mg/kg, about 0.01 to about 35 mg/kg, about 0.01 to about 30 mg/kg, about 0.01 to about 25 mg/kg, about 0.01 to about 20 mg/kg, about 0.01 to about 15 mg/kg, about 0.01 to about 10 mg/kg, about 0.01 to about 5 mg/kg, or about 0.01 to about 1 mg/kg administered daily, weekly, every two weeks, every three weeks, or every four weeks, for example. In exemplary embodiments, the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is administered in a dose of 0.01 to 45 mg/kg, 0.01 to 40 mg/kg, 0.01 to 35 mg/kg, 0.01 to 30 mg/kg, 0.01 to 25 mg/kg, 0.01 to 20 mg/kg, 0.01 to 15 mg/kg, 0.01 to 10 mg/kg, 0.01 to 5 mg/kg, or 0.01 to 1 mg/kg administered daily, weekly, every two weeks, every three weeks, or every four weeks, for example. In some instances, the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is administered on about Day 1 (e.g., Day -3, Day -2, Day -1, Day 1, Day 2, or Day 3) of a dosing cycle. In some instances, the effective amount of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of between about 30 mg to about 1200 mg (e.g., between about 30 mg to about 1100 mg, e.g., between about 60 mg to about 1000 mg, e.g., between about 100 mg to about 900 mg, e.g., between about 200 mg to about 800 mg, e.g., between about 300 mg to about 800 mg, e.g., between about 400 mg to about 800 mg, e.g., between about 400 mg to about 750 mg, e.g., between about 450 mg to about 750 mg, e.g., between about 500 PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO mg to about 700 mg, e.g., between about 550 mg to about 650 mg, e.g., 600 mg ± 10 mg, e.g., 600 ± 6 mg, e.g., 600 ± 5 mg, e.g., 600 ± 3 mg, e.g., 600 ± 1 mg, e.g., 600 ± 0.5 mg, e.g., 600 mg) every three weeks (Q3W). In some instances, the effective amount of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of between about 30 mg to about 600 mg (e.g., between about 50 mg to between 600 mg, e.g., between about 60 mg to about 600 mg, e.g., between about 100 mg to about 600 mg, e.g., between about 200 mg to about 600 mg, e.g., between about 200 mg to about 550 mg, e.g., between about 250 mg to about 500 mg, e.g., between about 300 mg to about 450 mg, e.g., between about 350 mg to about 400 mg, e.g., about 375 mg) every three weeks. In some instances, the effective amount of the anti-TIGIT antagonist antibody (e.g., an anti- TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of about 600 mg every three weeks. In some instances, the effective amount of the anti-TIGIT antagonist antibody (e.g., an anti- TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of 600 mg every three weeks. In some instances, the fixed dose of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) administered in a combination therapy (e.g., a combination treatment with a PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) may be reduced as compared to a standard dose of the anti-TIGIT antagonist antibody administered as a monotherapy. In some instances, the effective amount of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of between about 10 mg to about 1000 mg (e.g., between about 20 mg to about 1000 mg, e.g., between about 50 mg to about 900 mg, e.g., between about 100 mg to about 850 mg, e.g., between about 200 mg to about 800 mg, e.g., between about 300 mg to about 600 mg, e.g., between about 400 mg to about 500 mg, e.g., between about 405 mg to about 450 mg, e.g., between about 410 mg to about 430 mg, e.g., about 420 mg) every two weeks (Q2W). In some instances, the effective amount of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of about 420 mg every two weeks (e.g., 420 mg ± 10 mg, e.g., 420 ± 6 mg, e.g., 420 ± 5 mg, e.g., 420 ± 3 mg, e.g., 420 ± 1 mg, e.g., 420 ± 0.5 mg, e.g., 420 mg every two weeks). In some instances, the effective amount of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of between about 200 mg to about 2000 mg (e.g., between about 200 mg to about 1600 mg, e.g., between about 250 mg to about 1600 mg, e.g., between about 300 mg to about 1600 mg, e.g., between about 400 mg to about 1500 mg, e.g., between about 500 mg to about 1400 mg, e.g., between about 600 mg to about 1200 mg, e.g., between about 700 mg to about 1100 mg, e.g., between about 800 mg to about 1000 mg, e.g., between about 800 mg to about 900 mg, e.g., about 800, about 810, about 820, about 830, about 840, about 850, about 860, about 870, about 880, about 890, or about 900 mg) every four weeks (Q4W). In some instances, the effective amount of anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a fixed dose of about 840 mg every four weeks (e.g., 840 mg ± 10 mg, e.g., 840 ± 6 mg, e.g., 840 ± 5 mg, e.g., 840 ± 3 mg, e.g., 840 ± 1 mg, e.g., 840 ± 0.5 mg, e.g., 840 mg every four weeks). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some instances, the dose of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is a tiered dose based on a subject’s body weight (e.g., body weight (BW) > 40 kg: 600 mg, BW > 15 kg and ^ 40 kg: 400 mg, and BW ^ 15 kg: 300 mg). In some instances, the dose of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) administered in a combination therapy (e.g., a combination treatment with a PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) may be reduced as compared to a standard dose of the anti-TIGIT antagonist antibody administered as a monotherapy. In some instances, the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is administered intravenously. Alternatively, in some embodiments, the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) is administered subcutaneously. In some instances, tiragolumab is administered to the subject intravenously at a dose of about 420 mg every 2 weeks, about 600 mg every 3 weeks, or about 840 mg of every 4 weeks. In some instances, tiragolumab is administered to the subject intravenously at a dose of 420 mg every 2 weeks, 600 mg every 3 weeks, or 840 mg of every 4 weeks. In some instances, the dose of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) administered in a combination therapy (e.g., a combination treatment with a PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab) or an anti-PD-1 antagonist antibody (e.g., MDX-1106 (nivolumab) or MK-3475 (pembrolizumab, previously known as lambrolizumab))) may be reduced as compared to a standard dose of the anti-TIGIT antagonist antibody administered as a monotherapy. In some instances, the dose of the anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab) administered in a combination therapy (e.g., a combination treatment with a PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)), with or without one or more chemotherapeutic agents (e.g., a platinum-based chemotherapeutic agent (e.g., carboplatin or cisplatin) and/or a non-platinum-based chemotherapeutic agent (e.g., an alkylating agent (e.g., cyclophosphamide), a taxane (e.g., paclitaxel or nab-paclitaxel), and/or a topoisomerase II inhibitor (e.g., doxorubicin))) and/or G-CSF or GM-CSF, may be reduced as compared to a standard dose of the anti-TIGIT antagonist antibody administered as a monotherapy. In some instances, a subject is administered a total of 1 to 60 doses of an anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab), e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, or 60 doses. In some instances, a subject is administered a total of 1 to 60 doses of an anti-TIGIT antagonist antibody (e.g., an anti-TIGIT antagonist antibody as disclosed herein, e.g., tiragolumab), e.g., 1 to 60 doses, 1 to 55 doses, 1 to 50 doses, 1 to 45 doses, 1 to 40 doses, 1 to 35 doses, 1 to 30 doses, 1 to 25 doses, 1 to 20 doses, 1 to 15 doses, 1 to 10 doses, 1 to 5 doses, 2 to 60 doses, 2 to 55 doses, 2 to 50 doses, 2 to 45 doses, 2 to 40 doses, 2 to 35 doses, 2 to 30 doses, 2 to 25 doses, 2 to 20 doses, 2 to 15 doses, 2 to 10 doses, 2 to 5 doses, 3 to 60 doses, 3 to 55 doses, 3 to 50 doses, 3 to 45 doses, 3 to 40 doses, 3 to 35 doses, 3 to 30 doses, 3 to 25 doses, 3 to 20 doses, 3 to 15 doses, 3 to 10 doses, 3 to 5 PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO doses, 4 to 60 doses, 4 to 55 doses, 4 to 50 doses, 4 to 45 doses, 4 to 40 doses, 4 to 35 doses, 4 to 30 doses, 4 to 25 doses, 4 to 20 doses, 4 to 15 doses, 4 to 10 doses, 4 to 5 doses, 5 to 60 doses, 5 to 55 doses, 5 to 50 doses, 5 to 45 doses, 5 to 40 doses, 5 to 35 doses, 5 to 30 doses, 5 to 25 doses, 5 to 20 doses, 5 to 15 doses, 5 to 10 doses, 10 to 60 doses, 10 to 55 doses, 10 to 50 doses, 10 to 45 doses, 10 to 40 doses, 10 to 35 doses, 10 to 30 doses, 10 to 25 doses, 10 to 20 doses, 10 to 15 doses, 15 to 60 doses, 15 to 55 doses, 15 to 50 doses, 15 to 45 doses, 15 to 40 doses, 15 to 35 doses, 15 to 30 doses, 15 to 25 doses, 15 to 20 doses, 20 to 60 doses, 20 to 55 doses, 20 to 50 doses, 20 to 45 doses, 20 to 40 doses, 20 to 35 doses, 20 to 30 doses, 20 to 25 doses, 25 to 60 doses, 25 to 55 doses, 25 to 50 doses, 25 to 45 doses, 25 to 40 doses, 25 to 35 doses, 25 to 30 doses, 30 to 60 doses, 30 to 55 doses, 30 to 50 doses, 30 to 45 doses, 30 to 40 doses, 30 to 35 doses, 35 to 60 doses, 35 to 55 doses, 35 to 50 doses, 35 to 45 doses, 35 to 40 doses, 40 to 60 doses, 40 to 55 doses, 40 to 50 doses, 40 to 45 doses, 45 to 50 doses, 50 to 60 doses, or 55 to 60 doses. In particular instances, the doses may be administered intravenously. The anti-TIGIT antagonist antibody may be administered in any suitable manner known in the art. In some instances, the anti-TIGIT antagonist antibody is administered on about Day 1 (e.g., Day -3, Day - 2, Day -1, Day 1, Day 2, or Day 3) of a dosing cycle. In some instances, the anti-TIGIT antagonist antibody may be administered on the same day. In some instances, the PD-1 axis binding antagonist is administered intravenously, intramuscularly, subcutaneously, topically, orally, transdermally, intraperitoneally, intraorbitally, by implantation, by inhalation, intrathecally, intraventricularly, or intranasally. In some instances, the anti-TIGIT antagonist antibody is administered intravenously. In some instances, the anti-TIGIT antagonist antibody is administered intravenously, intramuscularly, subcutaneously, topically, orally, transdermally, intraperitoneally, intraorbitally, by implantation, by inhalation, intrathecally, intraventricularly, or intranasally. In some instances, the anti-TIGIT antagonist antibody is administered intravenously. In some instances, there is a first observation period following administration of anti-TIGIT antagonist antibody. In some instances, the observation period is between about 30 minutes to about 60 minutes in length. In some instances, the anti-TIGIT antagonist antibody is administered intravenously or subcutaneously. In one example, tiragolumab may be administered intravenously over 60 minutes; if the first infusion is tolerated, all subsequent infusions may be delivered over 30 minutes. In any of the preceding examples, each dosing cycle may have any suitable length, e.g., about 7 days (about 5, 6, 7, 8, or 9 days), about 14 days (e.g., about 12, 13, 14, 15, or 16 days), about 21 days (e.g., about 18, 19, 20, 21, 22, 23, or 24 days), about 28 days (about 25, 26, 27, 28, 29, 30, or 31 days), or longer. In some instances, each dosing cycle is about 21 days. V. PD-1 AXIS BINDING ANTAGONISTS PD-1 axis binding antagonists may include PD-L1 binding antagonists, PD-1 binding antagonists, and PD-L2 binding antagonists. Any suitable PD-1 axis binding antagonist may be used for treating a subject having a cancer (e.g., an HCC, e.g., a resectable HCC). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO A. PD-L1 Binding Antagonists In some instances, the PD-L1 binding antagonist inhibits the binding of PD-L1 to one or more of its ligand binding partners. In other instances, the PD-L1 binding antagonist inhibits the binding of PD-L1 to PD-1. In yet other instances, the PD-L1 binding antagonist inhibits the binding of PD-L1 to B7-1. In some instances, the PD-L1 binding antagonist inhibits the binding of PD-L1 to both PD-1 and B7-1. The PD-L1 binding antagonist may be, without limitation, an antibody, an antigen-binding fragment thereof, an immunoadhesin, a fusion protein, an oligopeptide, or a small molecule. In some instances, the PD-L1 binding antagonist is a small molecule that inhibits PD-L1 (e.g., GS-4224, INCB086550, MAX-10181, INCB090244, CA-170, or ABSK041). In some instances, the PD-L1 binding antagonist is a small molecule that inhibits PD-L1 and VISTA. In some instances, the PD-L1 binding antagonist is CA-170 (also known as AUPM-170). In some instances, the PD-L1 binding antagonist is a small molecule that inhibits PD-L1 and TIM3. In some instances, the small molecule is a compound described in WO 2015/033301 and/or WO 2015/033299. In some instances, the PD-L1 binding antagonist is an anti-PD-L1 antibody. A variety of anti-PD- L1 antibodies are contemplated and described herein. In any of the instances herein, the isolated anti- PD-L1 antibody can bind to a human PD-L1, for example a human PD-L1 as shown in UniProtKB/Swiss- Prot Accession No. Q9NZQ7-1, or a variant thereof. In some instances, the anti-PD-L1 antibody is capable of inhibiting binding between PD-L1 and PD-1 and/or between PD-L1 and B7-1. In some instances, the anti-PD-L1 antibody is a monoclonal antibody. In some instances, the anti-PD-L1 antibody is an antibody fragment selected from the group consisting of Fab, Fab’-SH, Fv, scFv, and (Fab’)2 fragments. In some instances, the anti-PD-L1 antibody is a humanized antibody. In some instances, the anti-PD-L1 antibody is a human antibody. Exemplary anti-PD-L1 antibodies include atezolizumab, MDX- 1105, MEDI4736 (durvalumab), MSB0010718C (avelumab), SHR-1316, CS1001, envafolimab, TQB2450, ZKAB001, LP-002, CX-072, IMC-001, KL-A167, APL-502, cosibelimab, lodapolimab, FAZ053, TG-1501, BGB-A333, BCD-135, AK-106, LDP, GR1405, HLX20, MSB2311, RC98, PDL-GEX, KD036, KY1003, YBL-007, and HS-636. Examples of anti-PD-L1 antibodies useful in the methods of this invention and methods of making them are described in International Patent Application Publication No. WO 2010/077634 and U.S. Patent No.8,217,149, each of which is incorporated herein by reference in its entirety. In some instances, the anti-PD-L1 antibody comprises: (a) an HVR-H1, HVR-H2, and HVR-H3 sequence of GFTFSDSWIH (SEQ ID NO: 3), AWISPYGGSTYYADSVKG (SEQ ID NO: 4) and RHWPGGFDY (SEQ ID NO: 5), respectively, and (b) an HVR-L1, HVR-L2, and HVR-L3 sequence of RASQDVSTAVA (SEQ ID NO: 6), SASFLYS (SEQ ID NO: 7) and QQYLYHPAT (SEQ ID NO: 8), respectively. In one embodiment, the anti-PD-L1 antibody comprises: (a) a heavy chain variable region (VH) comprising the amino acid sequence: EVQLVESGGGLVQPGGSLRLSCAASGFTFSDSWIHWVRQAPGKGLEWVAWISPYGGSTYYADSVKGRF TISADTSKNTAYLQMNSLRAEDTAVYYCARRHWPGGFDYWGQGTLVTVSS (SEQ ID NO: 9), and PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO (b) the light chain variable region (VL) comprising the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKPGKAPKLLIYSASFLYSGVPSRFSGSGSGTD FTLTISSLQPEDFATYYCQQYLYHPATFGQGTKVEIKR (SEQ ID NO: 10). In some instances, the anti-PD-L1 antibody comprises (a) a VH comprising an amino acid sequence comprising having at least 95% sequence identity (e.g., at least 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of SEQ ID NO: 9; (b) a VL comprising an amino acid sequence comprising having at least 95% sequence identity (e.g., at least 95%, 96%, 97%, 98%, or 99% sequence identity) to, or the sequence of SEQ ID NO: 10; or (c) a VH as in (a) and a VL as in (b). In one embodiment, the anti-PD-L1 antibody comprises atezolizumab, which comprises: (a) the heavy chain amino acid sequence: EVQLVESGGGLVQPGGSLRLSCAASGFTFSDSWIHWVRQAPGKGLEWVAWISPYGGSTYYADSVKGRF TISADTSKNTAYLQMNSLRAEDTAVYYCARRHWPGGFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTS GGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKP SNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFN WYVDGVEVHNAKTKPREEQYASTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPRE PQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKS RWQQGNVFSCSVMHEALHNHYTQKSLSLSPG (SEQ ID NO: 1), and (b) the light chain amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKPGKAPKLLIYSASFLYSGVPSRFSGSGSGTD FTLTISSLQPEDFATYYCQQYLYHPATFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR GEC (SEQ ID NO: 2). In some instances, the anti-PD-L1 antibody is avelumab (CAS Registry Number: 1537032-82-8). Avelumab, also known as MSB0010718C, is a human monoclonal IgG1 anti-PD-L1 antibody (Merck KGaA, Pfizer). In some instances, the anti-PD-L1 antibody is durvalumab (CAS Registry Number: 1428935-60- 7). Durvalumab, also known as MEDI4736, is an Fc-optimized human monoclonal IgG1 kappa anti-PD-L1 antibody (MedImmune, AstraZeneca) described in WO 2011/066389 and US 2013/034559. In some instances, the anti-PD-L1 antibody is MDX-1105 (Bristol Myers Squibb). MDX-1105, also known as BMS-936559, is an anti-PD-L1 antibody described in WO 2007/005874. In some instances, the anti-PD-L1 antibody is LY3300054 (Eli Lilly). In some instances, the anti-PD-L1 antibody is STI-A1014 (Sorrento). STI-A1014 is a human anti- PD-L1 antibody. In some instances, the anti-PD-L1 antibody is KN035 (Suzhou Alphamab). KN035 is single- domain antibody (dAB) generated from a camel phage display library. In some instances, the anti-PD-L1 antibody comprises a cleavable moiety or linker that, when cleaved (e.g., by a protease in the tumor microenvironment), activates an antibody antigen-binding domain to allow it to bind its antigen, e.g., by removing a non-binding steric moiety. In some instances, the anti-PD-L1 antibody is CX-072 (CytomX Therapeutics). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some instances, the anti-PD-L1 antibody comprises the six HVR sequences (e.g., the three heavy chain HVRs and the three light chain HVRs) and/or the heavy chain variable domain and light chain variable domain from an anti-PD-L1 antibody described in US 20160108123, WO 2016/000619, WO 2012/145493, U.S. Pat. No.9,205,148, WO 2013/181634, or WO 2016/061142. In a still further specific aspect, the anti-PD-L1 antibody has reduced or minimal effector function. In a still further specific aspect, the minimal effector function results from an “effector-less Fc mutation” or aglycosylation mutation. In still a further instance, the effector-less Fc mutation is an N297A or D265A/N297A substitution in the constant region. In still a further instance, the effector-less Fc mutation is an N297A substitution in the constant region. In some instances, the isolated anti-PD-L1 antibody is aglycosylated. Glycosylation of antibodies is typically either N-linked or O- linked. N-linked refers to the attachment of the carbohydrate moiety to the side chain of an asparagine residue. The tripeptide sequences asparagine-X-serine and asparagine-X-threonine, where X is any amino acid except proline, are the recognition sequences for enzymatic attachment of the carbohydrate moiety to the asparagine side chain. Thus, the presence of either of these tripeptide sequences in a polypeptide creates a potential glycosylation site. O-linked glycosylation refers to the attachment of one of the sugars N- acetylgalactosamine, galactose, or xylose to a hydroxyamino acid, most commonly serine or threonine, although 5-hydroxyproline or 5-hydroxylysine may also be used. Removal of glycosylation sites from an antibody is conveniently accomplished by altering the amino acid sequence such that one of the above- described tripeptide sequences (for N-linked glycosylation sites) is removed. The alteration may be made by substitution of an asparagine, serine or threonine residue within the glycosylation site with another amino acid residue (e.g., glycine, alanine, or a conservative substitution). B. PD-1 Binding Antagonists In some instances, the PD-1 axis binding antagonist is a PD-1 binding antagonist. For example, in some instances, the PD-1 binding antagonist inhibits the binding of PD-1 to one or more of its ligand binding partners. In some instances, the PD-1 binding antagonist inhibits the binding of PD-1 to PD-L1. In other instances, the PD-1 binding antagonist inhibits the binding of PD-1 to PD-L2. In yet other instances, the PD-1 binding antagonist inhibits the binding of PD-1 to both PD-L1 and PD-L2. The PD-1 binding antagonist may be, without limitation, an antibody, an antigen-binding fragment thereof, an immunoadhesin, a fusion protein, an oligopeptide, or a small molecule. In some instances, the PD-1 binding antagonist is an immunoadhesin (e.g., an immunoadhesin comprising an extracellular or PD-1 binding portion of PD-L1 or PD-L2 fused to a constant region (e.g., an Fc region of an immunoglobulin sequence). For example, in some instances, the PD-1 binding antagonist is an Fc-fusion protein. In some instances, the PD-1 binding antagonist is AMP-224. AMP-224, also known as B7-DCIg, is a PD-L2- Fc fusion soluble receptor described in WO 2010/027827 and WO 2011/066342. In some instances, the PD-1 binding antagonist is a peptide or small molecule compound. In some instances, the PD-1 binding antagonist is AUNP-12 (PierreFabre/Aurigene). See, e.g., WO 2012/168944, WO 2015/036927, WO 2015/044900, WO 2015/033303, WO 2013/144704, WO 2013/132317, and WO 2011/161699. In some instances, the PD-1 binding antagonist is a small molecule that inhibits PD-1. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some instances, the PD-1 binding antagonist is an anti-PD-1 antibody. A variety of anti-PD-1 antibodies can be utilized in the methods and uses disclosed herein. In any of the instances herein, the PD-1 antibody can bind to a human PD-1 or a variant thereof. In some instances, the anti-PD-1 antibody is a monoclonal antibody. In some instances, the anti-PD-1 antibody is an antibody fragment selected from the group consisting of Fab, Fab’, Fab’-SH, Fv, scFv, and (Fab’)₂ fragments. In some instances, the anti-PD-1 antibody is a humanized antibody. In other instances, the anti-PD-1 antibody is a human antibody. Exemplary anti-PD-1 antagonist antibodies include nivolumab, pembrolizumab, MEDI-0680, PDR001 (spartalizumab), REGN2810 (cemiplimab), BGB-108, prolgolimab, camrelizumab, sintilimab, tislelizumab, toripalimab, dostarlimab, retifanlimab, sasanlimab, penpulimab, CS1003, HLX10, SCT-I10A, zimberelimab, balstilimab, genolimzumab, BI 754091, cetrelimab, YBL-006, BAT1306, HX008, budigalimab, AMG 404, CX-188, JTX-4014, 609A, Sym021, LZM009, F520, SG001, AM0001, ENUM 244C8, ENUM 388D4, STI-1110, AK-103, and hAb21. In some instances, the anti-PD-1 antibody is nivolumab (CAS Registry Number: 946414-94-4). Nivolumab (Bristol-Myers Squibb/Ono), also known as MDX-1106-04, MDX-1106, ONO-4538, BMS- 936558, and OPDIVO®, is an anti-PD-1 antibody described in WO 2006/121168. In some instances, the anti-PD-1 antibody is pembrolizumab (CAS Registry Number: 1374853- 91-4). Pembrolizumab (Merck), also known as MK-3475, Merck 3475, lambrolizumab, SCH-900475, and KEYTRUDA®, is an anti-PD-1 antibody described in WO 2009/114335. In some instances, the anti-PD-1 antibody is MEDI-0680 (AMP-514; AstraZeneca). MEDI-0680 is a humanized IgG4 anti-PD-1 antibody. In some instances, the anti-PD-1 antibody is PDR001 (CAS Registry No.1859072-53-9; Novartis). PDR001 is a humanized IgG4 anti-PD-1 antibody that blocks the binding of PD-L1 and PD-L2 to PD-1. In some instances, the anti-PD-1 antibody is REGN2810 (Regeneron). REGN2810 is a human anti-PD-1 antibody. In some instances, the anti-PD-1 antibody is BGB-108 (BeiGene). In some instances, the anti-PD-1 antibody is BGB-A317 (BeiGene). In some instances, the anti-PD-1 antibody is JS-001 (Shanghai Junshi). JS-001 is a humanized anti-PD-1 antibody. In some instances, the anti-PD-1 antibody is STI-A1110 (Sorrento). STI-A1110 is a human anti- PD-1 antibody. In some instances, the anti-PD-1 antibody is INCSHR-1210 (Incyte). INCSHR-1210 is a human IgG4 anti-PD-1 antibody. In some instances, the anti-PD-1 antibody is PF-06801591 (Pfizer). In some instances, the anti-PD-1 antibody is TSR-042 (also known as ANB011; Tesaro/AnaptysBio). In some instances, the anti-PD-1 antibody is AM0001 (ARMO Biosciences). In some instances, the anti-PD-1 antibody is ENUM 244C8 (Enumeral Biomedical Holdings). ENUM 244C8 is an anti-PD-1 antibody that inhibits PD-1 function without blocking binding of PD-L1 to PD-1. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some instances, the anti-PD-1 antibody is ENUM 388D4 (Enumeral Biomedical Holdings). ENUM 388D4 is an anti-PD-1 antibody that competitively inhibits binding of PD-L1 to PD-1. In some instances, the anti-PD-1 antibody comprises the six HVR sequences (e.g., the three heavy chain HVRs and the three light chain HVRs) and/or the heavy chain variable domain and light chain variable domain from an anti-PD-1 antibody described in WO 2015/112800, WO 2015/112805, WO 2015/112900, US 20150210769 , WO2016/089873, WO 2015/035606, WO 2015/085847, WO 2014/206107, WO 2012/145493, US 9,205,148, WO 2015/119930, WO 2015/119923, WO 2016/032927, WO 2014/179664, WO 2016/106160, and WO 2014/194302. In a still further specific aspect, the anti-PD-1 antibody has reduced or minimal effector function. In a still further specific aspect, the minimal effector function results from an “effector-less Fc mutation” or aglycosylation mutation. In still a further instance, the effector-less Fc mutation is an N297A or D265A/N297A substitution in the constant region. In some instances, the isolated anti-PD-1 antibody is aglycosylated. C. PD-L2 Binding Antagonists In some instances, the PD-1 axis binding antagonist is a PD-L2 binding antagonist. In some instances, the PD-L2 binding antagonist is a molecule that inhibits the binding of PD-L2 to its ligand binding partners. In a specific aspect, the PD-L2 binding ligand partner is PD-1. The PD-L2 binding antagonist may be, without limitation, an antibody, an antigen-binding fragment thereof, an immunoadhesin, a fusion protein, an oligopeptide, or a small molecule. In some instances, the PD-L2 binding antagonist is an anti-PD-L2 antibody. In any of the instances herein, the anti-PD-L2 antibody can bind to a human PD-L2 or a variant thereof. In some instances, the anti-PD-L2 antibody is a monoclonal antibody. In some instances, the anti-PD-L2 antibody is an antibody fragment selected from the group consisting of Fab, Fab’, Fab’-SH, Fv, scFv, and (Fab’)2 fragments. In some instances, the anti-PD-L2 antibody is a humanized antibody. In other instances, the anti-PD-L2 antibody is a human antibody. In a still further specific aspect, the anti-PD-L2 antibody has reduced or minimal effector function. In a still further specific aspect, the minimal effector function results from an “effector-less Fc mutation” or aglycosylation mutation. In still a further instance, the effector-less Fc mutation is an N297A or D265A/N297A substitution in the constant region. In some instances, the isolated anti-PD-L2 antibody is aglycosylated. D. Dosing of PD-1 axis binding antagonists As a general proposition, the therapeutically effective amount of a PD-1 axis binding antagonist (e.g., atezolizumab) administered to a subject having a cancer (e.g., an HCC) will be in the range of about 0.01 to about 50 mg/kg of subject body weight, whether by one or more administrations. In some exemplary embodiments, the PD-1 axis binding antagonist (e.g., atezolizumab) is administered in a dose of about 0.01 to about 45 mg/kg, about 0.01 to about 40 mg/kg, about 0.01 to about 35 mg/kg, about 0.01 to about 30 mg/kg, about 0.01 to about 25 mg/kg, about 0.01 to about 20 mg/kg, about 0.01 to about 15 mg/kg, about 0.01 to about 10 mg/kg, about 0.01 to about 5 mg/kg, or PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO about 0.01 to about 1 mg/kg administered daily, weekly, every two weeks, every three weeks, or every four weeks, for example. In some instances, the dose of the PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a dose based on a subject’s body weight (e.g., 15 mg/kg). In some instances, the dose of the PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a dose based on a subject’s body surface area (e.g., body surface area (BSA) > 1.25 m²: 600 mg, BSA > 0.75 m² and ^ 1.25 m²: 450 mg, BSA > 0.5 m² and ^ 0.75 m²: 350 mg, and BSA ^ 0.5 m²: 300 mg). In some instances, the effective amount of the PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a fixed dose of between about 80 mg to about 1600 mg (e.g., between about 100 mg to about 1600 mg, e.g., between about 200 mg to about 1600 mg, e.g., between about 300 mg to about 1600 mg, e.g., between about 400 mg to about 1600 mg, e.g., between about 500 mg to about 1600 mg, e.g., between about 600 mg to about 1600 mg, e.g., between about 700 mg to about 1600 mg, e.g., between about 800 mg to about 1600 mg, e.g., between about 900 mg to about 1500 mg, e.g., between about 1000 mg to about 1400 mg, e.g., between about 1050 mg to about 1350 mg, e.g., between about 1100 mg to about 1300 mg, e.g., between about 1150 mg to about 1250 mg, e.g., between about 1175 mg to about 1225 mg, e.g., between about 1190 mg to about 1210 mg, e.g., 1200 mg ± 5 mg, e.g., 1200 ± 2.5 mg, e.g., 1200 ± 1.0 mg, e.g., 1200 ± 0.5 mg, e.g., 1200) every three weeks. In some embodiments, the effective amount of the PD-1 axis binding antagonist is atezolizumab at a fixed dose of about 1200 mg every three weeks. In some embodiments, the effective amount of the PD-1 axis binding antagonist is pembrolizumab at a fixed dose of about 200 mg every three weeks or, alternatively, pembrolizumab at a fixed dose of about 400 mg every six weeks. In some instances, the fixed dose of the PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) administered in a combination therapy (e.g., a combination treatment with an anti-TIGIT antagonist antibody, such as an anti-TIGIT antagonist antibody disclosed herein, e.g., tiragolumab) may be reduced as compared to a standard dose of the PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) administered as a monotherapy. In some instances, the effective amount of the PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a dose of between about 0.01 mg/kg to about 50 mg/kg of the subject’s body weight (e.g., between about 0.01 mg/kg to about 45 mg/kg, e.g., between about 0.1 mg/kg to about 40 mg/kg, e.g., between about 1 mg/kg to about 35 mg/kg, e.g., between about 2.5 mg/kg to about 30 mg/kg, e.g., between about 5 mg/kg to about 25 mg/kg, e.g., between about 10 mg/kg to about 20 mg/kg, e.g., between about 12.5 mg/kg to about 15 mg/kg, e.g., about 15 ± 2 mg/kg, about 15 ± 1 mg/kg, about 15 ± 0.5 mg/kg, about 15 ± 0.2 mg/kg, or about 15 ± 0.1 mg/kg, e.g., about 15 mg/kg) every three weeks. In some instances, the effective amount of the PD-1 axis binding antagonist (e.g., an anti- PD-L1 antagonist antibody (e.g., atezolizumab)) is a dose of between about 0.01 mg/kg to about 15 mg/kg of the subject’s body weight (e.g., between about 0.1 mg/kg to about 15 mg/kg, e.g., between about 0.5 mg/kg to about 15 mg/kg, e.g., between about 1 mg/kg to about 15 mg/kg, e.g., between about 2.5 mg/kg to about 15 mg/kg, e.g., between about 5 mg/kg to about 15 mg/kg, e.g., between about 7.5 mg/kg to about 15 mg/kg, e.g., between about 10 mg/kg to about 15 mg/kg, e.g., between about 12.5 mg/kg to PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO about 15 mg/kg, e.g., between about 14 mg/kg to about 15 mg/kg, e.g., about 15 ± 1 mg/kg, e.g., about 15 ± 0.5 mg/kg, e.g., about 15 ± 0.2 mg/kg, e.g., about 15 ± 0.1 mg/kg, e.g., about 15 mg/kg) every three weeks. In some instances, the effective amount of PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a dose of about 15 mg/kg administered every three weeks. In some instances, the dose of the PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) administered in a combination therapy (e.g., a combination treatment with an anti- TIGIT antagonist antibody, such as an anti-TIGIT antagonist antibody disclosed herein, e.g., tiragolumab) may be reduced as compared to a standard dose of the PD-1 axis binding antagonist (e.g., an anti-PD-L1 antagonist antibody (e.g., atezolizumab)) administered as a monotherapy. In some instances, the effective amount of the PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a fixed dose of between about 20 mg to about 1600 mg (e.g., between about 40 mg to about 1500 mg, e.g., between about 200 mg to about 1400 mg, e.g., between about 300 mg to about 1400 mg, e.g., between about 400 mg to about 1400 mg, e.g., between about 500 mg to about 1300 mg, e.g., between about 600 mg to about 1200 mg, e.g., between about 700 mg to about 1100 mg, e.g., between about 800 mg to about 1000 mg, e.g., between about 800 mg to about 900 mg, e.g., about 800, about 810, about 820, about 830, about 840, about 850, about 860, about 870, about 880, about 890, or about 900 mg) every two weeks (Q2W). In some instances, the effective amount of the PD-1 axis binding antagonist is atezolizumab at a fixed dose of about 840 mg every two weeks (e.g., 840 mg ± 10 mg, e.g., 840 ± 6 mg, e.g., 840 ± 5 mg, e.g., 840 ± 3 mg, e.g., 840 ± 1 mg, e.g., 840 ± 0.5 mg, e.g., 840 mg every two weeks). In some embodiments, the effective amount of the PD-1 axis binding antagonist is avelumab at a fixed dose of about 800 mg every two weeks. In some embodiments, the effective amount of the PD-1 axis binding antagonist is nivolumab at a fixed dose of about 240 mg every two weeks. In some instances, the effective amount of the PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a fixed dose of between about 500 mg to about 3000 mg (e.g., between about 500 mg to about 2800 mg, e.g., between about 600 mg to about 2700 mg, e.g., between about 650 mg to about 2600 mg, e.g., between about 700 mg to about 2500 mg, e.g., between about 1000 mg to about 2400 mg, e.g., between about 1100 mg to about 2300 mg, e.g., between about 1200 mg to about 2200 mg, e.g., between about 1300 mg to about 2100 mg, e.g., between about 1400 mg to about 2000 mg, e.g., between about 1500 mg to about 1900 mg, e.g., between about 1600 mg to about 1800 mg, e.g., between about 1620 mg to about 1700 mg, e.g., between about 1640 mg to about 1690 mg, e.g., between about 1660 mg to about 1680 mg, about 1680 mg, e.g., about 1600 mg, about 1610 mg, about 1620 mg, about 1630 mg, about 1640 mg, about 1650 mg, about 1660 mg, about 1670 mg, about 1680 mg, about 1690 mg, or about 1700 mg) every four weeks (Q4W). In some instances, the effective amount of the PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) is a fixed dose of 1680 mg every four weeks (e.g., 1680 mg ± 10 mg, e.g., 1680 ± 6 mg, e.g., 1680 ± 5 mg, e.g., 1680 ± 3 mg, e.g., 1680 ± 1 mg, e.g., 1680 ± 0.5 mg, e.g., 1680 mg every four weeks). In some embodiments, the effective amount of the PD-1 axis binding antagonist is nivolumab at a fixed dose of about 480 mg every four weeks. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some instances, the dose of the PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) administered in a combination therapy (e.g., a combination treatment with an anti-TIGIT antagonist antibody, such as an anti-TIGIT antagonist antibody disclosed herein (e.g., tiragolumab) may be reduced as compared to a standard dose of the anti-PD-L1 antagonist antibody administered as a monotherapy. In some instances, the dose of the PD-1 axis binding antagonist (e.g., anti-PD-L1 antagonist antibody (e.g., atezolizumab)) administered in a combination therapy (e.g., a combination treatment with an anti-TIGIT antagonist antibody, such as an anti-TIGIT antagonist antibody disclosed herein, e.g., tiragolumab), with or without one or more chemotherapeutic agents (e.g., a platinum-based chemotherapeutic agent (e.g., carboplatin or cisplatin) and/or a non-platinum-based chemotherapeutic agent (e.g., an alkylating agent (e.g., cyclophosphamide), a taxane (e.g., paclitaxel, e.g., nab-paclitaxel), and/or a topoisomerase II inhibitor (e.g., doxorubicin))) and/or G-CSF or GM-CSF may be reduced as compared to a standard dose of the PD-1 axis binding antagonist administered as a monotherapy. In some instances, a subject is administered a total of 1 to 60 doses of a PD-1 axis binding antagonist (e.g., atezolizumab), e.g., 1 to 60 doses, 1 to 55 doses, 1 to 50 doses, 1 to 45 doses, 1 to 40 doses, 1 to 35 doses, 1 to 30 doses, 1 to 25 doses, 1 to 20 doses, 1 to 15 doses, 1 to 10 doses, 1 to 5 doses, 2 to 60 doses, 2 to 55 doses, 2 to 50 doses, 2 to 45 doses, 2 to 40 doses, 2 to 35 doses, 2 to 30 doses, 2 to 25 doses, 2 to 20 doses, 2 to 15 doses, 2 to 10 doses, 2 to 5 doses, 3 to 60 doses, 3 to 55 doses, 3 to 50 doses, 3 to 45 doses, 3 to 40 doses, 3 to 35 doses, 3 to 30 doses, 3 to 25 doses, 3 to 20 doses, 3 to 15 doses, 3 to 10 doses, 3 to 5 doses, 4 to 60 doses, 4 to 55 doses, 4 to 50 doses, 4 to 45 doses, 4 to 40 doses, 4 to 35 doses, 4 to 30 doses, 4 to 25 doses, 4 to 20 doses, 4 to 15 doses, 4 to 10 doses, 4 to 5 doses, 5 to 60 doses, 5 to 55 doses, 5 to 50 doses, 5 to 45 doses, 5 to 40 doses, 5 to 35 doses, 5 to 30 doses, 5 to 25 doses, 5 to 20 doses, 5 to 15 doses, 5 to 10 doses, 10 to 60 doses, 10 to 55 doses, 10 to 50 doses, 10 to 45 doses, 10 to 40 doses, 10 to 35 doses, 10 to 30 doses, 10 to 25 doses, 10 to 20 doses, 10 to 15 doses, 15 to 60 doses, 15 to 55 doses, 15 to 50 doses, 15 to 45 doses, 15 to 40 doses, 15 to 35 doses, 15 to 30 doses, 15 to 25 doses, 15 to 20 doses, 20 to 60 doses, 20 to 55 doses, 20 to 50 doses, 20 to 45 doses, 20 to 40 doses, 20 to 35 doses, 20 to 30 doses, 20 to 25 doses, 25 to 50 doses, 25 to 45 doses, 25 to 40 doses, 25 to 35 doses, 25 to 30 doses, 30 to 60 doses, 30 to 55 doses, 30 to 50 doses, 30 to 45 doses, 30 to 40 doses, 30 to 35 doses, 35 to 60 doses, 35 to 55 doses, 35 to 50 doses, 35 to 45 doses, 35 to 40 doses, 40 to 60 doses, 40 to 55 doses, 40 to 50 doses, 40 to 45 doses, 45 to 50 doses, 50 to 60 doses, or 55 to 60 doses. In particular instances, the doses may be administered intravenously. In some instances, atezolizumab is administered to the subject intravenously at a dose of about 840 mg every 2 weeks, about 1200 mg every 3 weeks, or about 1680 mg of every 4 weeks. For example, in some aspects, atezolizumab is administered to the subject intravenously at a dose of 1200 mg every 3 weeks. In some aspects, atezolizumab is administered to the subject intravenously at a dose of 840 mg every 2 weeks. In some aspects, atezolizumab is administered to the subject intravenously at a dose of 1680 mg every 4 weeks. The PD-1 axis binding antagonist and/or any additional therapeutic agent(s) may be administered in any suitable manner known in the art. For example, the PD-1 axis binding antagonist and/or any PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO additional therapeutic agent(s) may be administered sequentially (on different days) or concurrently (on the same day or during the same treatment cycle). In some instances, the PD-1 axis binding antagonist is administered prior to the additional therapeutic agent. In other instances, the PD-1 axis binding antagonist is administered after the additional therapeutic agent. In some instances, the PD-1 axis binding antagonist and/or any additional therapeutic agent(s) may be administered on the same day. In some instances, the PD-1 axis binding antagonist may be administered prior to an additional therapeutic agent that is administered on the same day. For example, the PD-1 axis binding antagonist may be administered prior to chemotherapy on the same day. In another example, the PD-1 axis binding antagonist may be administered prior to both chemotherapy and another drug (e.g., bevacizumab) on the same day. In other instances, the PD-1 axis binding antagonist may be administered after an additional therapeutic agent that is administered on the same day. In yet other instances, the PD-1 axis binding antagonist is administered at the same time as the additional therapeutic agent. In some instances, the PD-1 axis binding antagonist is in a separate composition as the additional therapeutic agent. In some instances, the PD-1 axis binding antagonist is in the same composition as the additional therapeutic agent. In some instances, the PD-1 axis binding antagonist is administered through a separate intravenous line from any other therapeutic agent administered to the subject on the same day. The PD-1 axis binding antagonist and any additional therapeutic agent(s) may be administered by the same route of administration or by different routes of administration. In some instances, the PD-1 axis binding antagonist is administered intravenously, intramuscularly, subcutaneously, topically, orally, transdermally, intraperitoneally, intraorbitally, by implantation, by inhalation, intrathecally, intraventricularly, or intranasally. In some instances, the additional therapeutic agent is administered intravenously, intramuscularly, subcutaneously, topically, orally, transdermally, intraperitoneally, intraorbitally, by implantation, by inhalation, intrathecally, intraventricularly, or intranasally. In a preferred embodiment, the PD-1 axis binding antagonist is administered intravenously. In one example, atezolizumab may be administered intravenously over 60 minutes; if the first infusion is tolerated, all subsequent infusions may be delivered over 30 minutes. In some examples, the PD-1 axis binding antagonist is not administered as an intravenous push or bolus. D. Co-administration of anti-TIGIT antagonist antibodies and PD-1 axis binding antagonists In some aspects, the anti-TIGIT antagonist antibody (e.g., tiragolumab) and the PD-1 axis binding antagonist (e.g., atezolizumab) are co-administered. For example, in some aspects, tiragolumab and atezolizumab are co-administered intravenously. In some aspects, the co-infused tiragolumab and atezolizumab are mixed prior to infusion (e.g., are formulated separately and are mixed by the physician administering the drugs), e.g., are combined in an IV bag prior to administration. In other aspects, the co- infused tiragolumab and atezolizumab are formulated together (i.e., are not mixed by the physician administering the drugs) and are administered as an IV-administered fixed dose combination (FDC). In some aspects, the IV-administered co-infusion of tiragolumab and atezolizumab (e.g., FDC) comprises atezolizumab at a dose of 1200 mg and tiragolumab at a dose of 600 mg. In some aspects, tiragolumab and atezolizumab are co-infused simultaneously. In some aspects, the co-infused tiragolumab and atezolizumab are mixed prior to infusion (e.g., are formulated separately PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO and are mixed by the physician administering the drugs). In other aspects, the co-infused tiragolumab and atezolizumab are formulated together (i.e., are not mixed by the physician administering the drugs) and are administered as an SC-administered FDC. In some aspects, the SC-administered co-infusion of tiragolumab and atezolizumab (e.g., FDC) comprises atezolizumab at a dose of 1875 mg or 2000 mg and tiragolumab at a dose of 880 mg. In other aspects, the SC-administered co-infusion of tiragolumab and atezolizumab (e.g., FDC) comprises atezolizumab at a dose of 1875 mg or 2000 mg and tiragolumab at a dose of 1000 mg. In some aspects, the method comprises both IV and SC administration of tiragolumab and/or atezolizumab, e.g., comprises one or more IV-administered doses and one or more SC-administered doses of tiragolumab and/or atezolizumab. For example, in some aspects, the method comprises administering at least one dose of tiragolumab and atezolizumab as an IV-administered FDC and comprises administering at least one dose of tiragolumab and atezolizumab as an SC-administered FDC. Exemplary IV and SC FDC doses and formulations of tiragolumab and atezolizumab are provided in PCT/US2022/082139 and in U.S. Provisional Patent Application Nos.63/493,691 (filed March 31, 2023) and 63/494,983 (filed April 7, 2023) (both titled “Methods of Treating Tumors with Anti-TIGIT Antibodies”), each of which is incorporated herein by reference in its entirety. VI. Bispecific antibodies targeting PD-1 and LAG3 A. Exemplary bispecific antibodies that bind to PD-1 and LAG3 In one aspect, the invention provides a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein said first antigen-binding domain specifically binding to PD-1 comprises a VH domain comprising (i) HVR-H1 comprising the amino acid sequence of GFSFSSY (SEQ ID NO: 35), (ii) HVR-H2 comprising the amino acid sequence GGR, and (iii) HVR-H3 comprising an amino acid sequence of TGRVYFALD (SEQ ID NO: 37); and a VL domain comprising (i) HVR-L1 comprising the amino acid sequence of SESVDTSDNSF (SEQ ID NO: 38); (ii) HVR-L2 comprising the amino acid sequence RSS, and (iii) HVR-L3 comprising the amino acid sequence of NYDVPW (SEQ ID NO: 40). In one aspect, the bispecific antibody comprises a Fc domain that is an IgG, particularly an IgG1 Fc domain or an IgG4 Fc domain and wherein the Fc domain has reduced or even abolished effector function. In particular, the Fc domain comprises one or more amino acid substitution that reduces binding to an Fc receptor, in particular towards FcȖ receptor. In a further aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the bispecific antibody comprises a Fc domain that is an IgG, particularly an IgG1 Fc domain or an IgG4 Fc domain and wherein the Fc domain comprises one or more amino acid substitution that reduces binding to an Fc receptor, in particular towards FcȖ receptor. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In another aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the second antigen-binding domain that specifically binds to LAG3 comprises a VH domain comprising (i) HVR-H1 comprising the amino acid sequence of DYTMN (SEQ ID NO: 43), (ii) HVR-H2 comprising the amino acid sequence of VISWDGGGTYYTDSVKG (SEQ ID NO: 44), and (iii) HVR-H3 comprising an amino acid sequence of GLTDTTLYGSDY (SEQ ID NO: 45); and a VL domain comprising (i) HVR-L1 comprising the amino acid sequence of RASQSISSYLN (SEQ ID NO:46), (ii) HVR-L2 comprising the amino acid sequence of AASTLQS (SEQ ID NO:47), and (iii) HVR-L3 comprising the amino acid sequence of QQTYSSPLT (SEQ ID NO:48). In a further aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the first antigen-binding domain specifically binding to PD-1 comprises a VH domain comprising the amino acid sequence of EVQLLESGGGLVQPGGSLRLSCAASGFSFSSYTMSWVRQAPGKGLEWVATISGGGRDIYYPDSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCVLLTGRVYFALDSWGQGTLVTVSS (SEQ ID NO: 41) and a VL domain comprising the amino acid sequence of DIVMTQSPDSLAVSLGERATINCKASESVDTSDNSFIHWYQQKPGQSPKLLIYRSSTLESGVPDRF SGSGSGTDFTLTISSLQAEDVAVYYCQQNYDVPWTFGQGTKVEIK (SEQ ID NO: 42). In another aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the second antigen-binding domain specifically binding to LAG3 comprises a VH domain comprising the amino acid sequence of EVQLLESGGGLVQPGGSLRL SCAASGFIFDDYTMNWVRQAPGKGLEWVAVISWDGGGTYYTDSVKGRFTISRDDFKNTLY LQMNSLRAEDTAVYYCAKGLTDTTLYGSDYWGQGTLVTVSS(SEQ ID NO: 49) and a VL domain comprising the amino acid sequence of DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSG SGTDFTLTISSLQPEDFATYYCQQ TYSSPLTFGGGTKVEIK (SEQ ID NO: 50). In a particular aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the first antigen-binding domain specifically binding to PD-1 comprises a VH domain comprising the amino acid sequence of SEQ ID NO: 41 and a VL domain comprising the amino acid sequence of SEQ ID NO: 42, and the second antigen-binding domain specifically binding to LAG3 comprises a VH domain comprising the amino acid sequence of SEQ ID NO: 49 and a VL domain comprising the amino acid sequence of SEQ ID NO: 50. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In a further aspect, the bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3 is a human, humanized or chimeric antibody. In particular, it is a humanized or chimeric antibody. In one aspect, the bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3 is bivalent. This means that the bispecific antibody comprises one antigen-binding domain that specifically binds to PD-1 and one antigen-binding domain that specifically binds to LAG3 (1+1 format). In one aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the bispecific antibody comprises an Fc domain, a first Fab fragment comprising the antigen-binding domain that specifically binds to PD-1 and a second Fab fragment comprising the antigen-binding domain that specifically binds to LAG3. In a particular aspect, in one of the Fab fragments the variable domains VL and VH are replaced by each other so that the VH domain is part of the light chain and the VL domain is part of the heavy chain. In a particular aspect, in the first Fab fragment comprising the antigen-binding domain that specifically binds to PD-1 the variable domains VL and VH are replaced by each other. In a particular aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the bispecific antibody comprises a first heavy chain comprising an amino acid sequence with at least 95% sequence identity to the sequence of SEQ ID NO: 51, a first light chain comprising an amino acid sequence with at least 95% sequence identity to the sequence of SEQ ID NO: 52, a second heavy chain comprising an amino acid sequence with at least 95% sequence identity to the sequence of SEQ ID NO: 53, and a second light chain comprising an amino acid sequence with at least 95% sequence identity to the sequence of SEQ ID NO:54. More particularly, the bispecific antibody comprises a first heavy chain comprising an amino acid sequence of SEQ ID NO: 51, a first light chain comprising an amino acid sequence of SEQ ID NO: 52, a second heavy chain comprising an amino acid sequence of SEQ ID NO: 53, and a second light chain comprising an amino acid sequence of SEQ ID NO: 54 (tobemstomig; also known as RO7247699). In a further aspect, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the bispecific antibody comprises an Fc domain, a first Fab fragment comprising the antigen-binding domain that specifically binds to PD-1 and a second Fab fragment comprising the antigen-binding domain that specifically binds to LAG3 that is fused to the C-terminus of the Fc domain. Particularly, the Fab fragment comprising the antigen-binding domain that specifically binds to LAG3 is fused to the C-terminus of the Fc domain via its VH domain (trans 1+1 format). In a particular aspect, the bispecific antibody comprises a first heavy chain comprising an amino acid sequence with at least 95% sequence identity to the sequence of SEQ ID NO: 51, a first light chain comprising an amino acid sequence with at least 95% sequence identity to the sequence of SEQ ID NO: 52, a second heavy chain comprising an amino acid sequence with at least 95% sequence identity to the sequence of SEQ ID NO: 73, and a second light chain comprising an amino acid sequence with at least PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 95% sequence identity to the sequence of SEQ ID NO: 54. More particularly, the bispecific antibody comprises a first heavy chain comprising an amino acid sequence of SEQ ID NO: 51, a first light chain comprising an amino acid sequence of SEQ ID NO:52, a second heavy chain comprising an amino acid sequence of SEQ ID NO: 73, and a second light chain comprising an amino acid sequence of SEQ ID NO: 54. i. Fc domain modifications reducing Fc receptor binding and/or effector function In certain aspects, provided is a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the bispecific antibody comprises a Fc domain comprising one or more amino acid modifications that reduce binding to an Fc receptor, in particular towards FcȖ receptor, and reduce or abolish effector function. In certain aspects, one or more amino acid modifications may be introduced into the Fc region of an antibody provided herein, thereby generating an Fc region variant. The Fc region variant may comprise a human Fc region sequence (e.g., a human IgG1, IgG2, IgG3 or IgG4 Fc region) comprising an amino acid modification (e.g., a substitution) at one or more amino acid positions. The following section describes preferred aspects of the bispecific antigen binding molecules of the invention comprising Fc domain modifications reducing Fc receptor binding and/or effector function. In one aspect, the invention relates to a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the Fc domain comprises one or more amino acid substitution that reduces binding to an Fc receptor, in particular towards FcȖ receptor. In particular, the Fc domain is of human IgG1 subclass with the amino