TW202417477A - Antibodies that bind to multiple sarbecoviruses - Google Patents

Abstract

The instant disclosure provides antibodies and antigen-binding fragments thereof that can bind to S proteins of sarbecoviruses (including, in some embodiments, multiple sarbecoviruses) and, in certain embodiments, are capable of neutralizing infection by multiple sarbecoviruses.

Description

Antibodies that bind to multiple SARS-CoV-2 beta coronaviruses

This case relates to antibodies and antigen-binding fragments thereof that can bind to the S protein of severe acute respiratory syndrome beta coronavirus (including multiple severe acute respiratory syndrome beta coronavirus in some specific embodiments) and can neutralize infection caused by multiple severe acute respiratory syndrome beta coronavirus in certain specific embodiments.

In late 2019, a new SARS betacoronavirus named SARS-CoV-2 emerged in Wuhan, China. SARS-CoV-2 and SARS-CoV are members of the SARS betacoronavirus family. SARS betacoronaviruses can be further divided into four clades: 1a, 1b, 2, and 3. SARS-CoV is a member of clade 1a, and SARS-CoV-2 is a member of clade 1b. There is a need for therapies to prevent or treat SARS betacoronavirus infection and for diagnostic reagents to diagnose SARS betacoronavirus infection.

The antibodies and antigen-binding fragments provided herein are capable of binding to SARS beta coronaviruses (e.g., SARS-CoV-2). In some embodiments, the antibodies or antigen-binding fragments are capable of binding to a plurality of SARS beta coronaviruses (e.g., to one or more (e.g., one, two, three, four, five, six, or more) different SARS beta coronaviruses as described herein, optionally contained on virus particles and/or on the surface of cells infected with two or more SARS beta coronaviruses). In certain embodiments, the plurality of SARS beta coronaviruses comprises one or more clade 1b SARS beta coronaviruses. In certain embodiments, the antibodies and antigen-binding fragments disclosed herein can neutralize infection caused by one or more SARS-betacoronaviruses (e.g., one, two, three, four, or more SARS-betacoronaviruses) in an in vitro model of infection and/or in an animal model and/or in a human subject. Polynucleotides encoding antibodies and antigen binding fragments, vectors, host cells, and related compositions are also provided, as well as methods of using antibodies, antigen binding fragments, polynucleotides, vectors, host cells, and related compositions to treat (e.g., reduce, delay, eliminate, or prevent) an individual's infection caused by two or more severe acute respiratory syndrome beta coronaviruses and/or for the manufacture of a drug for treating an individual's infection caused by two or more severe acute respiratory syndrome beta coronaviruses (e.g., one, two, three, four, or more severe acute respiratory syndrome beta coronaviruses). Combinations of two or more antibodies or antigen binding fragments are also provided, for example for use in therapy and/or prevention. Before describing the present disclosure in more detail, it may be helpful to first provide definitions of certain terms used herein. Additional definitions are set forth throughout this disclosure. As used herein, an "anti-sarbecovirus antibody or antigen-binding fragment" specifically binds to at least one sarbecovirus and, in some embodiments, may bind to two or more, three or more, four or more, or five or more sarbecoviruses. As used herein, "sarbecovirus" refers to any betacoronavirus within lineage B, and includes lineage B viruses in clade 1a, clade 1b, clade 2, and clade 3. Examples of clade 1a SARS beta coronaviruses are SARS-CoV and bat SARS-like coronavirus WIV1 (WIV1). Examples of clade 1b SARS beta coronaviruses are SARS-CoV-2, RatG13, pangolin-Guanxi-2017 (PANG/GX) and pangolin-Guangdon-2019 (PANG/GD). Embodiments of clade 1b also include SARS-CoV-2 variants, such as variants having any of the following mutations: A67V, Δ69-70, T95I, G142D, 137-145de, 143-145de, Y145H, N211I, Δ212, V213G, ins214TDR, ins215EPE, A222V, G339D, R346K, R346S, V367F, S371L, S373P, S375F, T376A, P384L, N394S, D405N, R408S, Q414K, K41 7N, K417V, K417T, N439K, N440K, G446S, Y449H, Y449N, L452R, L452Q, L452X (wherein X is any amino acid), Y453F, S477N, T478K, V483A, E484A, E484Q, E484K, E484X (wherein X is any amino acid), F490R, F486V, F490S, R493Q, Q493R, S494P, G496S, Q498R, N501Y, N501T, Y505H, E516Q, T547K, Q 613H, D614G, A653V, H655Y, G669S, Q677H, N679K, ins679GIAL, P681H, P681R, A701V, N764K, D796Y, N856K, Q954H, N969K, L981F, or variants in the following genealogies: B.1.1.7 and Q genealogies and subsequent genealogies (Alpha); B.1.351 and subsequent genealogies (Beta); B.1.429 and B.1.427 and subsequent genealogies (Epsilon); P.1 and subsequent genealogies (Gamma); B.1.1. 222; C.37; B.1.617.2; AY.1, AY.2, other AY series and later series (Delta); B.1.525 and later series (Eta); B.1.526 and later series (Iota); B.1.617.1 and later series (Kappa); 1.617.3; B.1.621, and B.1.621.1 and later series (Mu); P.2 (Zeta); and B.1.1.529.1, BA.1, BA.2, BA.2.12, BA.3, BA.4, BA.5 and later series (Omicron). Examples of clade 2 SARS beta coronaviruses are bat ZC45 (ZC45), bat ZXC21 (ZXC21), YN2013, RmYN02, Anlong112, SC2018, and SX2011. Examples of clade 3 SARS beta coronaviruses are BtkY72 and BGR2008. Figure 1It also explains the evolutionary clades of severe acute respiratory syndrome beta coronavirus and Figure 2 In some embodiments, the antibody or antigen-binding fragment thereof is capable of binding to a clade 1b SARS beta coronavirus, such as SARS-CoV-2 (including all variants described herein), RatG13, Pangolin-Guanxi-2017 (PANG/GX), Pangolin-Guangdon-209, or any combination thereof. In certain further embodiments, the antibody or antigen-binding fragment thereof is capable of binding to a SARS-CoV-2 variant; for example, embodiments of clade 1b of SARS-CoV-2 variants are also included, such as variants having any one or more of the following mutations: A67V, Δ69-70, T95I, G142D, 137-145de, 143-145de, Y145H, N211I, Δ212, V213G, ins214TDR, ins215EPE, A222V, G339D, R346K, R346S, V367F, S371L, S373P, S375F, T376A, P 384L, N394S, D405N, R408S, Q414K, K417N, K417V, K417T, N439K, N440K, G446S, Y449H, Y449N, L452R, L452Q, L452X (wherein X is any amino acid except L), Y453F, S477N, T478K, V483A, E484A, E484Q, E484K, E484X (wherein X is any amino acid except E), F490R, F486V, F490S, R493Q, Q493R, S494P, G496S, Q498R, N501Y, N501T, Y505H, E516Q, T547K, Q613H, D614G, A653V, H655Y, G669S, Q677H, N679K, ins679GIAL, P681H, P681R, A701V, N764K, D796Y, N856K, Q954H, N969K, L981F, or variants in the following lineages: B.1.1.7 and Q lineages and subsequent lineages (Alpha); B.1.351 and subsequent lineages (Beta); B.1.429 and B.1.427 and subsequent lineages (Epsilon); P.1 and subsequent lineages (Gamma ); B.1.1.222; C.37; B.1.617.2; AY.1, AY.2, other AY series, and subsequent series (Delta); B.1.525 and subsequent series (Eta); B.1.526 and subsequent series (Iota); B.1.617.1 and subsequent series (Kappa); 1.617.3; B.1.621, and B.1.621.1 and subsequent series (Mu); P.2 (Zeta); and B.1.1.529.1, BA.1, BA.2, BA.2.12, BA.3, BA.4, BA.5 and subsequent series (Omicron), or any combination thereof. In some embodiments, the SARS-Cov-2 variant is an Omicron variant, such as BA.1, BA.2, BA.2.12, BA.3, BA.4, or BA.5. In some embodiments, the antibody is (or the antigen-binding fragment is) S3A3, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3A3 or a variant disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S3A3 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of inhibiting the binding interaction between human ACE2 and severe acute respiratory syndrome beta coronavirus (e.g., SARS-CoV-2) receptor binding domain (RBD) with an IC50 of about 0.5 ng/mL to about 100 ng/mL, about 1 ng/mL to about 100 