acid mutations L234A, L235A and P329G (numbering according to Kabat EU index). The Fc domain confers favorable pharmacokinetic properties to the bispecific antibodies of the invention, including a long serum half-life which contributes to good accumulation in the target tissue and a favorable tissue-blood distribution ratio. At the same time it may, however, lead to undesirable targeting of the bispecific antibodies of the invention to cells expressing Fc receptors rather than to the preferred antigen-bearing cells. Accordingly, in particular embodiments the Fc domain of the the bispecific antibodies of the invention exhibits reduced binding affinity to an Fc receptor and/or reduced effector function, as compared to a native IgG Fc domain, in particular an IgG1 Fc domain or an IgG4 Fc domain. More particularly, the Fc domain is an IgG1 FC domain. In one such aspect the Fc domain (or the bispecific antigen binding molecule of the invention comprising said Fc domain) exhibits less than 50%, preferably less than 20%, more preferably less than 10% and most preferably less than 5% of the binding affinity to an Fc receptor, as compared to a native IgG1 Fc domain (or the bispecific antigen binding molecule of the invention comprising a native IgG1 Fc domain), and/or less than 50%, preferably less than 20%, more preferably less than 10% and most preferably less than 5% of the effector function, as compared to a native IgG1 Fc domain (or the bispecific antigen binding molecule of the invention comprising a native IgG1 Fc domain). In one aspect, the Fc domain (or the bispecific antigen binding molecule of the invention comprising said Fc domain) does not substantially bind to an Fc receptor and/or induce effector function. In a particular aspect the Fc receptor PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO is an FcȖ receptor. In one aspect, the Fc receptor is a human Fc receptor. In one aspect, the Fc receptor is an activating Fc receptor. In a specific aspect, the Fc receptor is an activating human FcȖ receptor, more specifically human FcȖRIIIa, FcȖRI or FcȖRIIa, most specifically human FcȖRIIIa. In one aspect, the Fc receptor is an inhibitory Fc receptor. In a specific aspect, the Fc receptor is an inhibitory human FcȖ receptor, more specifically human FcȖRIIB. In one aspect the effector function is one or more of CDC, ADCC, ADCP, and cytokine secretion. In a particular aspect, the effector function is ADCC. In one aspect, the Fc domain domain exhibits substantially similar binding affinity to neonatal Fc receptor (FcRn), as compared to a native IgG1 Fc domain. Substantially similar binding to FcRn is achieved when the Fc domain (or the the bispecific antigen binding molecule of the invention comprising said Fc domain) exhibits greater than about 70%, particularly greater than about 80%, more particularly greater than about 90% of the binding affinity of a native IgG1 Fc domain (or the the bispecific antigen binding molecule of the invention comprising a native IgG1 Fc domain) to FcRn. In a particular aspect, the Fc domain is engineered to have reduced binding affinity to an Fc receptor and/or reduced effector function, as compared to a non-engineered Fc domain. In a particular aspect, the Fc domain of the bispecific antigen binding molecule of the invention comprises one or more amino acid mutation that reduces the binding affinity of the Fc domain to an Fc receptor and/or effector function. Typically, the same one or more amino acid mutation is present in each of the two subunits of the Fc domain. In one aspect, the amino acid mutation reduces the binding affinity of the Fc domain to an Fc receptor. In another aspect, the amino acid mutation reduces the binding affinity of the Fc domain to an Fc receptor by at least 2-fold, at least 5-fold, or at least 10-fold. In one aspect, the bispecific antigen binding molecule of the invention comprising an engineered Fc domain exhibits less than 20%, particularly less than 10%, more particularly less than 5% of the binding affinity to an Fc receptor as compared to bispecific antibodies of the invention comprising a non-engineered Fc domain. In a particular aspect, the Fc receptor is an FcȖ receptor. In other aspects, the Fc receptor is a human Fc receptor. In one aspect, the Fc receptor is an inhibitory Fc receptor. In a specific aspect, the Fc receptor is an inhibitory human FcȖ receptor, more specifically human FcȖRIIB. In some aspects the Fc receptor is an activating Fc receptor. In a specific aspect, the Fc receptor is an activating human FcȖ receptor, more specifically human FcȖRIIIa, FcȖRI or FcȖRIIa, most specifically human FcȖRIIIa. Preferably, binding to each of these receptors is reduced. In some aspects, binding affinity to a complement component, specifically binding affinity to C1q, is also reduced. In one aspect, binding affinity to neonatal Fc receptor (FcRn) is not reduced. Substantially similar binding to FcRn, i.e. preservation of the binding affinity of the Fc domain to said receptor, is achieved when the Fc domain (or the bispecific antigen binding molecule of the invention comprising said Fc domain) exhibits greater than about 70% of the binding affinity of a non-engineered form of the Fc domain (or the bispecific antigen binding molecule of the invention comprising said non- engineered form of the Fc domain) to FcRn. The Fc domain, or the the bispecific antigen binding molecule of the invention comprising said Fc domain, may exhibit greater than about 80% and even greater than about 90% of such affinity. In certain embodiments the Fc domain of the bispecific antigen binding molecule of the invention is engineered to have reduced effector function, as compared to a non- engineered Fc domain. The reduced effector function can include, but is not limited to, one or more of the following: reduced complement dependent cytotoxicity (CDC), reduced antibody-dependent cell-mediated PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO cytotoxicity (ADCC), reduced antibody-dependent cellular phagocytosis (ADCP), reduced cytokine secretion, reduced immune complex-mediated antigen uptake by antigen-presenting cells, reduced binding to NK cells, reduced binding to macrophages, reduced binding to monocytes, reduced binding to polymorphonuclear cells, reduced direct signaling inducing apoptosis, reduced dendritic cell maturation, or reduced T cell priming. Antibodies with reduced effector function include those with substitution of one or more of Fc region residues 238, 265, 269, 270, 297, 327 and 329 (U.S. Patent No.6,737,056). Such Fc mutants include Fc mutants with substitutions at two or more of amino acid positions 265, 269, 270, 297 and 327, including the so-called “DANA” Fc mutant with substitution of residues 265 and 297 to alanine (US Patent No.7,332,581). Certain antibody variants with improved or diminished binding to FcRs are described. (e.g. U.S. Patent No.6,737,056; WO 2004/056312, and Shields, R.L. et al., J. Biol. Chem.276 (2001) 6591-6604). In one aspect of the invention, the Fc domain comprises an amino acid substitution at a position of E233, L234, L235, N297, P331 and P329. In some aspects, the Fc domain comprises the amino acid substitutions L234A and L235A (“LALA”). In one such embodiment, the Fc domain is an IgG1 Fc domain, particularly a human IgG1 Fc domain. In one aspect, the Fc domain comprises an amino acid substitution at position P329. In a more specific aspect, the amino acid substitution is P329A or P329G, particularly P329G. In one embodiment the Fc domain comprises an amino acid substitution at position P329 and a further amino acid substitution selected from the group consisting of E233P, L234A, L235A, L235E, N297A, N297D or P331S. In more particular embodiments the Fc domain comprises the amino acid mutations L234A, L235A and P329G (“P329G LALA”). The “P329G LALA” combination of amino acid substitutions almost completely abolishes FcȖ receptor binding of a human IgG1 Fc domain, as described in PCT Patent Application No. WO 2012/130831 A1. Said document also describes methods of preparing such mutant Fc domains and methods for determining its properties such as Fc receptor binding or effector functions. Such antibody is an IgG1 with mutations L234A and L235A or with mutations L234A, L235A and P329G (numbering according to EU index of Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, MD, 1991). In one aspect, the bispecific antibody of the invention comprises (all positions according to EU index of Kabat) (i) a homodimeric Fc-region of the human IgG1 subclass optionally with the mutations P329G, L234A and L235A, or (ii) a homodimeric Fc-region of the human IgG4 subclass optionally with the mutations P329G, S228P and L235E, or (iii) a homodimeric Fc-region of the human IgG1 subclass optionally with the mutations P329G, L234A, L235A, I253A, H310A, and H435A, or optionally with the mutations P329G, L234A, L235A, H310A, H433A, and Y436A, or (iv) a heterodimeric Fc-region wherein one Fc-region polypeptide comprises the mutation T366W, and the other Fc-region polypeptide comprises the mutations T366S, L368A and Y407V, or wherein one Fc-region polypeptide comprises the mutations T366W and Y349C, and the other Fc-region polypeptide comprises the mutations T366S, L368A, Y407V, and S354C, or wherein one Fc-region polypeptide comprises the mutations T366W and S354C, and the other Fc-region polypeptide comprises the mutations T366S, L368A, Y407V and Y349C, or (v) a heterodimeric Fc-region of the human IgG1 subclass wherein both Fc-region polypeptides comprise the mutations P329G, L234A and L235A and one Fc-region polypeptide comprises the mutation T366W, and PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO the other Fc-region polypeptide comprises the mutations T366S, L368A and Y407V, or wherein one Fc- region polypeptide comprises the mutations T366W and Y349C, and the other Fc-region polypeptide comprises the mutations T366S, L368A, Y407V, and S354C, or wherein one Fc-region polypeptide comprises the mutations T366W and S354C, and the other Fc-region polypeptide comprises the mutations T366S, L368A, Y407V and Y349C. In one aspect, the Fc domain is an IgG4 Fc domain. In a more specific embodiment, the Fc domain is an IgG4 Fc domain comprising an amino acid substitution at position S228 (Kabat numbering), particularly the amino acid substitution S228P. In a more specific embodiment, the Fc domain is an IgG4 Fc domain comprising amino acid substitutions L235E and S228P and P329G. This amino acid substitution reduces in vivo Fab arm exchange of IgG4 antibodies (see Stubenrauch et al., Drug Metabolism and Disposition 38, 84-91 (2010)). Thus, in one aspect, provided is a bispecific antibody, comprising (all positions according to EU index of Kabat) a heterodimeric Fc-region of the human IgG4 subclass wherein both Fc-region polypeptides comprise the mutations P329G, S228P and L235E and one Fc-region polypeptide comprises the mutation T366W, and the other Fc-region polypeptide comprises the mutations T366S, L368A and Y407V, or wherein one Fc-region polypeptide comprises the mutations T366W and Y349C, and the other Fc-region polypeptide comprises the mutations T366S, L368A, Y407V, and S354C, or wherein one Fc-region polypeptide comprises the mutations T366W and S354C, and the other Fc-region polypeptide comprises the mutations T366S, L368A, Y407V and Y349C. Antibodies with increased half lives and improved binding to the neonatal Fc receptor (FcRn), which is responsible for the transfer of maternal IgGs to the fetus (Guyer, R.L. et al., J. Immunol.117 (1976) 587-593, and Kim, J.K. et al., J. Immunol.24 (1994) 2429-2434), are described in US 2005/0014934. Those antibodies comprise an Fc region with one or more substitutions therein which improve binding of the Fc region to FcRn. Such Fc variants include those with substitutions at one or more of Fc region residues: 238, 256, 265, 272, 286, 303, 305, 307, 311, 312, 317, 340, 356, 360, 362, 376, 378, 380, 382, 413, 424 or 434, e.g., substitution of Fc region residue 434 (US Patent No.7,371,826). See also Duncan, A.R. and Winter, G., Nature 322 (1988) 738-740; US 5,648,260; US 5,624,821; and WO 94/29351 concerning other examples of Fc region variants. Binding to Fc receptors can be easily determined, e.g., by ELISA, or by Surface Plasmon Resonance (SPR) using standard instrumentation such as a BIAcore instrument (GE Healthcare), and Fc receptors such as may be obtained by recombinant expression. A suitable such binding assay is described herein. Alternatively, binding affinity of Fc domains or cell activating bispecific antigen binding molecules comprising an Fc domain for Fc receptors may be evaluated using cell lines known to express particular Fc receptors, such as human NK cells expressing FcȖIIIa receptor. Effector function of an Fc domain, or bispecific antibodies of the invention comprising an Fc domain, can be measured by methods known in the art. A suitable assay for measuring ADCC is described herein. Other examples of in vitro assays to assess ADCC activity of a molecule of interest are described in U.S. Patent No.5,500,362; Hellstrom et al. Proc Natl Acad Sci USA 83, 7059-7063 (1986) and Hellstrom et al., Proc Natl Acad Sci USA 82, 1499-1502 (1985); U.S. Patent No.5,821,337; Bruggemann et al., J Exp Med 166, 1351-1361 (1987). Alternatively, non-radioactive assays methods may be employed (see, for example, ACTI™ non- radioactive cytotoxicity assay for flow cytometry (CellTechnology, Inc. Mountain View, CA); and CytoTox PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 96^® non-radioactive cytotoxicity assay (Promega, Madison, WI)). Useful effector cells for such assays include peripheral blood mononuclear cells (PBMC) and Natural Killer (NK) cells. Alternatively, or additionally, ADCC activity of the molecule of interest may be assessed in vivo, e.g. in an animal model such as that disclosed in Clynes et al., Proc Natl Acad Sci USA 95, 652-656 (1998). The following section describes preferred aspects of the bispecific antibodies of the invention comprising Fc domain modifications reducing Fc receptor binding and/or effector function. In one aspect, the invention relates to the bispecific comprising a first antigen-binding domain that specifically binds PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the Fc domain comprises one or more amino acid substitution that reduces the binding affinity of the antibody to an Fc receptor, in particular towards FcȖ receptor. In another aspect, the invention relates to the bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the Fc domain comprises one or more amino acid substitution that reduces effector function. In particular aspect, the Fc domain is of human IgG1 subclass with the amino acid mutations L234A, L235A and P329G (numbering according to Kabat EU index). ii. Fc domain modifications promoting heterodimerization The bispecific antigen binding molecules of the invention comprise different antigen-binding domains, fused to one or the other of the two subunits of the Fc domain, thus the two subunits of the Fc domain may be comprised in two non-identical polypeptide chains. Recombinant co-expression of these polypeptides and subsequent dimerization leads to several possible combinations of the two polypeptides. To improve the yield and purity of the bispecific antibodies of the invention in recombinant production, it will thus be advantageous to introduce in the Fc domain of the bispecific antigen binding molecules of the invention a modification promoting the association of the desired polypeptides. Accordingly, in particular aspects the invention relates to a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3, wherein the Fc domain comprises a modification promoting the association of the first and second subunit of the Fc domain. The site of most extensive protein-protein interaction between the two subunits of a human IgG Fc domain is in the CH3 domain of the Fc domain. Thus, in one aspect said modification is in the CH3 domain of the Fc domain. In a specific aspect said modification is a so-called “knob-into-hole” modification, comprising a “knob” modification in one of the two subunits of the Fc domain and a “hole” modification in the other one of the two subunits of the Fc domain. Thus, the invention relates to a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding site that specifically binds to LAG3, wherein the first subunit of the Fc domain comprises knobs and the second subunit of the Fc domain comprises holes according to the knobs into holes method. In a particular aspect, the first subunit of the Fc domain comprises the amino acid substitutions S354C and T366W (EU numbering) and the second subunit of the Fc domain comprises the amino acid substitutions Y349C, T366S and Y407V (numbering according to Kabat EU index). The knob-into-hole technology is described e.g., in US 5,731,168; US 7,695,936; Ridgway et al., Prot Eng 9, 617-621 (1996) and Carter, J Immunol Meth 248, 7-15 (2001). Generally, the method involves PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO introducing a protuberance (“knob”) at the interface of a first polypeptide and a corresponding cavity (“hole”) in the interface of a second polypeptide, such that the protuberance can be positioned in the cavity so as to promote heterodimer formation and hinder homodimer formation. Protuberances are constructed by replacing small amino acid side chains from the interface of the first polypeptide with larger side chains (e.g., tyrosine or tryptophan). Compensatory cavities of identical or similar size to the protuberances are created in the interface of the second polypeptide by replacing large amino acid side chains with smaller ones (e.g., alanine or threonine). Accordingly, in one aspect, in the CH3 domain of the first subunit of the Fc domain of the bispecific antigen binding molecules of the invention an amino acid residue is replaced with an amino acid residue having a larger side chain volume, thereby generating a protuberance within the CH3 domain of the first subunit which is positionable in a cavity within the CH3 domain of the second subunit, and in the CH3 domain of the second subunit of the Fc domain an amino acid residue is replaced with an amino acid residue having a smaller side chain volume, thereby generating a cavity within the CH3 domain of the second subunit within which the protuberance within the CH3 domain of the first subunit is positionable. The protuberance and cavity can be made by altering the nucleic acid encoding the polypeptides, e.g., by site-specific mutagenesis, or by peptide synthesis. In a specific aspect, in the CH3 domain of the first subunit of the Fc domain the threonine residue at position 366 is replaced with a tryptophan residue (T366W), and in the CH3 domain of the second subunit of the Fc domain the tyrosine residue at position 407 is replaced with a valine residue (Y407V). In one aspect, in the second subunit of the Fc domain additionally the threonine residue at position 366 is replaced with a serine residue (T366S) and the leucine residue at position 368 is replaced with an alanine residue (L368A). In yet a further aspect, in the first subunit of the Fc domain additionally the serine residue at position 354 is replaced with a cysteine residue (S354C), and in the second subunit of the Fc domain additionally the tyrosine residue at position 349 is replaced by a cysteine residue (Y349C). Introduction of these two cysteine residues leads to the formation of a disulfide bridge between the two subunits of the Fc domain, further stabilizing the dimer (Carter (2001), J Immunol Methods 248, 7-15). In a particular aspect, the first subunit of the Fc domain comprises the amino acid substitutions S354C and T366W (EU numbering) and the second subunit of the Fc domain comprises the amino acid substitutions Y349C, T366S and Y407V (numbering according to Kabat EU index). But also other knobs-in-holes technologies as described by EP 1870459, can be used alternatively or additionally. In one embodiment the multispecific antibody comprises the mutations R409D and K370E in the CH3 domain of the “knobs chain” and the mutations D399K and E357K in the CH3 domain of the “hole-chain” (numbering according to Kabat EU index). In one aspect, the bispecific antibody comprises a T366W mutation in the CH3 domain of the “knobs chain” and the mutations T366S, L368A and Y407V in the CH3 domain of the “hole chain” and additionally the mutations R409D and K370E in the CH3 domain of the “knobs chain” and the mutations D399K and E357K in the CH3 domain of the “hole chain” (numbering according to the Kabat EU index). In one aspect, the bispecific antibody comprises the mutations Y349C and T366W in one of the two CH3 domains and the mutations S354C, T366S, L368A and Y407V in the other of the two CH3 domains, or the multispecific antibody comprises the mutations Y349C and T366W in one of the two CH3 PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO domains and the mutations S354C, T366S, L368A and Y407V in the other of the two CH3 domains and additionally the mutations R409D and K370E in the CH3 domain of the “knobs chain” and the mutations D399K and E357K in the CH3 domain of the “hole chain” (numbering according to the Kabat EU index). In an alternative aspect, a modification promoting association of the first and the second subunit of the Fc domain comprises a modification mediating electrostatic steering effects, e.g., as described in PCT publication WO 2009/089004. Generally, this method involves replacement of one or more amino acid residues at the interface of the two Fc domain subunits by charged amino acid residues so that homodimer formation becomes electrostatically unfavorable but heterodimerization electrostatically favorable. Apart from the “knob-into-hole technology” other techniques for modifying the CH3 domains of the heavy chains of a multispecific antibody to enforce heterodimerization are known in the art. These technologies, especially the ones described in WO 96/27011, WO 98/050431, EP 1870459, WO 2007/110205, WO 2007/147901, WO 2009/089004, WO 2010/129304, WO 2011/90754, WO 2011/143545, WO 2012/058768, WO 2013/157954 and WO 2013/096291 are contemplated herein as alternatives to the “knob-into-hole technology” in combination with a bispecific antibody. In one aspect, in the bispecific antibody the approach described in EP 1870459 is used to support heterodimerization of the first heavy chain and the second heavy chain of the multispecific antibody. This approach is based on the introduction of charged amino acids with opposite charges at specific amino acid positions in the CH3/CH3-domain-interface between both, the first and the second heavy chain. Accordingly, in this aspect in the tertiary structure of the multispecific antibody the CH3 domain of the first heavy chain and the CH3 domain of the second heavy chain form an interface that is located between the respective antibody CH3 domains, wherein the respective amino acid sequences of the CH3 domain of the first heavy chain and the amino acid sequence of the CH3 domain of the second heavy chain each comprise a set of amino acids that is located within said interface in the tertiary structure of the antibody, wherein from the set of amino acids that is located in the interface in the CH3 domain of one heavy chain a first amino acid is substituted by a positively charged amino acid and from the set of amino acids that is located in the interface in the CH3 domain of the other heavy chain a second amino acid is substituted by a negatively charged amino acid. The bispecific antibody according to this aspect is herein also referred to as “CH3(+/-)-engineered bispecific antibody” (wherein the abbreviation “+/-” stands for the oppositely charged amino acids that were introduced in the respective CH3 domains). In one aspect, in the CH3(+/-)-engineered bispecific antibody the positively charged amino acid is selected from K, R and H, and the negatively charged amino acid is selected from E or D. In one aspect, in the CH3(+/-)-engineered bispecific antibody the positively charged amino acid is selected from K and R, and the negatively charged amino acid is selected from E or D. In one aspect, in the CH3(+/-)-engineered bispecific antibody the positively charged amino acid is K, and the negatively charged amino acid is E. In one aspect, in the CH3(+/-)-engineered bispecific antibody in the CH3 domain of one heavy chain the amino acid R at position 409 is substituted by D and the amino acid K at position is substituted by E, and in the CH3 domain of the other heavy chain the amino acid D at position 399 is substituted by K and the amino acid E at position 357 is substituted by K (numbering according to Kabat EU index). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In one aspect, the approach described in WO 2013/157953 is used to support heterodimerization of the first heavy chain and the second heavy chain of the multispecific antibody. In one embodiment in the CH3 domain of one heavy chain the amino acid T at position 366 is substituted by K, and in the CH3 domain of the other heavy chain the amino acid L at position 351 is substituted by D (numbering according to Kabat EU index). In another embodiment in the CH3 domain of one heavy chain the amino acid T at position 366 is substituted by K and the amino acid L at position 351 is substituted by K, and in the CH3 domain of the other heavy chain the amino acid L at position 351 is substituted by D (numbering according to Kabat EU index). In another aspect, in the CH3 domain of one heavy chain the amino acid T at position 366 is substituted by K and the amino acid L at position 351 is substituted by K, and in the CH3 domain of the other heavy chain the amino acid L at position 351 is substituted by D (numbering according to Kabat EU index). Additionally at least one of the following substitutions is comprised in the CH3 domain of the other heavy chain: the amino acid Y at position 349 is substituted by E, the amino acid Y at position 349 is substituted by D and the amino acid L at position 368 is substituted by E (numbering according to Kabat EU index). In one embodiment the amino acid L at position 368 is substituted by E (numbering according to Kabat EU index). In one aspect, the approach described in WO 2012/058768 is used to support heterodimerization of the first heavy chain and the second heavy chain of the multispecific antibody. In one aspect, in the CH3 domain of one heavy chain the amino acid L at position 351 is substituted by Y and the amino acid Y at position 407 is substituted by A, and in the CH3 domain of the other heavy chain the amino acid T at position 366 is substituted by A and the amino acid K at position 409 is substituted by F (numbering according to Kabat EU index). In another embodiment, in addition to the aforementioned substitutions, in the CH3 domain of the other heavy chain at least one of the amino acids at positions 411 (originally T), 399 (originally D), 400 (originally S), 405 (originally F), 390 (originally N) and 392 (originally K) is substituted (numbering according to Kabat EU index). Preferred substitutions are: - substituting the amino acid T at position 411 by an amino acid selected from N, R, Q, K, D, E and W (numbering according to Kabat EU index), - substituting the amino acid D at position 399 by an amino acid selected from R, W, Y, and K (numbering according to Kabat EU index), - substituting the amino acid S at position 400 by an amino acid selected from E, D, R and K (numbering according to Kabat EU index), - substituting the amino acid F at position 405 by an amino acid selected from I, M, T, S, V and W (numbering according to Kabat EU index; - substituting the amino acid N at position 390 by an amino acid selected from R, K and D (numbering according to Kabat EU index; and - substituting the amino acid K at position 392 by an amino acid selected from V, M, R, L, F and E (numbering according to Kabat EU index). In another aspect, the bispecific antibody is engineered according to WO 2012/058768), i.e. in the CH3 domain of one heavy chain the amino acid L at position 351 is substituted by Y and the amino acid Y at position 407 is substituted by A, and in the CH3 domain of the other heavy chain the amino acid T at PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO position 366 is substituted by V and the amino acid K at position 409 is substituted by F (numbering according to Kabat EU index). In another embodiment of the multispecific antibody, in the CH3 domain of one heavy chain the amino acid Y at position 407 is substituted by A, and in the CH3 domain of the other heavy chain the amino acid T at position 366 is substituted by A and the amino acid K at position 409 is substituted by F (numbering according to Kabat EU index). In the last aforementioned embodiment, in the CH3 domain of the other heavy chain the amino acid K at position 392 is substituted by E, the amino acid T at position 411 is substituted by E, the amino acid D at position 399 is substituted by R and the amino acid S at position 400 is substituted by R (numbering according to Kabat EU index). In one aspect, the approach described in WO 2011/143545 is used to support heterodimerization of the first heavy chain and the second heavy chain of the multispecific antibody. In one aspect, amino acid modifications in the CH3 domains of both heavy chains are introduced at positions 368 and/or 409 (numbering according to Kabat EU index). In one aspect, the approach described in WO 2011/090762 is used to support heterodimerization of the first heavy chain and the second heavy chain of the bispecific antibody. WO 2011/090762 relates to amino acid modifications according to the “knob-into-hole” (KiH) technology. In one embodiment in the CH3 domain of one heavy chain the amino acid T at position 366 is substituted by W, and in the CH3 domain of the other heavy chain the amino acid Y at position 407 is substituted by A (numbering according to Kabat EU index). In another embodiment in the CH3 domain of one heavy chain the amino acid T at position 366 is substituted by Y, and in the CH3 domain of the other heavy chain the amino acid Y at position 407 is substituted by T (numbering according to Kabat EU index). In one aspect, the approach described in WO 2009/089004 is used to support heterodimerization of the first heavy chain and the second heavy chain of the bispecific antibody. In one embodiment in the CH3 domain of one heavy chain the amino acid K or N at position 392 is substituted by a negatively charged amino acid (in one embodiment by E or D, in one preferred embodiment by D), and in the CH3 domain of the other heavy chain the amino acid D at position 399 the amino acid E or D at position 356 or the amino acid E at position 357 is substituted by a positively charged amino acid (in one embodiment K or R, in one preferred embodiment by K, in one preferred embodiment the amino acids at positions 399 or 356 are substituted by K) (numbering according to Kabat EU index). In one further embodiment, in addition to the aforementioned substitutions, in the CH3 domain of the one heavy chain the amino acid K or R at position 409 is substituted by a negatively charged amino acid (in one embodiment by E or D, in one preferred embodiment by D) (numbering according to Kabat EU index). In one even further aspect, in addition to or alternatively to the aforementioned substitutions, in the CH3 domain of the one heavy chain the amino acid K at position 439 and/or the amino acid K at position 370 is substituted independently from each other by a negatively charged amino acid (in one embodiment by E or D, in one preferred embodiment by D) (numbering according to Kabat EU index). In one aspect, the approach described in WO 2007/147901 is used to support heterodimerization of the first heavy chain and the second heavy chain of the multispecific antibody. In one embodiment in the CH3 domain of one heavy chain the amino acid K at position 253 is substituted by E, the amino acid D at position 282 is substituted by K and the amino acid K at position 322 is substituted by D, and in the CH3 domain of the other heavy chain the amino acid D at position 239 is substituted by K, the amino acid PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO E at position 240 is substituted by K and the amino acid K at position 292 is substituted by D (numbering according to Kabat EU index). The C-terminus of the heavy chain of the bispecific antibody as reported herein can be a complete C-terminus ending with the amino acid residues PGK. The C-terminus of the heavy chain can be a shortened C-terminus in which one or two of the C terminal amino acid residues have been removed. In one preferred aspect, the C-terminus of the heavy chain is a shortened C-terminus ending PG. In one aspect of all aspects as reported herein, a bispecific antibody comprising a heavy chain including a C-terminal CH3 domain as specified herein, comprises the C-terminal glycine-lysine dipeptide (G446 and K447, numbering according to Kabat EU index). In one embodiment of all aspects as reported herein, a bispecific antibody comprising a heavy chain including a C-terminal CH3 domain, as specified herein, comprises a C-terminal glycine residue (G446, numbering according to Kabat EU index). iii. Modifications in the Fab domains In one aspect, the invention relates to a bispecific antibody comprising a first Fab fragment that specifically binds to PD-1 and a second Fab fragment that specifically binds to LAG3, wherein in one of the Fab fragments either the variable domains VH and VL or the constant domains CH1 and CL are exchanged. The bispecific antibodies are prepared according to the Crossmab technology. Multispecific antibodies with a domain replacement/exchange in one binding arm (CrossMabVH- VL or CrossMabCH-CL) are described in detail in WO2009/080252, WO2009/080253 and Schaefer, W. et al, PNAS, 108 (2011) 11187-1191. They clearly reduce the byproducts caused by the mismatch of a light chain against a first antigen with the wrong heavy chain against the second antigen (compared to approaches without such domain exchange). In a particular aspect, the invention relates to a bispecific antibody comprising a first Fab fragment that specifically binds to PD-1 and a second Fab fragment that specifically binds to LAG3, wherein in one of the Fab fragments the variable domains VL and VH are replaced by each other so that the VH domain is part of the light chain and the VL domain is part of the heavy chain. In a particular aspect, the bispecific antibody is one, wherein in the first Fab fragment comprising the antigen-binding domain that specifically binds to PD-1 the variable domains VL and VH are replaced by each other. In another aspect, and to further improve correct pairing, the bispecific antibody comprising a first Fab fragment that specifically binds to PD-1 and a second Fab fragment that specifically binds to LAG3, can contain different charged amino acid substitutions (so-called “charged residues”). These modifications are introduced in the crossed or non-crossed CH1 and CL domains. Such modifiactions are described e.g., in WO2015/150447, WO2016/020309 and PCT/EP2016/073408. In a particular aspect, the invention is concerned with a bispecific antibody comprising a first Fab fragment that specifically binds to PD-1 and a second Fab fragment that specifically binds to LAG3, wherein in one of the Fab fragments in the constant domain CL the amino acid at position 124 is substituted independently by lysine (K), arginine (R) or histidine (H) (numbering according to Kabat EU Index), and in the constant domain CH1 the amino acids at positions 147 and 213 are substituted independently by glutamic acid (E) or aspartic acid (D) (numbering according to Kabat EU index). In a particular aspect, the bispecific antibody is one, wherein in the second Fab fragment comprising the PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO antigen-binding domain that specifically binds to TIM3 the constant domain CL the amino acid at position 124 is substituted independently by lysine (K), arginine (R) or histidine (H) (numbering according to Kabat EU Index), and in the constant domain CH1 the amino acids at positions 147 and 213 are substituted independently by glutamic acid (E) or aspartic acid (D) (numbering according to Kabat EU index). In a particular aspect, the invention relates to a bispecific antibody comprising a first Fab fragment that specifically binds to PD-1 and a second Fab fragment that specifically binds to LAG3, wherein in one of CL domains the amino acid at position 123 (EU numbering) has been replaced by arginine (R) and the amino acid at position 124 (EU numbering) has been substituted by lysine (K) and wherein in one of the CH1 domains the amino acids at position 147 (EU numbering) and at position 213 (EU numbering) have been substituted by glutamic acid (E). In a particular aspect, the bispecific antibody is one, wherein in the second Fab fragment comprising the antigen-binding domain that specifically binds to LAG3 the amino acid at position 123 (EU numbering) has been replaced by arginine (R) and the amino acid at position 124 (EU numbering) has been substituted by lysine (K) and wherein in one of the CH1 domains the amino acids at position 147 (EU numbering) and at position 213 (EU numbering) have been substituted by glutamic acid (E). In a further aspect, the bispecific antibody is a bivalent antibody comprising a) a first light chain and a first heavy chain of an antibody specifically binding to a first antigen, and b) a second light chain and a second heavy chain of an antibody specifically binding to a second antigen, wherein the variable domains VL and VH of the second light chain and the second heavy chain are replaced by each other. The antibody under a) does not contain a modification as reported under b) and the heavy chain and the light chain under a) are isolated chains. In the antibody under b) within the light chain the variable light chain domain VL is replaced by the variable heavy chain domain VH of said antibody, and within the heavy chain the variable heavy chain domain VH is replaced by the variable light chain domain VL of said antibody. In one aspect, (i) in the constant domain CL of the first light chain under a) the amino acid at position 124 (numbering according to Kabat) is substituted by a positively charged amino acid, and wherein in the constant domain CH1 of the first heavy chain under a) the amino acid at position 147 or the amino acid at position 213 (numbering according to Kabat EU index) is substituted by a negatively charged amino acid, or (ii) in the constant domain CL of the second light chain under b) the amino acid at position 124 (numbering according to Kabat) is substituted by a positively charged amino acid, and wherein in the constant domain CH1 of the second heavy chain under b) the amino acid at position 147 or the amino acid at position 213 (numbering according to Kabat EU index) is substituted by a negatively charged amino acid. In another aspect, (i) in the constant domain CL of the first light chain under a) the amino acid at position 124 is substituted independently by lysine (K), arginine (R) or histidine (H) (numbering according to Kabat) (in one preferred embodiment independently by lysine (K) or arginine (R)), and wherein in the constant domain CH1 of the first heavy chain under a) the amino acid at position 147 or the amino acid at position 213 is substituted independently by glutamic acid (E) or aspartic acid (D) (numbering according to Kabat EU index), or (ii) in the constant domain CL of the second light chain under b) the amino acid at PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO position 124 is substituted independently by lysine (K), arginine (R) or histidine (H) (numbering according to Kabat) (in one preferred embodiment independently by lysine (K) or arginine (R)), and wherein in the constant domain CH1 of the second heavy chain under b) the amino acid at position 147 or the amino acid at position 213 is substituted independently by glutamic acid (E) or aspartic acid (D) (numbering according to Kabat EU index). In one aspect, in the constant domain CL of the second heavy chain the amino acids at position 124 and 123 are substituted by K (numbering according to Kabat EU index). In one aspect, in the constant domain CL of the second heavy chain the amino acid at position 123 is substituted by R and the amino acid as position 124 is substituted by K (numbering according to Kabat EU index). In one aspect, in the constant domain CH1 of the second light chain the amino acids at position 147 and 213 are substituted by E (numbering according to EU index of Kabat). In one aspect, in the constant domain CL of the first light chain the amino acids at position 124 and 123 are substituted by K, and in the constant domain CH1 of the first heavy chain the amino acids at position 147 and 213 are substituted by E (numbering according to Kabat EU index). In one aspect, in the constant domain CL of the first light chain the amino acid at position 123 is substituted by R and the amino acid at position 124 is substituted by K, and in the constant domain CH1 of the first heavy chain the amino acids at position 147 and 213 are both substituted by E (numbering according to Kabat EU index). In one aspect, in the constant domain CL of the second heavy chain the amino acids at position 124 and 123 are substituted by K, and wherein in the constant domain CH1 of the second light chain the amino acids at position 147 and 213 are substituted by E, and in the variable domain VL of the first light chain the amino acid at position 38 is substituted by K, in the variable domain VH of the first heavy chain the amino acid at position 39 is substituted by E, in the variable domain VL of the second heavy chain the amino acid at position 38 is substituted by K, and in the variable domain VH of the second light chain the amino acid at position 39 is substituted by E (numbering according to Kabat EU index). In one aspect, the bispecific antibody is a bivalent antibody comprising a) a first light chain and a first heavy chain of an antibody specifically binding to a first antigen, and b) a second light chain and a second heavy chain of an antibody specifically binding to a second antigen, wherein the variable domains VL and VH of the second light chain and the second heavy chain are replaced by each other, and wherein the constant domains CL and CH1 of the second light chain and the second heavy chain are replaced by each other. The antibody under a) does not contain a modification as reported under b) and the heavy chain and the light chain und a) are isolated chains. In the antibody under b) within the light chain the variable light chain domain VL is replaced by the variable heavy chain domain VH of said antibody, and the constant light chain domain CL is replaced by the constant heavy chain domain CH1 of said antibody; and within the heavy chain the variable heavy chain domain VH is replaced by the variable light chain domain VL of said antibody, and the constant heavy chain domain CH1 is replaced by the constant light chain domain CL of said antibody. In one aspect, the bispecific antibody is a bivalent antibody comprising PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO a) a first light chain and a first heavy chain of an antibody specifically binding to a first antigen, and b) a second light chain and a second heavy chain of an antibody specifically binding to a second antigen, wherein the constant domains CL and CH1 of the second light chain and the second heavy chain are replaced by each other. The antibody under a) does not contain a modification as reported under b) and the heavy chain and the light chain under a) are isolated chains. In the antibody under b) within the light chain the constant light chain domain CL is replaced by the constant heavy chain domain CH1of said antibody; and within the heavy chain the constant heavy chain domain CH1 is replaced by the constant light chain domain CL of said antibody. In one aspect, the bispecific antibody is a bispecific antibody comprising a) a full-length antibody specifically binding to a first antigen and consisting of two antibody heavy chains and two antibody light chains, and b) one, two, three or four single chain Fab fragments specifically binding to a second antigen, wherein said single chain Fab fragments under b) are fused to said full-length antibody under a) via a peptide linker at the C- or N- terminus of the heavy or light chain of said full length antibody. In one aspect, one or two identical single chain Fab fragments binding to a second antigen are fused to the full-length antibody via a peptide linker at the C terminus of the heavy or light chains of said full-length antibody. In one aspect, one or two identical single chain Fab (scFab) fragments binding to a second antigen are fused to the full-length antibody via a peptide linker at the C terminus of the heavy chains of said full-length antibody. In one aspect, one or two identical single chain Fab (scFab) fragments binding to a second antigen are fused to the full-length antibody via a peptide linker at the C terminus of the light chains of said full-length antibody. In one aspect, two identical single chain Fab (scFab) fragments binding to a second antigen are fused to the full-length antibody via a peptide linker at the C-terminus of each heavy or light chain of said full-length antibody. In one aspect, two identical single chain Fab (scFab) fragments binding to a second antigen are fused to the full-length antibody via a peptide linker at the C-terminus of each heavy chain of said full- length antibody. In one aspect, two identical single chain Fab (scFab) fragments binding to a second antigen are fused to the full-length antibody via a peptide linker at the C-terminus of each light chain of said full-length antibody. In one aspect, the bispecific antibody is a trivalent antibody comprising a) a full-length antibody specifically binding to a first antigen and consisting of two antibody heavy chains and two antibody light chains, b) a first polypeptide consisting of ba) an antibody heavy chain variable domain (VH), or bb) an antibody heavy chain variable domain (VH) and an antibody constant domain 1 (CH1), PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO wherein said first polypeptide is fused with the N-terminus of its VH domain via a peptidic linker to the C-terminus of one of the two heavy chains of said full-length antibody, c) a second polypeptide consisting of ca) an antibody light chain variable domain (VL), or cb) an antibody light chain variable domain (VL) and an antibody light chain constant domain (CL), wherein said second polypeptide is fused with the N-terminus of the VL domain via a peptide linker to the C-terminus of the other of the two heavy chains of said full-length antibody, and wherein the antibody heavy chain variable domain (VH) of the first polypeptide and the antibody light chain variable domain (VL) of the second polypeptide together form an antigen-binding domain specifically binding to a second antigen. In one aspect, the antibody heavy chain variable domain (VH) of the polypeptide under b) and the antibody light chain variable domain (VL) of the polypeptide under c) are linked and stabilized via an interchain disulfide bridge by introduction of a disulfide bond between the following positions: (i) heavy chain variable domain position 44 to light chain variable domain position 100, or (ii) heavy chain variable domain position 105 to light chain variable domain position 43, or (iii) heavy chain variable domain position 101 to light chain variable domain position 100 (numbering always according to Kabat EU index). Techniques to introduce unnatural disulfide bridges for stabilization are described e.g. in WO 94/029350, Rajagopal, V., et al., Prot. Eng. (1997) 1453-1459; Kobayashi, H., et al., Nucl. Med. Biol.25 (1998) 387-393; and Schmidt, M., et al., Oncogene 18 (1999) 1711-1721. In one embodiment the optional disulfide bond between the variable domains of the polypeptides under b) and c) is between heavy chain variable domain position 44 and light chain variable domain position 100. In one embodiment the optional disulfide bond between the variable domains of the polypeptides under b) and c) is between heavy chain variable domain position 105 and light chain variable domain position 43 (numbering always according to Kabat). In one embodiment a trivalent, bispecific antibody without said optional disulfide stabilization between the variable domains VH and VL of the single chain Fab fragments is preferred. In one aspect, the bispecific antibody is a trispecific or tetraspecific antibody, comprising a) a first light chain and a first heavy chain of a full-length antibody which specifically binds to a first antigen, and b) a second (modified) light chain and a second (modified) heavy chain of a full-length antibody which specifically binds to a second antigen, wherein the variable domains VL and VH are replaced by each other, and/or wherein the constant domains CL and CH1 are replaced by each other, and c) wherein one to four antigen-binding domains which specifically bind to one or two further antigens (i.e. to a third and/or fourth antigen) are fused via a peptide linker to the C- or N-terminus of the light chains or heavy chains of a) and/or b). The antibody under a) does not contain a modification as reported under b) and the heavy chain and the light chain und a) are isolated chains. In one aspect, the trispecific or tetraspecific antibody comprises under c) one or two antigen- binding domains which specifically bind to one or two further antigens. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In one aspect, the antigen-binding domains are selected from the group of a scFv fragment and a scFab fragment. In one aspect, the antigen-binding domains are scFv fragments. In one aspect, the antigen-binding domains are scFab fragments. In one aspect, the antigen-binding domains are fused to the C-terminus of the heavy chains of a) and/or b). In one aspect, the trispecific or tetraspecific antibody comprises under c) one or two antigen- binding domains which specifically bind to one further antigen. In one aspect, the trispecific or tetraspecific antibody comprises under c) two identical antigen- binding domains which specifically bind to a third antigen. In one preferred embodiment such two identical antigen-binding domains are fused both via the same peptidic linker to the C-terminus of the heavy chains of a) and b). In one preferred embodiment the two identical antigen-binding domains are either a scFv fragment or a scFab fragment. In one aspect, the trispecific or tetraspecific antibody comprises under c) two antigen-binding domains which specifically bind to a third and a fourth antigen. In one embodiment said two antigen- binding domains are fused both via the same peptide connector to the C-terminus of the heavy chains of a) and b). In one preferred embodiment said two antigen-binding domains are either a scFv fragment or a scFab fragment. In one aspect, the bispecific antibody is a bispecific, tetravalent antibody comprising a) two light chains and two heavy chains of an antibody, which specifically bind to a first antigen (and comprise two Fab fragments), b) two additional Fab fragments of an antibody, which specifically bind to a second antigen, wherein said additional Fab fragments are fused both via a peptidic linker either to the C- or N-termini of the heavy chains of a), and wherein in the Fab fragments the following modifications were performed (i) in both Fab fragments of a), or in both Fab fragments of b), the variable domains VL and VH are replaced by each other, and/or the constant domains CL and CH1 are replaced by each other, or (ii) in both Fab fragments of a) the variable domains VL and VH are replaced by each other, and the constant domains CL and CH1 are replaced by each other, and in both Fab fragments of b) the variable domains VL and VH are replaced by each other, or the constant domains CL and CH1 are replaced by each other, or (iii) in both Fab fragments of a) the variable domains VL and VH are replaced by each other, or the constant domains CL and CH1 are replaced by each other, and in both Fab fragments of b) the variable domains VL and VH are replaced by each other, and the constant domains CL and CH1 are replaced by each other, or (iv) in both Fab fragments of a) the variable domains VL and VH are replaced by each other, and in both Fab fragments of b) the constant domains CL and CH1 are replaced by each other, or (v) in both Fab fragments of a) the constant domains CL and CH1 are replaced by each other, and in both Fab fragments of b) the variable domains VL and VH are replaced by each other. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In one aspect, said additional Fab fragments are fused both via a peptidic linker either to the C- termini of the heavy chains of a), or to the N-termini of the heavy chains of a). In one aspect, said additional Fab fragments are fused both via a peptidic linker either to the C- termini of the heavy chains of a). In one aspect, said additional Fab fragments are fused both via a peptide linker to the N-termini of the heavy chains of a). In one aspect, in the Fab fragments the following modifications are performed: in both Fab fragments of a), or in both Fab fragments of b), the variable domains VL and VH are replaced by each other, and/or the constant domains CL and CH1 are replaced by each other. In one aspect, the bispecific antibody is a tetravalent antibody comprising: a) a (modified) heavy chain of a first antibody, which specifically binds to a first antigen and comprises a first VH-CH1 domain pair, wherein to the C terminus of said heavy chain the N-terminus of a second VH-CH1 domain pair of said first antibody is fused via a peptide linker, b) two light chains of said first antibody of a), c) a (modified) heavy chain of a second antibody, which specifically binds to a second antigen and comprises a first VH-CL domain pair, wherein to the C-terminus of said heavy chain the N-terminus of a second VH-CL domain pair of said second antibody is fused via a peptide linker, and d) two (modified) light chains of said second antibody of c), each comprising a CL-CH1 domain pair. In one aspect, the bispecific antibody comprises a) the heavy chain and the light chain of a first full-length antibody that specifically binds to a first antigen, and b) the heavy chain and the light chain of a second full-length antibody that specifically binds to a second antigen, wherein the N-terminus of the heavy chain is connected to the C-terminus of the light chain via a peptide linker. The antibody under a) does not contain a modification as reported under b) and the heavy chain and the light chain are isolated chains. In one aspect, the bispecific antibody comprises a) a full-length antibody specifically binding to a first antigen and consisting of two antibody heavy chains and two antibody light chains, and b) an Fv fragment specifically binding to a second antigen comprising a VH2 domain and a VL2 domain, wherein both domains are connected to each other via a disulfide bridge, wherein only either the VH2 domain or the VL2 domain is fused via a peptide linker to the heavy or light chain of the full-length antibody specifically binding to a first antigen. In the bispecific antibody the heavy chains and the light chains under a) are isolated chains. In one aspect, the other of the VH2 domain or the VL2 domain is not fused via a peptide linker to the heavy or light chain of the full-length antibody specifically binding to a first antigen. In all aspects as reported herein the first light chain comprises a VL domain and a CL domain and the first heavy chain comprises a VH domain, a CH1 domain, a hinge region, a CH2 domain and a CH3 domain. In one aspect, the bispecific antibody is a trivalent antibody comprising PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO a) two Fab fragments that specifically binds to a first antigen, b) one CrossFab fragment that specifically binds to a second antigen in which the CH1 and the CL domain are exchanged for each other, c) one Fc-region comprising a first Fc-region heavy chain and a second Fc region heavy chain, wherein the C-terminus of CH1 domains of the two Fab fragments are connected to the N-terminus of the heavy chain Fc-region polypeptides, and wherein the C-terminus of the CL domain of the CrossFab fragment is connected to the N-terminus of the VH domain of one of the Fab fragments. In one aspect, the bispecific antibody is a trivalent antibody comprising a) two Fab fragments that specifically binds to a first antigen, b) one CrossFab fragment that specifically binds to a second antigen in which the CH1 and the CL domain are exchanged for each other, c) one Fc-region comprising a first Fc-region heavy chain and a second Fc region heavy chain, wherein the C-terminus of CH1 domain of the first Fab fragment is connected to the N-terminus of one of the heavy chain Fc-region polypeptides and the C-terminus of the CL-domain of the CrossFab fragment is connected to the N-terminus of the other heavy chain Fc-region polypeptide, and wherein the C-terminus of the CH1 domain of the second Fab fragment is connected to the N-terminus of the VH domain of the first Fab fragment or to the N-terminus of the VH domain of the CrossFab fragment. In one aspect, the bispecific antibody comprises a) a full-length antibody specifically binding to a first antigen and consisting of two antibody heavy chains and two antibody light chains, and b) a Fab fragment specifically binding to a second antigen comprising a VH2 domain and a VL2 domain comprising a heavy chain fragment and a light chain fragment, wherein within the light chain fragment the variable light chain domain VL2 is replaced by the variable heavy chain domain VH2 of said antibody, and within the heavy chain fragment the variable heavy chain domain VH2 is replaced by the variable light chain domain VL2 of said antibody wherein the heavy chain Fab fragment is inserted between the CH1 domain of one of the heavy chains of the full-length antibody and the respective Fc-region of the full-length antibody, and the N- terminus of the light chain Fab fragment is conjugated to the C-terminus of the light chain of the full-length antibody that is paired with the heavy chain of the full-length antibody into which the heavy chain Fab fragment has been inserted. In one aspect, the bispecific antibody comprises a) a full-length antibody specifically binding to a first antigen and consisting of two antibody heavy chains and two antibody light chains, and b) a Fab fragment specifically binding to a second antigen comprising a VH2 domain and a VL2 domain comprising a heavy chain fragment and a light chain fragment, wherein within the light chain fragment the variable light chain domain VL2 is replaced by the variable heavy chain domain VH2 of said antibody, and within the heavy chain fragment the variable heavy chain domain VH2 is replaced by the variable light chain domain VL2 of said antibody and wherein the C-terminus of the heavy chain fragment of the Fab fragment is conjugated to the N-terminus of one of the heavy chains of the full-length antibody and the C-terminus of the light chain fragment of the Fab fragment is conjugated to the N-terminus of the PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO light chain of the full-length antibody that pairs with the heavy chain of the full-length antibody to which the heavy chain fragment of the Fab fragment is conjugated. B. Dosing of bispecific antibodies that bind to PD-1 and LAG3 For the prevention or treatment of disease, the appropriate dosage of a bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3 of the invention (when used alone or in combination with one or more other additional therapeutic agents) will depend on the type of disease to be treated, the route of administration, the body weight of the subject, the type of fusion protein, the severity and course of the disease, whether the bispecific antibody is administered for preventive or therapeutic purposes, previous or concurrent therapeutic interventions, the subject's clinical history and response to the fusion protein, and the discretion of the attending physician. The practitioner responsible for administration will, in any event, determine the concentration of active ingredient(s) in a composition and appropriate dose(s) for the individual subject. Various dosing schedules including but not limited to single or multiple administrations over various time-points, bolus administration, and pulse infusion are contemplated herein. The bispecific antibody comprising a first antigen-binding domain that specifically binds to PD-1 and a second antigen-binding domain that specifically binds to LAG3 as defined herein is suitably administered to the subject at one time or over a series of treatments. Depending on the type and severity of the disease, about 1 μg/kg to 15 mg/kg (e.g., 0.1 mg/kg – 10 mg/kg) of the bispecific antibody can be an initial candidate dosage for administration to the subject, whether, for example, by one or more separate administrations, or by continuous infusion. One typical daily dosage might range from about 1 μg/kg to 100 mg/kg or more, depending on the factors mentioned above. For repeated administrations over several days or longer, depending on the condition, the treatment would generally be sustained until a desired suppression of disease symptoms occurs. One exemplary dosage of the bispecific antibody would be in the range from about 0.005 mg/kg to about 10 mg/kg. In other examples, a dose may also comprise from about 1 ^g/kg body weight, about 5 ^g/kg body weight, about 10 ^g/kg body weight, about 50 ^g/kg body weight, about 100 ^g/kg body weight, about 200 ^g/kg body weight, about 350 ^g/kg body weight, about 500 ^g/kg body weight, about 1 mg/kg body weight, about 5 mg/kg body weight, about 10 mg/kg body weight, about 50 mg/kg body weight, about 100 mg/kg body weight, about 200 mg/kg body weight, about 350 mg/kg body weight, about 500 mg/kg body weight, to about 1000 mg/kg body weight or more per administration, and any range derivable therein. In examples of a derivable range from the numbers listed herein, a range of about 5 mg/kg body weight to about 100 mg/kg body weight, about 5 ^g/kg body weight to about 500 mg/kg body weight etc., can be administered, based on the numbers described above. Thus, one or more doses of about 0.5 mg/kg, 2.0 mg/kg, 5.0 mg/kg or 10 mg/kg (or any combination thereof) may be administered to the subject. Such doses may be administered intermittently, e.g. every week or every three weeks (e.g. such that the subject receives from about two to about twenty, or e.g. about six doses of the fusion protein). An initial higher loading dose, followed by one or more lower doses may be administered. However, other dosage regimens may be useful. The progress of this therapy is easily monitored by conventional techniques and assays. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO In some instances, the effective amount of the bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) is a fixed dose of between about 30 mg to about 1200 mg (e.g., between about 30 mg to about 1100 mg, e.g., between about 60 mg to about 1000 mg, e.g., between about 100 mg to about 900 mg, e.g., between about 200 mg to about 800 mg, e.g., between about 300 mg to about 800 mg, e.g., between about 400 mg to about 800 mg, e.g., between about 400 mg to about 750 mg, e.g., between about 450 mg to about 750 mg, e.g., between about 500 mg to about 700 mg, e.g., between about 550 mg to about 650 mg, e.g., 600 mg ± 10 mg, e.g., 600 ± 6 mg, e.g., 600 ± 5 mg, e.g., 600 ± 3 mg, e.g., 600 ± 1 mg, e.g., 600 ± 0.5 mg, e.g., 600 mg) every three weeks (Q3W). In some instances, the effective amount of the bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) is an intravenous fixed dose of about 600 mg every three weeks. In some instances, the effective amount of the bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) is an intravenous fixed dose of 600 mg every three weeks. VII. VEGF Antagonists Provided herein are methods for treating a cancer (e.g., HCC, e.g., resectable HCC) in a subject comprising administering to the subject a treatment regimen comprising an anti-TIGIT antagonist antibody (e.g., tiragolumab), a PD-1 axis binding antagonist (e.g., atezolizumab), and a VEGF antagonist (e.g., bevacizumab). Also provided are related compositions (e.g., pharmaceutical compositions) for use, kits, and articles of manufacture. Any of the methods, compositions for use, kits, or articles of manufacture described herein may include or involve any of the agents described below. VEGF antagonists include any molecule capable of binding VEGF, reducing VEGF expression levels, or neutralizing, blocking, inhibiting, abrogating, reducing, or interfering with VEGF biological activities. An exemplary human VEGF is shown under UniProtKB/Swiss-Prot Accession No. P15692, Gene ID (NCBI): 7422. In some instances, the VEGF antagonist is an anti-VEGF antibody. In some embodiments, the anti-VEGF antibody is bevacizumab, also known as “rhuMab VEGF” or “AVASTIN®.” Bevacizumab is a recombinant humanized anti-VEGF monoclonal antibody generated according to Presta et al. (Cancer Res.57:4593-4599, 1997). It comprises mutated human IgG1 framework regions and antigen-binding complementarity-determining regions from the murine anti-hVEGF monoclonal antibody A.4.6.1 that blocks binding of human VEGF to its receptors. Approximately 93% of the amino acid sequence of bevacizumab, including most of the framework regions, is derived from human IgG1, and about 7% of the sequence is derived from the murine antibody A4.6.1. Bevacizumab has a molecular mass of about 149,000 daltons and is glycosylated. Bevacizumab and other humanized anti-VEGF antibodies are further described in U.S. Pat. No.6,884,879, issued Feb.26, 2005, the entire disclosure of which is expressly incorporated herein by reference. Additional preferred antibodies include the G6 or B20 series antibodies (e.g., G6-31, B20-4.1), as described in PCT Application Publication No. WO 2005/012359. For additional preferred antibodies see U.S. Pat. Nos.7,060,269, 6,582,959, 6,703,020; 6,054,297; WO98/45332; WO 96/30046; WO94/10202; EP 0666868B1; U.S. Patent Application Publication Nos.2006009360, 20050186208, 20030206899, 20030190317, 20030203409, and 20050112126; and Popkov et al. (Journal of Immunological Methods PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 288:149-164, 2004). Other preferred antibodies include those that bind to a functional epitope on human VEGF comprising of residues F17, M18, D19, Y21, Y25, Q89, 191, K101, E103, and C104 or, alternatively, comprising residues F17, Y21, Q22, Y25, D63, 183, and Q89. In other instances, the VEGF antagonist is an anti-VEGFR2 antibody or related molecule (e.g., ramucirumab, tanibirumab, aflibercept); an anti-VEGFR1 antibody or related molecules (e.g., icrucumab, aflibercept (VEGF Trap-Eye; EYLEA®), or ziv-aflibercept (VEGF Trap; ZALTRAP®)); a bispecific VEGF antibody (e.g., MP-0250, vanucizumab (VEGF-ANG2), or bispecific antibodies disclosed in US 2001/0236388); a bispecific antibody including a combination of two of anti-VEGF, anti-VEGFR1, and anti-VEGFR2 arms; an anti-VEGFA antibody (e.g., bevacizumab, sevacizumab); an anti-VEGFB antibody; an anti-VEGFC antibody (e.g., VGX-100), an anti-VEGFD antibody; or a nonpeptide small molecule VEGF antagonist (e.g., pazopanib, axitinib, vandetanib, stivarga, cabozantinib, lenvatinib, nintedanib, orantinib, telatinib, dovitinib, cediranib, motesanib, sulfatinib, apatinib, foretinib, famitinib, or tivozanib). In some examples, the VEGF antagonist may be a tyrosine kinase inhibitor, including a receptor tyrosine kinase inhibitors (e.g., a multi-targeted receptor tyrosine kinase inhibitor such as sunitinib or axitinib). For the prevention or treatment of disease, the appropriate dosage of a VEGF antagonist of the invention (e.g., bevacizumab) (when used alone or in combination with one or more other additional therapeutic agents) will depend on the type of disease to be treated, the route of administration, the body weight of the subject, the type of fusion protein, the severity and course of the disease, whether the VEGF antagonist is administered for preventive or therapeutic purposes, previous or concurrent therapeutic interventions, the subject's clinical history and response to the VEGF antagonist, and the discretion of the attending physician. Various dosing schedules including but not limited to single or multiple administrations over various time-points, bolus administration, and pulse infusion are contemplated herein. The VEGF antagonist as defined herein is suitably administered to the subject at one time or over a series of treatments. Depending on the type and severity of the disease, about 5 mg/kg to 20 mg/kg of the bispecific antibody can be an initial candidate dosage for administration to the subject, whether, for example, by one or more separate administrations, or by continuous infusion. One typical daily dosage might range from about 5 mg/kg to 20 mg/kg, depending on the factors mentioned above. For example, the VEGF antagonist may be administered at a dose of about 5 mg/kg, 6 mg/kg, 7 mg/kg, 8 mg/kg, 9 mg/kg, 10 mg/kg, 11 mg/kg, 12 mg/kg, 13 mg/kg, 14 mg/kg, 15 mg/kg, 16 mg/kg, 17 mg/kg, 18 mg/kg, 19 mg/kg, or 20 mg/kg (e.g., at a dose of 5-10 mg/kg, 10-15 mg/kg, or 15-20 mg/kg). However, other dosage regimens may be useful. The progress of this therapy is easily monitored by conventional techniques and assays. In some instances, the effective amount of the VEGF antagonist (e.g., bevacizumab) is an intravenous dose of about 15 mg/kg every three weeks. In some instances, the effective amount of the VEGF antagonist (e.g., bevacizumab) is an intravenous dose of 15 mg/kg every three weeks. VIII. PHARMACEUTICAL COMPOSITIONS, FORMULATIONS, AND KITS Any of the anti-cancer agents described herein (e.g., a PD-1 axis binding antagonist (e.g., atezolizumab); a VEGF antagonist (e.g., bevacizumab); an anti-TIGIT antagonist antibody (e.g., PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO tiragolumab); and/or a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig)) can be used in pharmaceutical compositions and formulations. Pharmaceutical compositions and formulations of a PD-1 axis binding antagonist (e.g., atezolizumab); a VEGF antagonist (e.g., bevacizumab); an anti-TIGIT antagonist antibody (e.g., tiragolumab); and/or a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) can be prepared by mixing one, two, three, four, or more than four agents having the desired degree of purity with one or more optional pharmaceutically acceptable carriers (Remington’s Pharmaceutical Sciences 16th edition, Osol, A. Ed. (1980)), in the form of lyophilized formulations or aqueous solutions. Pharmaceutically acceptable carriers are generally nontoxic to recipients at the dosages and concentrations employed, and include, but are not limited to: buffers such as phosphate, citrate, and other organic acids; antioxidants including ascorbic acid and methionine; preservatives (such as octadecyldimethylbenzyl ammonium chloride; hexamethonium chloride; benzalkonium chloride; benzethonium chloride; phenol, butyl or benzyl alcohol; alkyl parabens such as methyl or propyl paraben; catechol; resorcinol; cyclohexanol; 3-pentanol; and m-cresol); low molecular weight (less than about 10 residues) polypeptides; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine, or lysine; monosaccharides, disaccharides, and other carbohydrates including glucose, mannose, or dextrins; chelating agents such as EDTA; sugars such as sucrose, mannitol, trehalose or sorbitol; salt-forming counter-ions such as sodium; metal complexes (e.g., Zn-protein complexes); and/or non-ionic surfactants such as polyethylene glycol (PEG). Exemplary pharmaceutically acceptable carriers herein further include insterstitial drug dispersion agents such as soluble neutral-active hyaluronidase glycoproteins (sHASEGP), for example, human soluble PH-20 hyaluronidase glycoproteins, such as rHuPH20 (HYLENEX^®, Baxter International, Inc.). Certain exemplary sHASEGPs and methods of use, including rHuPH20, are described in US Patent Publication Nos.2005/0260186 and 2006/0104968. In one aspect, a sHASEGP is combined with one or more additional glycosaminoglycanases such as chondroitinases. Exemplary lyophilized antibody formulations are described in U.S. Patent No.6,267,958. Aqueous antibody formulations include those described in US Patent No.6,171,586 and WO 2006/044908, the latter formulations including a histidine-acetate buffer. An exemplary atezolizumab formulation comprises glacial acetic acid, L-histidine, polysorbate 20, and sucrose, with a pH of 5.8. For example, atezolizumab may be provided in a 20 mL vial containing 1200 mg of atezolizumab that is formulated in glacial acetic acid (16.5 mg), L-histidine (62 mg), polysorbate 20 (8 mg), and sucrose (821.6 mg), with a pH of 5.8. In another example, atezolizumab may be provided in a 14 mL vial containing 840 mg of atezolizumab that is formulated in glacial acetic acid (11.5 mg), L-histidine (43.4 mg), polysorbate 20 (5.6 mg), and sucrose (575.1 mg) with a pH of 5.8. An exemplary tiragolumab formulation comprises a histidine solution containing polysorbate 20, sucrose, L-methionine, and WFI. Tiragolumab may be provided in a 15-mL vial containing 10 mL of tiragolumab drug product at an approximate concentration of tiragolumab antibody of 60 mg/mL. The formulation herein may also contain more than one active ingredients as necessary for the particular indication being treated, preferably those with complementary activities that do not adversely affect each other. For example, it may be desirable to further provide an additional therapeutic agent. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Such active ingredients are suitably present in combination in amounts that are effective for the purpose intended. Active ingredients may be entrapped in microcapsules prepared, for example, by coacervation techniques or by interfacial polymerization, for example, hydroxymethylcellulose or gelatin-microcapsules and poly-(methylmethacylate) microcapsules, respectively, in colloidal drug delivery systems (for example, liposomes, albumin microspheres, microemulsions, nano-particles and nanocapsules) or in macroemulsions. Such techniques are disclosed in Remington’s Pharmaceutical Sciences 16th edition, Osol, A. Ed. (1980). Sustained-release preparations may be prepared. Suitable examples of sustained-release preparations include semipermeable matrices of solid hydrophobic polymers containing the antibody, which matrices are in the form of shaped articles, for example, films, or microcapsules. The formulations to be used for in vivo administration are generally sterile. Sterility may be readily accomplished, e.g., by filtration through sterile filtration membranes. In some aspects, the invention provides kits that include (a) a PD-1 axis binding antagonist for use in combination with a VEGF antagonist, (b) a VEGF antagonist for use in combination with a PD-1 axis binding antagonist, or (c) a PD-1 axis binding antagonist and a VEGF antagonist for treating a subject having a cancer (e.g., a hepatocellular carcinoma (HCC), e.g., a resectable HCC) according to any of the methods described herein. In some instances, the article of manufacture or kit further comprises package insert comprising instructions for using (a) a PD-1 axis binding antagonist in combination with a VEGF antagonist, (b) a VEGF antagonist in combination with a PD-1 axis binding antagonist, or (c) a PD-1 axis binding antagonist and a VEGF antagonist to treat or delay progression of a cancer (e.g., a HCC, e.g., a resectable HCC) in a patient. Accordingly, in some aspects, the invention provides kits that include (a) atezolizumab for use in combination with bevacizumab, (b) bevacizumab for use in combination with atezolizumab, or (c) atezolizumab and bevacizumab for treating a subject having a cancer (e.g., a hepatocellular carcinoma (HCC), e.g., a resectable HCC) according to any of the methods described herein. In some instances, the article of manufacture or kit further comprises package insert comprising instructions for using (a) atezolizumab in combination with bevacizumab, (b) bevacizumab in combination with atezolizumab, or (c) atezolizumab and bevacizumab to treat or delay progression of a cancer (e.g., a HCC, e.g., a resectable HCC) in a patient. In some aspects, the invention provides kits that include (a) a PD-1 axis binding antagonist for use in combination with a VEGF antagonist and an anti-TIGIT antagonist antibody, (b) a VEGF antagonist for use in combination with a PD-1 axis binding antagonist and an anti-TIGIT antagonist antibody, (c) an anti-TIGIT antagonist antibody for use in combination with a PD-1 axis binding antagonist and a VEGF antagonist, or (d) a PD-1 axis binding antagonist, a VEGF antagonist, and an anti-TIGIT antagonist antibody for treating a subject having a cancer (e.g., a hepatocellular carcinoma (HCC), e.g., a resectable HCC) according to any of the methods described herein. In some instances, the article of manufacture or kit further comprises package insert comprising instructions for using (a) a PD-1 axis binding antagonist in combination with a VEGF antagonist and an anti-TIGIT antagonist antibody, (b) a VEGF antagonist in combination with a PD-1 axis binding antagonist and an anti-TIGIT antagonist antibody, (c) an anti-TIGIT PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO antagonist antibody in combination with a PD-1 axis binding antagonist and a VEGF antagonist, or (d) a PD-1 axis binding antagonist, a VEGF antagonist, and an anti-TIGIT antagonist antibody to treat or delay progression of a cancer (e.g., a HCC, e.g., a resectable HCC) in a patient. Accordingly, in some aspects, the invention provides kits that include (a) atezolizumab for use in combination with bevacizumab and tiragolumab, (b) bevacizumab for use in combination with atezolizumab and tiragolumab, (c) tiragolumab for use in combination with atezolizumab and bevacizumab, or (d) atezolizumab, bevacizumab, and tiragolumab for treating a subject having a cancer (e.g., a hepatocellular carcinoma (HCC), e.g., a resectable HCC) according to any of the methods described herein. In some instances, the