ng/mL, about 2.0 ng/mL to about 100 ng/mL, about 2.5 ng/mL to about 100 ng/mL, about 5.0 ng/mL to about 100 ng/mL, about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 1 ng/mL to about 50 ng/mL, about 2.0 ng/mL to about 50 ng/mL, about 2.5 ng/mL to about 50 ng/mL, about 5.0 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 In some embodiments, the antibody is (or the antigen-binding fragment is) S3A19, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3A19 or a variant disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S3A19 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of inhibiting the binding interaction between human ACE2 and severe acute respiratory syndrome beta coronavirus (e.g., SARS-CoV-2) receptor binding domain (RBD) with an IC50 of about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 18.5 ng/mL to about 100 ng/mL, about 19.5 ng/mL to about 100 ng/mL, about 20.0 ng/mL to about 100 ng/mL, about 21.5 ng/mL to about 100 ng/mL, about 22.5 ng/mL to about 100 ng/mL, about 24.5 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 26.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or about at least about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is) S3I2, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3I2 or a variant disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S3I2 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of inhibiting the binding interaction between human ACE2 and severe acute respiratory syndrome beta coronavirus (e.g., SARS-CoV-2) receptor binding domain (RBD) with an IC50 of about 0.5 ng/mL to about 100 ng/mL, about 1 ng/mL to about 100 ng/mL, about 2.0 ng/mL to about 100 ng/mL, about 2.5 ng/mL to about 100 ng/mL, about 5.0 ng/mL to about 100 ng/mL, about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 1 ng/mL to about 50 ng/mL, about 2.0 ng/mL to about 50 ng/mL, about 2.5 ng/mL to about 50 ng/mL, about 5.0 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is) S3O13, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3O13 or variants disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S3O13 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of inhibiting the binding interaction between human ACE2 and severe acute respiratory syndrome beta coronavirus (e.g., SARS-CoV-2) receptor binding domain (RBD) with an IC50 of about 0.5 ng/mL to about 100 ng/mL, about 1 ng/mL to about 100 ng/mL, about 2.0 ng/mL to about 100 ng/mL, about 2.5 ng/mL to about 100 ng/mL, about 5.0 ng/mL to about 100 ng/mL, about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 1 ng/mL to about 50 ng/mL, about 2.0 ng/mL to about 50 ng/mL, about 2.5 ng/mL to about 50 ng/mL, about 5.0 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is) S3L17, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3L17 or a variant disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S3L17 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of inhibiting the binding interaction between human ACE2 and severe acute respiratory syndrome beta coronavirus (e.g., SARS-CoV-2) receptor binding domain (RBD) with an IC50 of about 0.5 ng/mL to about 100 ng/mL, about 1 ng/mL to about 100 ng/mL, about 2.0 ng/mL to about 100 ng/mL, about 2.5 ng/mL to about 100 ng/mL, about 5.0 ng/mL to about 100 ng/mL, about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 1 ng/mL to about 50 ng/mL, about 2.0 ng/mL to about 50 ng/mL, about 2.5 ng/mL to about 50 ng/mL, about 5.0 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. As used herein, "S2V29" includes any VH and VL variants disclosed herein. In some embodiments, the antibody is (or the antigen-binding fragment is) S2V29, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S2V29 or a variant disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S2V29 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of inhibiting the binding interaction between human ACE2 and severe acute respiratory syndrome beta coronavirus (e.g., SARS-CoV-2) receptor binding domain (RBD) with an IC50 of about 0.5 ng/mL to about 100 ng/mL, about 1 ng/mL to about 100 ng/mL, about 2.0 ng/mL to about 100 ng/mL, about 2.5 ng/mL to about 100 ng/mL, about 5.0 ng/mL to about 100 ng/mL, about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 1 ng/mL to about 50 ng/mL, about 2.0 ng/mL to about 50 ng/mL, about 2.5 ng/mL to about 50 ng/mL, about 5.0 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. As used herein, "SARS-CoV-2" also known as "Wuhan coronavirus", "Wuhan seafood market pneumonia virus", "Wuhan CoV", "novel CoV", "nCoV", "2019 nCoV", "Wuhan nCoV", or its variants, is a lineage B betacoronavirus (severe acute respiratory syndrome betacoronavirus). SARS-CoV-2 was first identified in Wuhan, Hubei Province, China in late 2019 and spread in China and other parts of the world in early 2020. SARS CoV-2 infection can cause a disease called COVID-19; symptoms of COVID-19 include fever or chills, dry cough, difficulty breathing, fatigue, body aches, headache, new loss of taste or smell, sore throat, stuffy or runny nose, nausea or vomiting, diarrhea, persistent chest pressure or pain, new confusion, inability to wake up or stay awake, and bluish lips or face. The genomic sequence of the SARS-CoV-2 isolate Wuhan-Hu-1 is provided in GenBank MN908947.3 (January 23, 2020), and the amino acid transcripts of the genome are provided in GenBank QHD43416.1 (January 23, 2020). These GenBank sequences and the GenBank sequences of all SARS-CoV-2 variants are incorporated herein by reference as describing the severe acute respiratory syndrome beta coronavirus or SARS-CoV-2 to which the antibodies or antigen-binding fragments thereof according to the present disclosure specifically bind. Like other coronaviruses (e.g., SARS-CoV), SARS-CoV-2 contains a "spike" or surface ("S") type I transmembrane glycoprotein containing a receptor binding domain (RBD). The RBD is believed to mediate entry of lineage B SARS coronavirus into respiratory epithelial cells by binding to the cell surface receptor angiotensin-converting enzyme 2 (ACE2). In particular, the receptor binding motif (RBM) in the viral RBD is believed to interact with ACE2. The amino acid sequence of the Wuhan-Hu-1 surface glycoprotein is provided in SEQ ID NO: 1. The amino acid sequence of the Wuhan-Hu-1 RBD is provided in SEQ ID NO: 2. The Wuhan-Hu-1 S protein has approximately 73% amino acid sequence identity with SARS-CoV. The amino acid sequence of the Wuhan-Hu-1 RBM is provided in SEQ ID NO: 3. Many SARS-CoV-2 variants have emerged, which may differ in genome and amino acid sequence, particularly in surface glycoprotein or RBD. Some SARS-CoV-2 variant mutations increase affinity for ACE receptors and/or infectivity of the virus. Important variants of SARS-CoV-2 include embodiments of clade 1b of SARS-CoV-2 variants, such as variants having any of the following mutations: A67V, Δ69-70, T95I, G142D, 137-145de, 143-145de, Y145H, N211I, Δ212, V213G, ins214TDR, ins215EPE, A222V, G339D, R346K, R346S, V367F, S371L, S373P, S375F, T376A, P384L, N394S, D405N, R408S, Q414K, K417N, K417V, K417T, N439K, N440K, G446S, Y449H, Y449N, L452R, L452Q, L452X (wherein X is any amino acid except L), Y453F, S477N, T478K, V483A, E484A, E484Q, E484K, E484X (wherein X is any amino acid except E), F490R, F486V, F490S, R493Q, Q493R, S494P, G496S, Q498R, N501Y, N501T, Y505H, E51 6Q, T547K, Q613H, D614G, A653V, H655Y, G669S, Q677H, N679K, ins679GIAL, P681H, P681R, A701V, N764K, D796Y, N856K, Q954H, N969K, L981F, or variants in the following genealogies: B.1.1.7 and Q genealogies and subsequent genealogies (Alpha); B.1.351 and subsequent genealogies (Beta); B.1.429 and B.1.427 and subsequent genealogies (Epsilon); P.1 and subsequent genealogies (Gamma); B.1.1 .222; C.37; B.1.617.2; AY.1, AY.2, other AY series, and subsequent series (Delta); B.1.525 and subsequent series (Eta); B.1.526 and