article of manufacture or kit further comprises package insert comprising instructions for using (a) atezolizumab in combination with bevacizumab and tiragolumab, (b) bevacizumab in combination with atezolizumab and tiragolumab, (c) tiragolumab in combination with atezolizumab and bevacizumab, or (d) atezolizumab, bevacizumab, and tiragolumab to treat or delay progression of a cancer (e.g., a HCC, e.g., a resectable HCC) in a patient. In some aspects, the invention provides kits that include (a) a bispecific antibody that binds to PD- 1 and LAG3 for use in combination with a VEGF antagonist, (b) a VEGF antagonist for use in combination with a bispecific antibody that binds to PD-1 and LAG3, or (c) a bispecific antibody that binds to PD-1 and LAG3 and a VEGF antagonist for treating a subject having a cancer (e.g., a hepatocellular carcinoma (HCC), e.g., a resectable HCC) according to any of the methods described herein. In some instances, the article of manufacture or kit further comprises package insert comprising instructions for using (a) a bispecific antibody that binds to PD-1 and LAG3 in combination with a VEGF antagonist, (b) a VEGF antagonist in combination with a bispecific antibody that binds to PD-1 and LAG3, or (c) a bispecific antibody that binds to PD-1 and LAG3 and a VEGF antagonist to treat or delay progression of a cancer (e.g., a HCC, e.g., a resectable HCC) in a patient. Accrodingly, in some aspects, the invention provides kits that include (a) tobemstomig for use in combination with bevacizumab, (b) bevacizumab for use in combination with tobemstomig, or (c) tobemstomig and bevacizumab for treating a subject having a cancer (e.g., a hepatocellular carcinoma (HCC), e.g., a resectable HCC) according to any of the methods described herein. In some instances, the article of manufacture or kit further comprises package insert comprising instructions for using (a) tobemstomig in combination with bevacizumab, (b) bevacizumab in combination with tobemstomig, or (c) tobemstomig and bevacizumab to treat or delay progression of a cancer (e.g., a HCC, e.g., a resectable HCC) in a patient. In some instances, (i) a PD-1 axis binding antagonist (e.g., atezolizumab) and a VEGF antagonist (e.g., bevacizumab); (ii) a PD-1 axis binding antagonist (e.g., atezolizumab), a VEGF antagonist (e.g., bevacizumab), and an anti-TIGIT antagonist antibody (e.g., tiragolumab); or (iii) a bispecific antibody that binds to PD-1 and LAG3 (e.g., tobemstomig) and a VEGF antagonist (e.g., bevacizumab) are in the same container or separate containers. Suitable containers include, for example, bottles, vials, bags and syringes. The container may be formed from a variety of materials such as glass, plastic (such as polyvinyl chloride or polyolefin), or metal alloy (such as stainless steel or hastelloy). In some instances, the container holds the formulation and the label on, or associated with, the container may indicate directions for use. The article of manufacture or kit may further include other materials desirable from a PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO commercial and user standpoint, including other buffers, diluents, filters, needles, syringes, and package inserts with instructions for use. In some instances, the article of manufacture further includes one or more of another agent (e.g., an additional chemotherapeutic agent or anti-neoplastic agent). Suitable containers for the one or more agents include, for example, bottles, vials, bags and syringes. EXAMPLES Example 1: A Phase Ib/II, Open-Label, Multicenter, Randomized Platform Study Evaluating the Efficacy and Safety of Neoadjuvant Immunotherapy Combinations in Patients With Surgically Resectable Hepatocellular Carcinoma GO44457 is a phase Ib/II, open-label, multicenter, randomized platform study that evaluates the efficacy and safety of immunotherapy-based treatment combinations, administered as neoadjuvant treatment, in patients with resectable hepatocellular carcinoma (HCC). Specific objectives and corresponding endpoints for the study are outlined in Table 1, below. Table 1. Objectives and Corresponding Endpoints

PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO

PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO

A. Study Rationale Moving immune checkpoint inhibitoríbased treatments forward from the advanced to the early HCC setting is logical both clinically and biologically. Neoadjuvant administration of PD-1/PD-L1 inhibitors combined with standard-of-care chemotherapy significantly improved event-free survival (EFS) and/or pathologic response rates in patients with early-stage triple-negative breast cancer or nonísmall cell lung cancer (Garufi et al., Cancers, 144: 4064, 2022; Forde et al., N Engl J Med, 386: 1973-1985, 2022). In contrast, the study of neoadjuvant therapy in HCC is at a more nascent stage of development. Nonetheless, the anti-tumor activity and survival benefit observed with immunotherapies in unresectable HCC, coupled with a manageable safety profile, provide a rationale for evaluating them in the neoadjuvant setting. The present Phase Ib/II umbrella study is designed to enable the development of neoadjuvant cancer immunotherapy (CIT) combinations by identifying preliminary efficacy and safety signals in patients with resectable HCC. The study assesses the importance of simultaneously targeting multiple mechanisms of immune escape through immune cell priming and activation, tumor infiltration, and/or recognition of tumor cells for elimination. The target and proposed mechanism-of-action classification for each experimental investigational medicinal product (IMP) are summarized in Table 2. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Table 2. Target and Proposed Mechanism-of-Action Classification for Experimental Investigational Medicinal Products

^a Wallin et al., Nat Commun, 7: 12624, 2016; ^b Stanietsky et al., Proc Natl Acad Sci USA, 106: 17858- 17863, 2009; Yu et al., Nat Immunol, 10: 48-57, 2009; Johnston et al., Cancer Cell, 26: 923-937, 2014; ^c Deak et al., J Immunother Cancer, 7: 282(P287), 2019. Example 2: Study Design A study schema for the GO44457 is provided in Fig.1, and a detailed study design is shown in Fig.2. At the discretion of the investigator, participants have the option to either start adjuvant therapy with atezolizumab plus bevacizumab, or move into surveillance following resection. Adjuvant atezolizumab plus bevacizumab may be commenced 4í12 weeks from the date of resection once the participant has fully recovered from surgery. The study design includes an optional expansion phase (Fig. 2). Approximately 90í150 participants are enrolled during the study, with approximately 30í50 participants enrolled into each arm. Approximately 10 participants are enrolled in each treatment arm during the safety evaluation. If no new safety signals are detected, up to approximately 20 additional participants may be enrolled in each treatment arm during the preliminary phase. The study design includes an optional expansion phase. It is not planned to expand the experimental arms upfront. However, in each experimental arm, if clinical activity is observed in the absence of concerning safety issues during the preliminary phase, and additional data are required for interpretation, up to approximately 20 additional participants may be enrolled in that arm during the expansion phase. Additional participants may be enrolled to ensure balance among treatment arms with respect to demographic and baseline characteristics, including potential predictive biomarkers, to enable further subgroup analyses. A. Treatment assigment Participants are randomly assigned to receive one of three experimental neoadjuvant treatments: x Atezolizumab plus bevacizumab (Atezo +Bev); x Atezolizumab plus bevacizumab plus tiragolumab (Atezo +Bev +Tira); or x Tobemstomig plus bevacizumab (Tobe +Bev). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Randomization is stratified according to the Milan criteria status (i.e., within [single tumor ^ 5 cm or 2 to 3 nodules all ^ 3 cm] or beyond [single tumor > 5 cm or 2 to 3 nodules >3 cm, or ^ 4 nodules]). Treatment regimens are summarized in Table 3 and Table 4. Table 3. Dose and Schedule for Neoadjuvant Treatment Regimens

Atezo = atezolizumab; Bev = bevacizumab; Tira = tiragolumab; Tobe = tobemstomig. ^a On Day 1 of each cycle, bevacizumab is administered at least 5 minutes after completion of the atezolizumab infusion. ^b On Day 1 of Cycle 1, tiragolumab is administered at least 60 minutes after completion of the bevacizumab infusion. The interval between subsequent infusions is at least 30 minutes if the previous bevacizumab infusion was given without premedication and tolerated without an infusion-related reaction (IRR) or 60 minutes if the participant experienced an IRR with the previous bevacizumab infusion. ^c On Day 1 of Cycle 1, bevacizumab is administered at least 90 minutes after completion of the tobemstomig infusion. If the first infusion is tolerated without an IRR, bevacizumab is administered at least 60 minutes after the tobemstomig infusion. If the second infusion is tolerated without an IRR, bevacizumab is administered at least 30 minutes after all subsequent tobemstomig infusions. Table 4. Treatment Regimens

^a The randomization ratio depends on the

of experimental arms that are open for enrollment. ^b Enrollment may be delayed or suspended within a given treatment arm. Thus, all listed experimental arms may not be open for enrollment at the same time. ^c Enrollment is suspended in the Atezo + Bev, Atezo + Bev + Tira, and Tobe +Bev arms to allow for a safety evaluation in a minimum of 10 participants. ^d The study design includes an optional expansion phase. It is not planned to expand the experimental arms upfront. However, in each experimental arm, if clinical activity is observed in the absence of concerning safety issues during the preliminary phase, and the Sponsor requires additional data to interpret, up to approximately 20 additional participants may be enrolled in that arm during the expansion phase. The Sponsor may decide to delay or suspend enrollment within a given treatment arm. Experimental arms with minimal clinical activity or unacceptable toxicity will not undergo expansion. Participants in the experimental arms receive up to three cycles (21 days each) of neoadjuvant treatment (see Table 3) until surgery or unacceptable toxicity, whichever occurs first. Participants must receive the first dose of neoadjuvant treatment within 7 business days of randomization. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Atezolizumab + Bevacizumab Participants in the atezolizumab plus bevacizumab (Atezo + Bev) arm receive up to three cycles of treatment as outlined in Table 4 until surgery or unacceptable toxicity, whichever occurs first. It is recommended that treatment be initiated no later than 7 days after randomization. However, the first dose of study treatment should not occur within 3 days after a core biopsy or other surgical procedure. Atezolizumab + Bevacizumab + Tiragolumab Participants in the atezolizumab plus bevacizumab plus tiragolumab (Atezo + Bev + Tira) arm receive up to three cycles of treatment as outlined in Table 4 until surgery or unacceptable toxicity, whichever occurs first. It is recommended that treatment be initiated no later than 7 days after randomization. However, the first dose of study treatment should not occur within 3 days after a core biopsy or other surgical procedure. Tobemstomig + Bevacizumab Participants in the tobemstomig + bevacizumab (Tobe + Bev) arm receive up to three cycles of treatment as outlined in Table 4 until surgery or unacceptable toxicity, whichever occurs first. It is recommended that treatment be initiated no later than 7 days after randomization. However, the first dose of study treatment should not occur within 3 days after a core biopsy or other surgical procedure. After completion of neoadjuvant treatment, or in case of discontinuation due to toxicity and in the absence of disease progression, participants undergo curative-intent liver resection. Liver resection must take place at least 28 days after the final dose of neoadjuvant treatment. Recently, results from the IMbrave050 study (WO41535) evaluating adjuvant therapy with atezolizumab plus bevacizumab showed an improved recurrence-free survival when compared to active surveillance in patients with early-stage HCC following surgical resection or ablation (Chow et al., Adjuvant treatment with atezolizumab and bevacizumab may delay recurrence after surgical resection in patients with liver cancer. Press Conference I of the American Association for Cancer Research Annual Meeting: 2023 April 14í16; Orlando, FL.2023 (cited 16 May 2023)). At the discretion of the investigator, participants have the option to start either adjuvant therapy with atezolizumab + bevacizumab or observation following resection. Adjuvant atezolizumab + bevacizumab treatment (see Table 5) may commence 4í12 weeks from the date of resection once the participant has fully recovered from surgery. Table 5. Dose and Schedule for Optional Adjuvant Treatment Regimen

PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO B. Safety evaluation phase To evaluate the toxicities of the experimental treatments in the neoadjuvant setting, enrollment is suspended after approximately 10 participants have been enrolled in to each treatment arm to allow for a safety evaluation. The safety evaluation is based on safety data from a minimum of 10 participants who have received at least one dose of treatment (i.e., one dose of each agent for a given combination) and who have completed safety follow-up assessments until surgery. Notably, timely conduct of liver resection is an indicator of treatment feasibility and tolerability. Surgical feasibility is assessed based on the number of participants who fail to undergo surgery as a result of a treatment-related adverse event resulting in an extended delay in surgery (defined as > 28 days from surgical restaging visit). Delays in surgery as a result of factors not associated with treatment, such as scheduling or logistical issues, are not included in the evaluation of surgical feasibility. In addition, during the 10-participant safety evaluation, or at any time following the safety evaluation phase, if ^30% of participants experience one or more of the following events that is considered to be at least possibly related to study treatment, enrollment for that combination is put on hold while the benefitírisk profile of that treatment is evaluated: x A treatment-related Grade ^ 3 adverse event that does not improve (with or without treatment) to Grade 2 or better within 2 weeks. x A treatment-related serious adverse event that does not improve (with or without treatment) to a non-serious adverse event or better within 2 weeks. x A treatment-related adverse event that requires permanent discontinuation of study drug. x Death, except those that are incontrovertibly related to disease progression or extraneous causes such as accidents. If no new safety signals are detected, enrollment is resumed in that arm. C. Assessments and monitoring All participants are closely monitored for safety and tolerability throughout the study. Adverse events are graded according to the National Cancer Institute Common Terminology Criteria for Adverse Events, Version 5.0 (NCI CTCAE v5.0) and the American Society for Transplantation and Cellular Therapy (ASTCT) CRS Consensus Grading Scale. The ASTCT CRS Consensus Grading Scale is used in addition to NCI CTCAE when reporting severity of cytokine release syndrome (CRS). Participants undergo pathologic tumor assessments at the time of surgery based on the resected tumor mass. Radiologic response is assessed and determined by the investigator in accordance with RECIST v1.1 and HCC mRECIST, but confirmation by subsequent imaging assessments is not required. Pretreatment baseline tumor tissue samples str collected from all participants, preferably by means of a biopsy performed at study entry. If a biopsy is not deemed feasible by the investigator, archival tumor tissue may be submitted, provided the tissue was obtained prior to enrollment and the participant has not received any anti-cancer therapy, including locoregional liver-directed therapy, since the time of the biopsy. Post-treatment surgical tissue samples are collected from all participants. These samples are utilized for biomarker research. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO To characterize the pharmacokinetic (PK) properties and/or immunogenicity of atezolizumab and the other therapeutic agents, blood samples are taken at various timepoints before and during study treatment administration. On the basis of a review of real-time safety data and available pharmacokinetic (PK) data, treatment regimens may be modified. D. End of study, length of study, and duration of participation The end of this study is defined as the date when the last patient completes the last visit (LPLV), including survival follow-up visits conducted by telephone or in the clinic. The total length of the study, from screening of the first participant to the end of the study, is expected to be approximately 2 to 3 years. Participants will receive up to three cycles of neoadjuvant treatment until surgery or unacceptable toxicity, whichever occurs first. The total duration of study participation for each individual is expected to range from 1 day to approximately 2 to 3 years. Example 3: Materials and Methods A. Inclusion criteria Patients must meet all of the following criteria for study entry: x Age ^ 18 years. x Ability to fully comply with the protocol, in the investigator’s judgment. x Diagnosis of hepatocellular carcinoma (HCC) confirmed either histologically or clinically according to American Association for the Study of Liver Diseases (AASLD) criteria for patients with cirrhosis (Bruix et al., Hepatology, 53: 1020-1022, 2011). For participants without cirrhosis, histological confirmation is mandatory. x HCC that is amenable to negative surgical margins (R0) surgical resection with curative intent in the opinion of the surgeons and oncologists or hepatologists involved in the care of the participant. Patients presenting with resectable HCC within or beyond Milan criteria (without extrahepatic spread or macrovascular invasion) are eligible. x Measurable disease (at least one target lesion) according to RECIST v1.1 as determined by the investigator. x Eastern Cooperative Oncology Group (ECOG) Performance Status of 0 or 1 within 7 days prior to randomization. x Child-Pugh Class A within 7 days prior to randomization (Child and Turcotte: Surgery and portal hypertension. In: Child CG, editor. The liver and portal hypertension. Philadelphia, Saunders, 50-64, 1964; Pugh et al., J Hepatol, 69: 182-236, 2018). x No prior locoregional or systemic treatment for HCC. x Adequate hematologic and end-organ function, defined by the following laboratory test results, obtained within 7 days prior to initiation of study treatment: o ANC ^ 1.5×10⁹/L (1500/mL) without granulocyte colony-stimulating factor (G-CSF) support, except participants with benign ethnic neutropenia (BEN): ANC ^ 1.3 × 10⁹/L (1300/mL without G-CSF support). PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO o Lymphocyte count ^ 0.5×10⁹/L (500/mL). o Platelet count ^ 75× 10⁹/L (75,000/mL) without transfusion. o Hemoglobin ^ 90 g/L (9.0 g/dL) without transfusion. Participants must not have required transfusion during screening or within 2 weeks prior to screening to meet this criterion. o AST, ALT, and ALP ^ 5 × upper limit of normal (ULN). o Bilirubin ^ 3 ×ULN. o Adequate renal function: creatinine clearance by estimated glomerular filtration rate (eGFR) by Modification of Diet in Renal Disease Study (MDRD) formula ^ 50 mL/min. Participants with creatinine clearance by estimating eGFR by MDRD formula of ^ 30 mL/ml and ^ 50 mL/min may be enrolled if renal function was stable for ^ 28 days prior to randomization. o Albumin ^ 28 g/L (2.8 g/dL) without transfusion. o For participants not receiving anticoagulation: INR or aPTT ^ 1.5 × ULN. x Documented virology status of hepatitis, as confirmed by screening tests for hepatitis B virus (HBV) and hepatitis C virus (HCV). Patients with active HBV must have HBV DNA< 500 IU/mL during screening, must have initiated anti-HBV treatment at least 14 days prior to randomization, and must be willing to continue anti-HBV treatment during the study (per local standard of care; e.g., entecavir). Patients with HCV, either with resolved infection (as evidenced by detectable antibody) or chronic infection (as evidenced by detectable HCV RNA), are eligible. x Negative HIV test at screening with the following exception: Individuals with a positive HIV test at screening are eligible provided they are stable on anti-retroviral therapy, have a CD4 count ^ 200/mL, and have an undetectable viral load. x For women of childbearing potential: agreement to remain abstinent (refrain from heterosexual intercourse) or use contraception x For men: agreement to remain abstinent (refrain from heterosexual intercourse) or use contraception, and agreement to refrain from donating sperm. B. Exclusion criteria Participants are excluded from the study if they meet any of the following criteria: x Presence of extrahepatic disease or macrovascular invasion. x Known fibrolamellar HCC, sarcomatoid HCC, mixed cholangiocarcinoma and HCC, or other rare variants of HCC. x History of hepatic encephalopathy if clinically significant within one year prior to initiation of study treatment. x Moderate or severe ascites. x Active co-infection with HBV and HCV (defined as detectable HCV RNA plus positive HBV surface antigen or HBV DNA). x Active co-infection with HBV and hepatitis D viral infection. x Prior treatment with CD137 agonists or immune checkpoint blockade therapies, including antiíCTLA-4, antiíPD-1, and antiíPD-L1 therapeutic antibodies. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO x Treatment with investigational therapy within 28 days prior to initiation of study treatment. x Untreated or incompletely treated esophageal and/or gastric varices with bleeding or that are at high risk for bleeding. x A prior bleeding event due to esophageal and/or gastric varices within 6 months prior to initiation of study treatment. x Inadequately controlled hypertension, defined as systolic blood pressure (BP) > 150 mmHg and/or diastolic BP > 100 mmHg (average of at least three readings at two or more sessions). Anti-hypertensive therapy to achieve these parameters is allowed. x History of hypertensive crisis or hypertensive encephalopathy. x Significant vascular disease (e.g., aortic aneurysm requiring surgical repair or recent peripheral arterial thrombosis) within 6 months prior to initiation of study treatment. x History of hemoptysis (^ 2.5 mL of bright red blood per episode) within 1 month prior to initiation of study treatment. x Evidence of bleeding diathesis or significant coagulopathy (in the absence of therapeutic anticoagulation). x Current or recent (^ 10 days prior to initiation of study treatment) use of aspirin (> 325 mg/day) or treatment with clopidogrel, dipyramidole, ticlopidine, or cilostazol. Chronic use of low dose aspirin (< 325 mg/day) for cardioprotection is allowed. x Current or recent (^ 10 days prior to initiation of study treatment) use of full-dose oral or parenteral anticoagulants or thrombolytic agents for therapeutic (as opposed to prophylactic) purpose. Prophylactic anticoagulation for the patency of venous access devices is allowed provided the activity of the agent results in an INR < 1.5×ULN and aPTT is within normal limits within 14 days prior to initiation of study treatment. Prophylactic use of low-molecular-weight heparin (LMWH; i.e., enoxaparin 40 mg/day) is allowed. x History of abdominal or tracheoesophageal fistula, GI perforation, or intra-abdominal abscess within 6 months prior to initiation of study treatment. x History of intestinal obstruction and/or clinical signs or symptoms of GI obstruction, including subocclusive or occlusive syndrome related to the underlying disease, or requirement for routine parenteral hydration, parenteral nutrition, or tube feeding prior to initiation of study treatment. x Evidence of abdominal free air that is not explained by paracentesis or recent surgical procedure. x Serious, non-healing, or dehiscing wound, active ulcer, or untreated bone fracture. x Grade ^ 2 proteinuria, as demonstrated by ^ 2+ protein on dipstick urinalysis and ^ 1.0 g of protein in a 24-hour urine collection. All patients with ^2+ protein on dipstick urinalysis at screening must undergo a 24-hour urine collection (or an alternative method such as protein:creatinine ratio, per local guidance) for protein and must demonstrate < 1 g of protein in 24 hours. Patients with <2+ protein on dipstick urinalysis are eligible for the study. x History of intra-abdominal inflammatory process within 6 months prior to initiation of study treatment, including but not limited to peptic ulcer disease, diverticulitis, or colitis. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO x Major surgical procedure, open biopsy, or significant traumatic injury within 28 days prior to initiation of study treatment; or abdominal surgery, abdominal interventions or significant abdominal traumatic injury within 60 days prior to initiation of study treatment; or anticipation of need for major surgical procedure, other than potentially curative liver resection, during the course of the study; or non-recovery from side effects of any such procedure. Complete healing from minor surgery (e.g., simple excision, tooth extraction) must have occurred at least 7 days before enrollment. x Chronic daily treatment with a non-steroidal anti-inflammatory drug (NSAID). x Serious infection requiring oral or IV antibiotics and/or hospitalization within 4 weeks prior to screening, including but not limited to hospitalization for complications of infection, bacteremia, or severe pneumonia, or any active infection that, in the opinion of the investigator, could impact participant safety. x History of malignancy within 5 years prior to screening, with the exception of the cancer under investigation in this study and malignancies with a negligible risk of metastasis or death (e.g., 5-year OS rate > 90%), such as adequately treated carcinoma in situ of the cervix, non-melanoma skin carcinoma, localized prostate cancer, ductal carcinoma in situ, or Stage I uterine cancer. Patients with localized prostate cancer (defined as Stage ^pT2c, Gleason score ^ 7, and prostate-specific antigen (PSA) at prostate cancer diagnosis ^ 20 ng/mL) treated with curative intent and without PSA recurrence are eligible. Patients with pre-existing low-risk prostate cancer (defined as Stage cT1/T2a, Gleason score ^ 6, and PSA ^ 10 ng/mL) who are treatment-naive and undergoing active surveillance are eligible. x Active or history of autoimmune disease or immune deficiency, including but not limited to myasthenia gravis, myositis, autoimmune hepatitis, systemic lupus erythematosus, rheumatoid arthritis, inflammatory bowel disease, antiphospholipid antibody syndrome, granulomatosis with polyangiitis, Sjögren syndrome, Guillain-Barré syndrome, or multiple sclerosis, with the following exceptions: patients with a history of autoimmune-related hypothyroidism who are on thyroid-replacement hormone are eligible for the study; patients with controlled Type 1 diabetes mellitus who are on an insulin regimen are eligible for the study; patients with eczema, psoriasis, lichen simplex chronicus, or vitiligo with dermatologic manifestations only (e.g., patients with psoriatic arthritis are excluded) are eligible for the study provided all of following conditions are met: rash must cover < 10% of body surface area; disease is well controlled at baseline and requires only low-potency topical corticosteroids; no occurrence of acute exacerbations of the underlying condition requiring psoralen plus ultraviolet A radiation, methotrexate, retinoids, biologic agents, oral calcineurin inhibitors, or high-potency or oral corticosteroids within the previous 12 months. x Pregnancy or breastfeeding, or intention of becoming pregnant during the study. x Prior treatment with an anti-TIGIT agent. x Active Epstein-Barr virus (EBV) infection or known or suspected chronic active EBV infection at screening. x Prior treatment with an antiíLAG-3 agent. x History of myocarditis (regardless of etiology). x Left ventricular ejection fraction (LVEF) <50% assessed by either transthoracic echocardiogram (TTE) or multiple-gated acquisition (MUGA) scan (TTE preferred test) within 6 months prior to initiation of study treatment. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO x Cardiac enzymes: Troponin T (TnT) or troponin I (TnI) > institutional ULN. C. Concomitant therapy for atezolizumab + bevacizumab arm Concomitant therapy consists of any medication (e.g., prescription drugs, over-the-counter drugs, vaccines, herbal or homeopathic remedies, nutritional supplements) used by a participant in addition to protocol-mandated study treatment from 7 days prior to initiation of study treatment to the treatment discontinuation visit. Permitted therapy for atezolizumab + bevacizumab arm Participants are permitted to use the following therapies during the study: x Oral contraceptives with a failure rate of < 1% per year. x Hormone-replacement therapy. x Prophylactic use of low-dose anticoagulation, unfractionated heparin, or low-molecular-weight heparin (LMWH). x Low-dose aspirin (< 325 mg/day). x Vaccinations (such as influenza, COVID-19). x Megestrol acetate administered as an appetite stimulant. x Mineralocorticoids (e.g., fludrocortisone). x Corticosteroids administered for chronic obstructive pulmonary disease or asthma. x Low-dose corticosteroids administered for orthostatic hypotension or adrenocortical insufficiency. Other use of corticosteroids may be at the investigator’s discretion. x Premedication with antihistamines, antipyretics, and/or analgesics may be administered for the second and subsequent atezolizumab infusions only. In general, investigators manage a participant's care (including preexisting conditions) with supportive therapies other than those defined as cautionary or prohibited therapies as clinically indicated, per local standard practice. Participants who experience infusion-associated symptoms may be treated symptomatically with acetaminophen, ibuprofen, diphenhydramine, and/or H₂-receptor antagonists (e.g., famotidine, cimetidine), or equivalent medications per local standard practice. Serious infusion- associated events manifested by dyspnea, hypotension, wheezing, bronchospasm, tachycardia, reduced oxygen saturation, or respiratory distress are managed with supportive therapies as clinically indicated (e.g., supplemental oxygen and ȕ2-adrenergic agonists). Cautionary therapy for atezolizumab + bevacizumab arm Systemic corticosteroids, immunosuppressive medications, and tumor necrosis factor (TNF) inhibitors may attenuate potential beneficial immunologic effects of treatment with atezolizumab. Therefore, in situations in which systemic corticosteroids, immunosuppressive medications, or TNF inhibitors would be routinely administered, alternatives, including antihistamines, should be considered. If the alternatives are not feasible, systemic corticosteroids, immunosuppressive medications, and TNF inhibitors may be administered. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Systemic corticosteroids or immunosuppressive medications are recommended, at the discretion of the investigator, for the treatment of specific adverse events when associated with atezolizumab therapy. Concomitant use of herbal therapies is not recommended because their pharmacokinetics, safety profiles, and potential drug-drug interactions are generally unknown. However, herbal therapies not intended for the treatment of cancer may be used during the study at the discretion of the investigator. Osteonecrosis of the jaw has been reported in patients receiving bevacizumab, mainly in combination with bisphosphonates. Thus, caution must be exercised in using bevacizumab in participants receiving concomitant bisphosphonates. Prohibited therapy for atezolizumab + bevacizumab arm Use of the following concomitant therapies is prohibited as described below: x Concomitant therapy intended for the treatment of cancer (including but not limited to chemotherapy, hormonal therapy, immunotherapy, radiotherapy, and herbal therapy), whether health authority-approved or experimental, for various time periods prior to starting study treatment, depending on the agent, and during study treatment. x Concomitant use of herbal therapies or traditional Chinese medicine with anti-cancer activity included in the label. x Investigational therapy within 28 days prior to initiation of study treatment and during study treatment. x Live, attenuated vaccines (e.g., FLUMIST®) within 4 weeks prior to initiation of study treatment, during treatment with atezolizumab, and for 5 months after the final dose of atezolizumab. x Systemic immunostimulatory agents (including but not limited to interferons and interleukin-2) within 4 weeks or 5 drug-elimination half-lives (whichever is longer) prior to initiation of study treatment and during study treatment because these agents could potentially increase the risk for autoimmune conditions when given in combination with atezolizumab. x Current use of full-dose anticoagulants, thrombolytic therapy at therapeutic doses, or anti-platelet therapy. Local label-recommended doses for prophylactic use of anticoagulants or thrombolytic therapies are allowed. Low-dose aspirin (< 325 mg/day) is permitted. Co-administration of proton pump inhibitors is strongly recommended to reduce potential GI damage. x Use of warfarin or Coumadin-like products (includes for prophylactic use). Prophylactic use of low- dose anticoagulation, unfractionated heparin, or LMWH is permitted. x Concomitant chronic use of non-steroidal anti-inflammatory drugs (NSAIDs) while receiving study drugs, with the exception of chronic low-dose aspirin (< 325 mg/day). However, for the symptomatic relief of medical conditions (e.g., headache, fever) intermittent or short-term intake of oral NSAIDs is allowed, when co-administered with proton pump inhibitors to reduce potential GI damage. D. Concomitant therapy for atezolizumab + bevacizumab + tiragolumab arm Permitted therapy for atezolizumab + bevacizumab + tiragolumab arm Participants are permitted to use the following therapies during the study: PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO x Oral contraceptives with a failure rate of < 1% per year. x Hormone-replacement therapy. x Prophylactic use of low-dose anticoagulation, unfractionated heparin, or low-molecular-weight heparin (LMWH). x Low-dose aspirin (< 325 mg/day). x Vaccinations (such as influenza, COVID-19). x Megestrol acetate administered as an appetite stimulant. x Mineralocorticoids (e.g., fludrocortisone). x Corticosteroids administered for chronic obstructive pulmonary disease or asthma. x Low-dose corticosteroids administered for orthostatic hypotension or adrenocortical insufficiency. Other use of corticosteroids may be at the investigator’s discretion. x Premedication with antihistamines, antipyretics, and/or analgesics may be administered for the second and subsequent atezolizumab and tiragolumab infusions only. In general, investigators manage a participant's care (including preexisting conditions) with supportive therapies other than those defined as cautionary or prohibited therapies as clinically indicated, per local standard practice. Participants who experience infusion-associated symptoms may be treated symptomatically with acetaminophen, ibuprofen, diphenhydramine, and/or H₂-receptor antagonists (e.g., famotidine, cimetidine), or equivalent medications per local standard practice. Serious infusion- associated events manifested by dyspnea, hypotension, wheezing, bronchospasm, tachycardia, reduced oxygen saturation, or respiratory distress are managed with supportive therapies as clinically indicated (e.g., supplemental oxygen and ȕ2-adrenergic agonists). Cautionary therapy for atezolizumab + bevacizumab + tiragolumab arm Systemic corticosteroids, immunosuppressive medications, and tumor necrosis factor (TNF) inhibitors may attenuate potential beneficial immunologic effects of treatment with atezolizumab and/or tiragolumab. Therefore, in situations in which systemic corticosteroids, immunosuppressive medications, or TNF inhibitors would be routinely administered, alternatives, including antihistamines, should be considered. If the alternatives are not feasible, systemic corticosteroids, immunosuppressive medications, and TNF inhibitors may be administered. Systemic corticosteroids or immunosuppressive medications are recommended, at the discretion of the investigator, for the treatment of specific adverse events when associated with atezolizumab and/or tiragolumab therapy. Prohibited therapy for atezolizumab + bevacizumab + tiragolumab arm Use of the following concomitant therapies is prohibited as described below: x Concomitant therapy intended for the treatment of cancer (including but not limited to chemotherapy, hormonal therapy, immunotherapy, radiotherapy, and herbal therapy), whether health authority-approved or experimental, for various time periods prior to starting study treatment, depending on the agent, and during study treatment. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO x Concomitant use of herbal therapies or traditional Chinese medicine with anti-cancer activity included in the label. x Investigational therapy within 28 days prior to initiation of study treatment and during study treatment. x Live, attenuated vaccines (e.g., FLUMIST®) within 4 weeks prior to initiation of study treatment, during treatment with atezolizumab and tiragolumab, and for 5 months after the final dose of atezolizumab and for 90 days after the final dose of tiragolumab. x Systemic immunostimulatory agents (including but not limited to interferons and interleukin-2) within 4 weeks or 5 drug-elimination half-lives (whichever is longer) prior to initiation of study treatment and during study treatment because these agents could potentially increase the risk for autoimmune conditions when given in combination with atezolizumab. x Current use of full-dose anticoagulants, thrombolytic therapy at therapeutic doses, or anti-platelet therapy. Local label-recommended doses for prophylactic use of anticoagulants or thrombolytic therapies are allowed. Low-dose aspirin (< 325 mg/day) is permitted. Co-administration of proton pump inhibitors is strongly recommended to reduce potential GI damage. x Use of warfarin or Coumadin-like products (includes for prophylactic use). Prophylactic use of low- dose anticoagulation, unfractionated heparin, or LMWH is permitted. x Concomitant chronic use of non-steroidal anti-inflammatory drugs (NSAIDs) while receiving study drugs, with the exception of chronic low-dose aspirin (< 325 mg/day). However, for the symptomatic relief of medical conditions (e.g., headache, fever) intermittent or short-term intake of oral NSAIDs is allowed, when co-administered with proton pump inhibitors to reduce potential GI damage. E. Concomitant therapy for tobemstomig + bevacizumab arm Permitted therapy for tobemstomig + bevacizumab arm Participants are permitted to use the following therapies during the study: x Oral contraceptives with a failure rate of < 1% per year. x Hormone-replacement therapy. x Prophylactic use of low-dose anticoagulation, unfractionated heparin, or low-molecular-weight heparin (LMWH). x Low-dose aspirin (< 325 mg/day). x Vaccinations (such as influenza, COVID-19). x Megestrol acetate administered as an appetite stimulant. x Mineralocorticoids (e.g., fludrocortisone). x Corticosteroids administered for chronic obstructive pulmonary disease or asthma. x Low-dose corticosteroids administered for orthostatic hypotension or adrenocortical insufficiency. Other use of corticosteroids may be at the investigator’s discretion. x Premedication with antihistamines, antipyretics, and/or analgesics may be administered for the second and subsequent tobemstomig infusions only. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Cautionary therapy for tobemstomig + bevacizumab arm Systemic corticosteroids, immunosuppressive medications, and tumor necrosis factor (TNF) inhibitors may attenuate potential beneficial immunologic effects of treatment with atezolizumab and/or tiragolumab. Therefore, in situations in which systemic corticosteroids, immunosuppressive medications, or TNF inhibitors would be routinely administered, alternatives, including antihistamines, should be considered. If the alternatives are not feasible, systemic corticosteroids, immunosuppressive medications, and TNF inhibitors may be administered. Systemic corticosteroids or immunosuppressive medications are recommended, at the discretion of the investigator, for the treatment of specific adverse events when associated with atezolizumab and/or tiragolumab therapy. Prohibited therapy for tobemstomig + bevacizumab arm Use of the following concomitant therapies is prohibited as described below: x Concomitant therapy intended for the treatment of cancer (including but not limited to chemotherapy, hormonal therapy, immunotherapy, radiotherapy, and herbal therapy), whether health authority-approved or experimental, for various time periods prior to starting study treatment, depending on the agent, and during study treatment. x Concomitant use of herbal therapies or traditional Chinese medicine with anti-cancer activity included in the label. x Investigational therapy within 28 days prior to initiation of study treatment and during study treatment. x Live, attenuated vaccines (e.g., FLUMIST®) within 4 weeks prior to initiation of study treatment, during treatment with tobemstomig, and for 4 months after the final dose of tobemstomig. x Systemic immunostimulatory agents (including but not limited to interferons and interleukin-2) within 4 weeks or 5 drug-elimination half-lives (whichever is longer) prior to initiation of study treatment and during study treatment because these agents could potentially increase the risk for autoimmune conditions when given in combination with tobemstomig. x Current use of full-dose anticoagulants, thrombolytic therapy at therapeutic doses, or anti-platelet therapy. Local label-recommended doses for prophylactic use of anticoagulants or thrombolytic therapies are allowed. Low-dose aspirin (< 325 mg/day) is permitted. Co-administration of proton pump inhibitors is strongly recommended to reduce potential GI damage. x Use of warfarin or Coumadin-like products (includes for prophylactic use). Prophylactic use of low- dose anticoagulation, unfractionated heparin, or LMWH is permitted. x Concomitant chronic use of non-steroidal anti-inflammatory drugs (NSAIDs) while receiving study drugs, with the exception of chronic low-dose aspirin (< 325 mg/day). However, for the symptomatic relief of medical conditions (e.g., headache, fever) intermittent or short-term intake of oral NSAIDs is allowed, when co-administered with proton pump inhibitors to reduce potential GI damage. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO Example 4: Statistical Considerations and Analysis Plan The GO44457 final study analysis is based on participant data collected through study discontinuation. If not otherwise specified, efficacy analyses are based on the efficacy-evaluable population, defined as all participants who receive at least one dose of each drug for their assigned treatment regimen, and safety analyses are based on the safety-evaluable population, defined as all participants who receive any amount of study treatment. A. Efficacy analyses Primary efficacy endpoint The primary efficacy endpoint is major pathologic response (MPR) rate (as described in Table 1). MPR rate is defined as the proportion of participants who have achieved MPR and is estimated for each treatment cohort in the efficacy-evaluable population. MPR is defined as ^ 10% residual viable tumor in the tumor bed at the time of surgical resection in the primary tumor, as assessed by the central pathology laboratory. Participants who do not proceed to surgery are considered as non-responders for MPR. MPR is calculated for each arm along with 95% Clopper-Pearson CIs. Secondary efficacy endpoints and exploratory efficacy endpoints The secondary efficacy endpoints are relapse-free survival (RFS), event-free survival (EFS), overall survival (OS), objective response rate (ORR), proportion of resected participants with a pathologic complete response (pCR), proportion of participants downstaged to within Milan criteria (for participants beyond criteria at randomization), and negative surgical margins (R0) resection rate, as defined in Table 1. RFS is defined as the time from surgery to the first documented recurrence of disease (intrahepatic or extrahepatic) according to EASL and/or RECIST v1.1, or death from any cause. For participants who do not have documented recurrence of disease or death, RFS is censored at the day of the last tumor assessment. EFS is defined as the time from randomization to any of the following events (whichever occurs first): disease progression that precludes surgery, as assessed by the investigator according RECIST v1.1; local or distant disease recurrence as measured by EASL and/or RECIST v1.1; or death from any cause. Participants who have not experienced such events are censored at the time of their last post- surgical tumor assessment. OS is defined as the time from randomization to death from any cause. Participants who are still alive at the time of OS analysis are censored at the last date they were known to be alive. The Kaplan-Meier method is used to estimate the median for RFS, EFS, and OS, with 95% CIs constructed through use of the Brookmeyer and Crowley method. The OS rate at specific timepoints is estimated using the Kaplan-Meier method, with 95% CIs calculated on the basis of Greenwood’s estimate for the variance. The ORR is assessed after completion of neoadjuvant treatment and is defined as the proportion of participants with a complete response or partial response, as determined by the investigator according to RECIST v1.1 and HCC mRECIST. Responses are assessed and determined by the investigator in PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO accordance with RECIST v1.1 and HCC mRECIST, but confirmation by subsequent imaging assessments is not required. Participants with missing or no response assessments are classified as non-responders. Note that ORR is determined using unconfirmed pre-operative radiologic responses. ORR is calculated for each arm, along with 95% Clopper-Pearson CIs. The pCR rate is defined as the proportion of participants who have achieved pCR. pCR is defined as the absence of any viable tumor cells in both the primary tumor and all sampled lymph nodes at the time of surgical resection. pCR rate is analyzed using the same statistical methodology as MPR rate for each treatment cohort for the efficacy-evaluable population. The proportion of participants downstaged to within Milan criteria is defined as the number of participants who were beyond Milan criteria at enrollment and stage as within Milan criteria (single tumor ^5 cm or 2 to 3 nodules all ^ 3 cm) during the study. The proportion is calculated for each arm, along with 95% Clopper-Pearson CIs. R0 resection rate is defined as the proportion of participants who achieved complete resection (R0 resection, confirmed by pathology). The denominator of the proportion is based on the efficacy- evaluable population. R0 resection rate is calculated for each arm, along with 95% Clopper-Pearson CIs. The exploratory efficacy endpoints are landmark EFS, RFS, and OS, at specific timepoints (1 and 2 years) as defined in Table 1. Landmark EFS rates, landmark RFS rates, and landmark OS rates are estimated for each study arm using the Kaplan-Meier method, with 95% CIs calculated through use of Greenwood’s formula. B. Safety analyses Safety assessments consist of monitoring and recording adverse events, including serious adverse events and adverse events of special interest, performing protocol-specified safety laboratory assessments, measuring protocol-specified vital signs, and conducting other protocol-specified tests that are deemed critical to the safety evaluation of the study. Verbatim adverse event terms are mapped to MedDRA thesaurus terms, and adverse event severity is graded according to NCI CTCAE v5.0, with severity of cytokine release syndrome (CRS) graded according to the ASTCT CRS Consensus Grading Scale for CRS. Safety is assessed through summaries of adverse events, changes in laboratory test results, changes in vital signs and ECGs, and exposure to study drugs. Exposure to combination treatment and length of safety follow-up is summarized by treatment arm. To assess the impact of neoadjuvant treatment on surgical feasibility, the proportion of participants with delayed or canceled surgery due to treatment-related adverse events is evaluated in totality. All adverse events, serious adverse events, and drug-related adverse events resulting in surgical delays and post-surgical complications are collected. Specific data re collected to assess the impact of neoadjuvant treatment on surgical complexity, outcomes, and complications, including: x Preoperative attrition (percent not resected). x Treatment-related adverse events leading to delayed or cancelled surgery. x Length of surgical delay.. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO x Time from end of neoadjuvant treatment to surgery. x Duration of surgery. x Length of hospital stay. x Type of liver resection (anatomical or nonanatomical; based on Brisbane criteria). x Quality of liver resection (R0, R1, or R2). x Width of resection margin. x Surgical approach (minimally invasive vs. open). x Extent of surgery (minor (< 3 Couinaud segments) vs. major resection (^3 Couinaud segments) according to Brisbane criteria). x Intraoperative blood loss. x Requirement for intraoperative blood or platelet transfusion. x Postoperative 30- and 90-day mortality. Post-operative surgical complication rates are calculated according to the Clavien-Dindo surgical classification (clinically relevant complications are defined as Clavien-Dindo Grade ^ IIIa). Complication rates for every grade are reported and scored for participants that underwent liver resection. Post-operative mortality is defined as death within 90 days after surgery or prior to discharge. Surgical complications are scored according to Clavien-Dindo classification. C. Interim analyses It is anticipated that interim analyses will be conducted during the study, with the earliest interim analysis taking place when at least one experimental arm has completed enrollment of the safety evaluation period (first 10 participants), and participants have completed their MPR assessment. Further interim analyses may be conducted as appropriate. A posterior probability may be used to guide further enrollment in a treatment arm after completing safety evaluation and the preliminary phase, based on an interim analysis of clinical activity in the experimental arm compared with a predefined MPR threshold. All data from the safety evaluation are incorporated with the preliminary phase data at the time of interim analysis. The predefined MPR threshold is to be based on emerging internal and external data for in-class immune-modulating investigational and other compounds for the participant population. Enrollment in an arm may be expanded on the basis of the totality of available data including but not limited to RFS, EFS, and potentially early OS data. Safety and biomarker data (available at the time of making this decision) are also taken into consideration from the perspective of an adequate benefitírisk assessment. Although the foregoing invention has been described in some detail by way of illustration and example for purposes of clarity of understanding, the descriptions and examples should not be construed as limiting the scope of the invention. The disclosures of all patent and scientific literature cited herein are expressly incorporated in their entirety by reference.