subsequent series (Iota); B.1.617.1 and subsequent series (Kappa); 1.617.3; B.1.621 and B.1.621.1 and subsequent series (Mu); P.2 (Zeta); and B.1.1.529.1, BA.1, BA.2, BA.2.12, BA.3, BA.4, BA.5 and subsequent series (Omicron), or any combination thereof. In some embodiments, the SARS-Cov-2 variant is an Omicron variant, such as BA.1, BA.2, BA.2.12, BA.3, BA.4, or BA.5. SARS-CoV-2 variants circulating in the United States are classified as variants of concern by the Centers for Disease Control and Prevention (see https://www.cdc.gov/coronavirus/2019-ncov/variants/variant-info.html). In some embodiments, antibodies or antigen-binding fragments for treating severe acute respiratory syndrome beta coronavirus infection are provided. In certain embodiments, severe acute respiratory syndrome beta coronavirus infection comprises SARS-CoV-2 infection. Treatment of SARS CoV-2 infection according to the present disclosure includes treatment of infection caused by any one or more of the aforementioned SARS-CoV-2 viruses. In certain embodiments, treating SARS-CoV-2 infection comprises treating any one or more of the following: SARS CoV-2 Wuhan-Hu-1; also including embodiments of clade 1b of SARS-CoV-2 variants, such as variants having any of the following mutations: A67V, Δ69-70, T95I, G142D, 137-145de, 143-145de, Y145H, N211I, Δ212, V213G, ins214TDR, ins215EPE, A222V, G339D, R346K, R346S, V367F, S371L, S373P, S375F, T376A, P384L, N394S, D405N, R408S, Q414K, K417 N, K417V, K417T, N439K, N440K, G446S, Y449H, Y449N, L452R, L452Q, L452X (wherein X is any amino acid except L), Y453F, S477N, T478K, V483A, E484A, E484Q, E484K, E484X (wherein X is any amino acid except E), F490R, F486V, F490S, R493Q, Q493R, S494P, G496S, Q498R, N501Y, N501T, Y505H, E516Q, T547K, Q613H, D614G, A653V, H655Y, G669S, Q677H, N679K, ins679GIAL, P681H, P681R, A701V, N764K, D796Y, N856K, Q954H, N969K, L981F, D614, E340A, or variants in the following genealogies: B.1.1.7 and Q genealogies and descendant genealogies (Alpha); B.1.351 and descendant genealogies (Beta); B.1.429 and B.1.427 and descendant genealogies (Epsilon); P.1 and descendant genealogies (Gamma); B.1.1.222; C. 37; B.1.617.2; AY.1, AY.2, other AY series, and subsequent series (Delta); B.1.525 and subsequent series (Eta); B.1.526 and subsequent series (Iota); B.1.617.1 and subsequent series (Kappa); 1.617.3; B.1.621 and B.1.621.1 and subsequent series (Mu); P.2 (Zeta); and B.1.1.529.1, BA.1, BA.2, BA.2.12, BA.3, BA.4, BA.5 and subsequent series (Omicron), BQ.1.1, XBB.1, or any combination thereof. In some embodiments, the SARS-CoV-2 variant is an Omicron variant, such as BA.1, BA.2, BA.2.12, BA.3, BA.4, or BA.5. In some embodiments, the SARS-CoV-2 variant is BQ.1.1. In some embodiments, the SARS-CoV-2 is XBB.1. In this specification, unless otherwise indicated, any concentration range, percentage range, ratio range, or integer range should be understood to include any integer value within the range, and (when appropriate) its fraction (such as one tenth and one hundredth of an integer). In addition, unless otherwise indicated, any numerical range described herein related to any physical characteristic (such as polymer subunits, size or thickness) should be understood to include any integer within the range. As used herein, unless otherwise indicated, the term "about" means ±20% of a specified range, value, or structure. It should be understood that, as used herein, the term "a/an" refers to "one or more" of the listed components. The use of alternatives (e.g., "or") should be understood to mean any one, two, or any combination of the alternatives. As used herein, the terms "include," "have," and "comprise" are used synonymously, and these terms and variations thereof are intended to be interpreted as non-restrictive. The term "optional" or "optionally" means that the subsequently described element, component, event, or condition may or may not occur, and the