Claims

PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO WHAT IS CLAIMED IS: 1. A method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC. 2. The method of claim 1, wherein one, two, or three dosing cycles are completed prior to the surgery. 3. The method of claim 2, wherein three dosing cycles are completed prior to the surgery. 4. The method of any one of claims 1-3, wherein the atezolizumab is administered at a fixed dose of about 1200 mg every three weeks. 5. The method of any one of claims 1-4, wherein the bevacizumab is administered at a dose of about 15 mg/kg every three weeks. 6. The method of any one of claims 1-5, wherein the tiragolumab is administered at a fixed dose of about 600 mg every three weeks. 7. The method of any one of claims 1-6, wherein the length of each of the one or more dosing cycles is 21 days. 8. The method of claim 7, wherein the atezolizumab is administered on about Day 1 of each 21-day dosing cycle. 9. The method of claim 7 or 8, wherein the bevacizumab is administered on about Day 1 of each 21- day dosing cycle. 10. The method of any one of claims 7-9, wherein the tiragolumab is administered on about Day 1 of each 21-day dosing cycle. 11. The method of any one of claims 1-10, wherein the method comprises administering to the subject atezolizumab before bevacizumab. 12. The method of any one of claims 1-11, wherein the method comprises administering to the subject bevacizumab before tiragolumab. 13. The method of any one of claims 1-12, wherein the method comprises administering to the subject atezolizumab first, bevacizumab second, and tiragolumab third. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 14. The method of any one of claims 1-13, wherein the method comprises administering to the subject atezolizumab, bevacizumab, and/or tiragolumab intravenously. 15. The method of any one of claims 1-14, further comprising administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 16. A method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject: (a) one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 17. A method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. 18. The method of claim 17, wherein one, two, or three dosing cycles of atezolizumab and bevacizumab are completed prior to the surgery. 19. The method of claim 18, wherein three dosing cycles of atezolizumab and bevacizumab are completed prior to the surgery. 20. The method of any one of claims 17-19, wherein the atezolizumab is administered at a fixed dose of about 1200 mg every three weeks. 21. The method of any one of claims 17-20, wherein the bevacizumab is administered at a dose of about 15 mg/kg every three weeks. 22. The method of any one of claims 17-21, wherein the length of each of the one or more dosing cycles is 21 days. 23. The method of claim 22, wherein the atezolizumab is administered on about Day 1 of each 21- day dosing cycle. 24. The method of claim 22 or 23, wherein the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. 25. The method of any one of claims 17-24, wherein the method comprises administering to the subject atezolizumab before bevacizumab. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 26. The method of any one of claims 17-25, wherein the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously. 27. The method of any one of claims 17-26, further comprising administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 28. A method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject: (a) one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 29. A method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. 30. The method of claim 29, wherein one, two, or three dosing cycles are completed prior to the surgery. 31. The method of claim 30, wherein three dosing cycles are completed prior to the surgery. 32. The method of any one of claims 29-31, wherein the tobemstomig is administered at a fixed dose of about 600 mg every three weeks. 33. The method of any one of claims 29-32, wherein the bevacizumab is administered at a dose of about 15 mg/kg every three weeks. 34. The method of any one of claims 29-33, wherein the length of each of the one or more dosing cycles is 21 days. 35. The method of claim 34, wherein the tobemstomig is administered on about Day 1 of each 21-day dosing cycle. 36. The method of claim 34 or 35, wherein the bevacizumab is administered on about Day 1 of each 21-day dosing cycle. 37. The method of any one of claims 29-36, wherein the method comprises administering to the subject tobemstomig before bevacizumab. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 38. The method of any one of claims 29-37, wherein the method comprises administering to the subject tobemstomig and/or bevacizumab intravenously. 39. The method of any one of claims 29-38, further comprising administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 40. A method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject: (a) one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 41. The method of any one of claims 1-40, wherein the HCC is a resectable HCC. 42. The method of any one of claims 1-41, wherein the subject has received no prior systemic or locoregional treatment for HCC. 43. The method of any one of claims 1-42, wherein the subject does not have extrahepatic disease. 44. The method of any one of claims 1-43, wherein the subject does not have macroscopic vascular invasion (MVI). 45. The method of any one of claims 1-44, wherein the subject has been determined to have adequate liver function. 46. The method of claim 45, wherein the adequate liver function is characterized as Child-Pugh class A. 47. The method of any one of claims 1-46, wherein: (a) the subject has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) the subject has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm. 48. The method of claim 47, wherein the subject is within the Milan criteria. 49. The method of any one of claims 1-46, wherein: (a) the subject has a single HCC tumor with a longest diameter of > 5 cm; (b) the subject has between two and three HCC tumor nodules, and at least two of the nodules have a longest diameter of >3 cm; or PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO (c) the subject has four or more HCC tumor nodules. 50. The method of claim 49, wherein the subject is beyond the Milan criteria. 51. The method of any one of claims 1-50, wherein the surgery is a liver resection. 52. The method of claim 51, wherein the surgery is a negative surgical margins (R0) surgical resection. 53. The method of claim 51 or 52, wherein the surgery has curative intent. 54. The method of any one of claims 1-53, wherein the surgery is performed at least 28 days after the last day of the one or more dosing cycles. 55. The method of any one of claims 15, 16, 27, 28, and 39-54, wherein between 1 and 17 dosing cycles of atezolizumab and bevacizumab are administered to the subject as an adjuvant therapy after the surgery. 56. The method of claim 55, wherein 17 dosing cycles of atezolizumab and bevacizumab are administered to the subject as an adjuvant therapy after the surgery. 57. The method of any one of claims 15, 16, 27, 28, and 39-56, wherein dosing cycles of atezolizumab and bevacizumab are administered to the subject as an adjuvant therapy for up to 12 months after the surgery. 58. The method of any one of claims 15, 16, 27, 28, and 39-57, wherein the adjuvant therapy comprises administering the atezolizumab to the subject at a fixed dose of about 1200 mg every three weeks. 59. The method of any one of claims 15, 16, 27, 28, and 39-58, wherein the adjuvant therapy comprises administering the bevacizumab to the subject at a dose of about 15 mg/kg every three weeks. 60. The method of any one of claims 15, 16, 27, 28, and 39-59, wherein the length of each of the one or more dosing cycles of the adjuvant therapy is 21 days. 61. The method of claim 60, wherein the atezolizumab is administered on about Day 1 of each 21- day dosing cycle of the adjuvant therapy. 62. The method of claim 60 or 61, wherein the bevacizumab is administered on about Day 1 of each 21-day dosing cycle of the adjuvant therapy. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 63. The method of any one of claims 15, 16, 27, 28, and 39-62, wherein the method comprises administering to the subject atezolizumab before bevacizumab during each of the one or more dosing cycles of the adjuvant therapy. 64. The method of any one of claims 15, 16, 27, 28, and 39-63, wherein the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously during each of the one or more dosing cycles of the adjuvant therapy. 65. The method of any one of claims 1-64, wherein the treating results in an increase in the major pathologic response (MPR) rate as compared to a reference MPR rate. 66. The method of claim 65, wherein the reference MPR rate is the MPR rate of a population of subjects who have received a control treatment. 67. The method of any one of claims 1-64, wherein the treating results in an increase in the pathologic complete response (pCR) rate as compared to a reference pCR rate. 68. The method of claim 67, wherein the reference pCR rate is the pCR rate of a population of subjects who have received a control treatment. 69. The method of any one of claims 1-64, wherein the treating results in an increase in the duration of event-free survival (EFS) as compared to a reference EFS duration. 70. The method of claim 69, wherein the reference EFS duration is the mean or median EFS duration of a population of subjects who have received a control treatment. 71. The method of any one of claims 1-64, wherein the treating results in an increase in the duration of overall survival (OS) as compared to a reference OS duration. 72. The method of claim 71, wherein the reference OS duration is the mean or median OS duration of a population of subjects who have received a control treatment. 73. The method of any one of claims 1-64, wherein the treating results in an increase in the objective response rate (ORR) as compared to a reference ORR. 74. The method of claim 73, wherein the reference ORR is the ORR of a population of subjects who have received a control treatment. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 75. The method of any one of claims 1-64, wherein the treating results in an increase in the proportion of patients that are downstaged to within Milan criteria as compared to the proportion in a reference population. 76. The method of claim 75, wherein the proportion in a reference population is the proportion of patients that are downstaged to within Milan criteria in a population of subjects who have received a control treatment. 77. The method of any one of claims 1-64, wherein the treating results in an increase in the R0 resection rate as compared to a reference R0 resection rate. 78. The method of claim 77, wherein the reference R0 resection rate is the R0 resection rate of a population of subjects who have received a control treatment. 79. The method of any one of claims 1-78, wherein the subject is a human. 80. Atezolizumab, bevacizumab, and/or tiragolumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC. 81. The atezolizumab, bevacizumab, and/or tiragolumab for use of claim 80, wherein one, two, or three dosing cycles are to be completed prior to the surgery. 82. The atezolizumab, bevacizumab, and/or tiragolumab for use of claim 81, wherein three dosing cycles are to be completed prior to the surgery. 83. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-82, wherein the atezolizumab is to be administered at a fixed dose of about 1200 mg every three weeks. 84. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-83, wherein the bevacizumab is to be administered at a dose of about 15 mg/kg every three weeks. 85. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-84, wherein the tiragolumab is to be administered at a fixed dose of about 600 mg every three weeks. 86. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-85, wherein the length of each of the one or more dosing cycles is 21 days. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 87. The atezolizumab, bevacizumab, and/or tiragolumab for use of claim 86, wherein the atezolizumab is to be administered on about Day 1 of each 21-day dosing cycle. 88. The atezolizumab, bevacizumab, and/or tiragolumab for use of claim 86 or 87, wherein the bevacizumab to be is administered on about Day 1 of each 21-day dosing cycle. 89. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 86-88, wherein the tiragolumab is to be administered on about Day 1 of each 21-day dosing cycle. 90. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-89, wherein the method comprises administering to the subject atezolizumab before bevacizumab. 91. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-90, wherein the method comprises administering to the subject bevacizumab before tiragolumab. 92. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-91, wherein the method comprises administering to the subject atezolizumab first, bevacizumab second, and tiragolumab third. 93. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-92, wherein the method comprises administering to the subject atezolizumab, bevacizumab, and/or tiragolumab intravenously. 94. The atezolizumab, bevacizumab, and/or tiragolumab for use of any one of claims 80-93, wherein the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 95. Atezolizumab, bevacizumab, and/or tiragolumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject: (a) one or more dosing cycles of atezolizumab, bevacizumab, and tiragolumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 96. Atezolizumab and/or bevacizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. 97. The atezolizumab and/or bevacizumab for use of claim 96, wherein one, two, or three dosing cycles of atezolizumab and bevacizumab are to be completed prior to the surgery. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 98. The atezolizumab and/or bevacizumab for use of claim 97, wherein three dosing cycles of atezolizumab and bevacizumab are to be completed prior to the surgery. 99. The atezolizumab and/or bevacizumab for use of any one of claims 96-98, wherein the atezolizumab is to be administered at a fixed dose of about 1200 mg every three weeks. 100. The atezolizumab and/or bevacizumab for use of any one of claims 96-99, wherein the bevacizumab is to be administered at a dose of about 15 mg/kg every three weeks. 101. The atezolizumab and/or bevacizumab for use of any one of claims 96-100, wherein the length of each of the one or more dosing cycles is 21 days. 102. The atezolizumab and/or bevacizumab for use of claim 101, wherein the atezolizumab is to be administered on about Day 1 of each 21-day dosing cycle. 103. The atezolizumab and/or bevacizumab for use of claim 101 or 102, wherein the bevacizumab is to be administered on about Day 1 of each 21-day dosing cycle. 104. The atezolizumab and/or bevacizumab for use of any one of claims 96-103, wherein the method comprises administering to the subject atezolizumab before bevacizumab. 105. The atezolizumab and/or bevacizumab for use of any one of claims 96-104, wherein the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously. 106. The atezolizumab and/or bevacizumab for use of any one of claims 96-105, wherein the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 107. Atezolizumab and/or bevacizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject: (a) one or more dosing cycles of atezolizumab and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 108. Tobemstomig and/or bevacizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC. 109. The tobemstomig and/or bevacizumab for use of claim 108, wherein one, two, or three dosing cycles are to be completed prior to the surgery. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 110. The tobemstomig and/or bevacizumab for use of claim 109, wherein three dosing cycles are to be completed prior to the surgery. 111. The tobemstomig and/or bevacizumab for use of any one of claims 108-110, wherein the tobemstomig is to be administered at a fixed dose of about 600 mg every three weeks. 112. The tobemstomig and/or bevacizumab for use of any one of claims 108-111, wherein the bevacizumab is to be administered at a dose of about 15 mg/kg every three weeks. 113. The tobemstomig and/or bevacizumab for use of any one of claims 108-112, wherein the length of each of the one or more dosing cycles is 21 days. 114. The tobemstomig and/or bevacizumab for use of claim 113, wherein the tobemstomig is administered on about Day 1 of each 21-day dosing cycle. 115. The tobemstomig and/or bevacizumab for use of claim 113 or 114, wherein the bevacizumab is to be administered on about Day 1 of each 21-day dosing cycle. 116. The tobemstomig and/or bevacizumab for use of any one of claims 108-115, wherein the method comprises administering to the subject tobemstomig before bevacizumab. 117. The tobemstomig and/or bevacizumab for use of any one of claims 108-116, wherein the method comprises administering to the subject tobemstomig and/or bevacizumab intravenously. 118. The tobemstomig and/or bevacizumab for use of any one of claims 108-117, wherein the method further comprises administering to the subject one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 119. Tobemstomig, bevacizumab, and/or atezolizumab for use in a method of treating a subject having a hepatocellular carcinoma (HCC), the method comprising administering to the subject: (a) one or more dosing cycles of tobemstomig and bevacizumab as a neoadjuvant therapy prior to a surgery for the HCC; and (b) one or more dosing cycles of atezolizumab and bevacizumab as an adjuvant therapy after the surgery. 120. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-119, wherein the HCC is a resectable HCC. 121. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-120, wherein the subject has received no prior systemic or locoregional treatment for HCC. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 122. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-121, wherein the subject does not have extrahepatic disease. 123. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-122, wherein the subject does not have macroscopic vascular invasion (MVI). 124. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-123, wherein the subject has been determined to have adequate liver function. 125. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 124, wherein the adequate liver function is characterized as Child-Pugh class A. 126. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-125, wherein: (a) the subject has a single HCC tumor with a longest diameter of ^ 5 cm; or (b) the subject has between two and three HCC tumor nodules, each having a longest diameter of ^ 3 cm. 127. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 126, wherein the subject is within the Milan criteria. 128. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-125, wherein: (a) the subject has a single HCC tumor with a longest diameter of > 5 cm; (b) the subject has between two and three HCC tumor nodules, and at least two of the nodules have a longest diameter of >3 cm; or (c) the subject has four or more HCC tumor nodules. 129. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 128, wherein the subject is beyond the Milan criteria. 130. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-129, wherein the surgery is a liver resection. 131. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 130, wherein the surgery is a negative surgical margins (R0) surgical resection. 132. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 130 or 131, wherein the surgery has curative intent. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 133. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-132, wherein the surgery is to be performed at least 28 days after the last day of the one or more dosing cycles. 134. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 94, 95, 106, 107, and 118-133, wherein between 1 and 17 dosing cycles of atezolizumab and bevacizumab are to be administered to the subject as an adjuvant therapy after the surgery. 135. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 134, wherein 17 dosing cycles of atezolizumab and bevacizumab are to be administered to the subject as an adjuvant therapy after the surgery. 136. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 94, 95, 106, 107, and 118-135, wherein dosing cycles of atezolizumab and bevacizumab are to be administered to the subject as an adjuvant therapy for up to 12 months after the surgery. 137. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 94, 95, 106, 107, and 118-136, wherein the adjuvant therapy comprises administering the atezolizumab to the subject at a fixed dose of about 1200 mg every three weeks. 138. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 94, 95, 106, 107, and 118-137, wherein the adjuvant therapy comprises administering the bevacizumab to the subject at a dose of about 15 mg/kg every three weeks. 139. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 94, 95, 106, 107, and 118-137, wherein the length of each of the one or more dosing cycles of the adjuvant therapy is 21 days. 140. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 139, wherein the atezolizumab is to be administered on about Day 1 of each 21-day dosing cycle of the adjuvant therapy. 141. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 139 or 140, wherein the bevacizumab is to be administered on about Day 1 of each 21-day dosing cycle of the adjuvant therapy. 142. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 94, 95, 106, 107, and 118-141, wherein the method comprises administering to the subject atezolizumab before bevacizumab during each of the one or more dosing cycles of the adjuvant therapy. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 143. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 94, 95, 106, 107, and 118-142, wherein the method comprises administering to the subject atezolizumab and/or bevacizumab intravenously during each of the one or more dosing cycles of the adjuvant therapy. 144. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-143, wherein the treating results in an increase in the major pathologic response (MPR) rate as compared to a reference MPR rate. 145. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 144, wherein the reference MPR rate is the MPR rate of a population of subjects who have received a control treatment. 146. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-143, wherein the treating results in an increase in the pathologic complete response (pCR) rate as compared to a reference pCR rate. 147. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 146, wherein the reference pCR rate is the pCR rate of a population of subjects who have received a control treatment. 148. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-143, wherein the treating results in an increase in the duration of event-free survival (EFS) as compared to a reference EFS duration. 149. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 148, wherein the reference EFS duration is the mean or median EFS duration of a population of subjects who have received a control treatment. 150. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-143, wherein the treating results in an increase in the duration of overall survival (OS) as compared to a reference OS duration. 151. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 150, wherein the reference OS duration is the mean or median OS duration of a population of subjects who have received a control treatment. 152. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-143, wherein the treating results in an increase in the objective response rate (ORR) as compared to a reference ORR. PATENT Attorney Docket No.: 50474-336WO1 Genentech Reference No.: P38604-WO 153. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 152, wherein the reference ORR is the ORR of a population of subjects who have received a control treatment. 154. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-143, wherein the treating results in an increase in the proportion of patients that are downstaged to within Milan criteria as compared to the proportion in a reference population. 155. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 154, wherein the proportion in a reference population is the proportion of patients that are downstaged to within Milan criteria in a population of subjects who have received a control treatment. 156. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-143, wherein the treating results in an increase in the R0 resection rate as compared to a reference R0 resection rate. 157. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of claim 156, wherein the reference R0 resection rate is the R0 resection rate of a population of subjects who have received a control treatment. 158. The atezolizumab, bevacizumab, tiragolumab, and/or tobemstomig for use of any one of claims 80-157, wherein the subject is a human.