specification includes the occurrence and non-occurrence of the element, component, event, or condition. Furthermore, individual structures, or groups of structures, derived from various combinations of structures or subunits described herein are disclosed by the present application to the same extent as if each structure or group of structures were individually described. Thus, selection of a particular structure or a particular subunit is within the scope of the present disclosure. The term "consisting essentially of" is not equivalent to "comprising" and refers to specified materials or steps within the scope of the application, or materials or steps that do not materially affect the basic characteristics of the claimed subject matter. For example, a protein domain, region, or module (e.g., a binding domain) or protein "consists essentially of a particular amino acid sequence" when the amino acid sequence of the domain, region, module, or protein includes extensions, deletions, mutations, or combinations thereof (e.g., amino acids at the amino or carboxyl termini or between domains) that, taken together, account for up to 20% (e.g., up to 15%, 10%, 8%, 6%, 5%, 4%, 3%, 2%, or 1%) of the length of the domain, region, module, or protein and do not substantially affect (i.e., the activity is reduced by no more than 50%, such as no more than 40%, 30%, 25%, 20%, 15%, 10%, 5%, or 1%) the activity of one or more domains, one or more regions, one or more modules, or one or more proteins (e.g., the target binding affinity of the binding protein). As used herein, "amino acid" refers to naturally occurring and synthetic amino acids, as well as amino acid analogs and amino acid mimetics that function in a manner similar to naturally occurring amino acids. Naturally occurring amino acids are amino acids encoded by genetic codons, as well as those amino acids that are subsequently modified, such as hydroxyproline, γ-carboxyglutamine, and O-phosphoserine. Amino acid analogs refer to compounds that have the same basic chemical structure (i.e., α-carbon bound to hydrogen, carboxyl, amine, and R groups) as naturally occurring amino acids, such as serine, norleucine, methionine sulfoxide, and methionine methylsulfoxide. Such analogs have modified R groups (e.g., norleucine) or modified peptide backbones, but retain the same basic chemical structure as naturally occurring amino acids. Amino acid analogs refer to chemical compounds that have a structure that is different from the chemical structure of general amino acids, but function in a manner similar to naturally occurring amino acids. As used herein, "mutation" refers to a change in the sequence of a nucleic acid molecule or a polypeptide molecule compared to a reference or wild-type nucleic acid molecule or polypeptide molecule, respectively. Mutations can result in several different types of sequence changes, including substitutions, insertions, or deletions of one or more nucleotides or amino acids. "Reservation substitutions" refer to amino acid substitutions that do not significantly affect or change the binding properties of a particular protein. Generally speaking, a reservation substitution is one in which the substituted amino acid residue is replaced with an amino acid residue with a similar side chain. Conservative substitutions include substitutions found in one of the following groups: Group 1: alanine (Ala or A), glycine (Gly or G), serine (Ser or S), threonine (Thr or T); Group 2: aspartic acid (Asp or D), glutamine (Glu or Z); Group 3: asparagine (Asn or N), glutamine (Gln or Q); Group 4: arginine (Arg or R), lysine (Lys or K), histidine (His or H); Group 5: isoleucine (Ile or I), leucine (Leu or L), methionine (Met or M), valeric acid (Val or V); and Group 6: phenylalanine (Phe or F), tyrosine (Tyr or Y), tryptophan (Trp or W). Additionally or alternatively, amino acids can be grouped into conservative substitution groups by similar function, chemical structure, or composition (e.g., acidic, basic, aliphatic, aromatic, or sulfur-containing). For example, for substitution purposes, an aliphatic group can include Gly, Ala, Val, Leu, and Ile. Other reserved substitution groups include: sulfur-containing: Met and cysteine (Cys or C); acidic: Asp, Glu, Asn, and Gln; small aliphatic, nonpolar or slightly polar residues: Ala, Ser, Thr, Pro, and Gly; polar, negatively charged residues and their amides: Asp, Asn, Glu, and Gln; polar, positively charged residues: His, Arg, and Lys; large aliphatic, nonpolar residues: Met, Leu, Ile, Val, and Cys; and large aromatic residues: Phe, Tyr, and Trp. Additional information can be found in Creighton (1984) Proteins, W.H. Freeman and Company. As used herein, "protein" or "polypeptide" refers to a polymer of amino acid residues. Proteins are applicable to naturally occurring amino acid polymers, and to amino acid polymers in which one or more amino acid residues are artificial chemical analogs of naturally occurring amino acids, and non-naturally occurring amino acid polymers. Variants of the proteins, peptides, and polypeptides disclosed herein are also contemplated. In certain embodiments, the variant proteins, peptides, and polypeptides comprise or consist of the following: an amino acid sequence that is at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.9% identical to a defined amino acid sequence or a reference amino acid sequence as described herein. Any polypeptide disclosed herein (e.g., VH, VL, Fab, Fd, antibody heavy chain, antibody light chain) may be encoded by a polynucleotide sequence comprising a "signal peptide" (also referred to as a leader sequence, leader peptide, or transporter peptide). The signaling peptide targets the newly synthesized polypeptide to its appropriate location inside or outside the cell. The signaling peptide may be removed in whole or in part from the polypeptide during or after localization or secretion is completed. A polypeptide with a (e.g., full-length) signaling peptide may be referred to as a "pre-protein," and a polypeptide from which the signaling peptide has been removed - at least partially removed - may be referred to as a "mature" protein or polypeptide. In certain embodiments, the antibody or antigen-binding fragment is a mature protein or pre-protein. "Nucleic acid molecule" or "polynucleotide" or "polynucleic acid" refers to a polymeric compound comprising covalently linked nucleotides, which nucleotides may be composed of natural subunits (e.g., purine or pyrimidine bases) or non-natural subunits (e.g.,The nucleic acid molecules include polyribonucleic acid (RNA), including mRNA, microRNA, siRNA, viral genomic RNA, and synthetic RNA; and polydeoxyribonucleotide (DNA), including cDNA, genomic DNA, and synthetic DNA, any of which may be single-stranded or double-stranded. If single-stranded, the nucleic acid molecule may be a coding strand or a non-coding (antisense) strand. Nucleic acid molecules encoding amino acid sequences include all nucleotide sequences encoding the same amino acid sequence. Some forms of nucleotide sequences may also include one or more introns by removing one or more introns by co-transcriptional or post-transcriptional mechanisms. In other words, due to redundancy or simplification of the genetic code, or by splicing, different nucleotide sequences can encode the same amino acid sequence. Variants of the nucleic acid molecules disclosed herein are also contemplated. Variant nucleic acid molecules are at least 70%, 75%, 80%, 85%, 90%, and preferably 95%, 96%, 97%, 98%, 99%, or 99.9% identical to a defined nucleic acid molecule or reference polynucleotide as described herein, or hybridize with a polynucleotide under stringent hybridization conditions of 0.015M sodium chloride, 0.0015M sodium citrate at about 65 to 68°C or 0.015M sodium chloride, 0.0015M sodium citrate, and 50% formamide at about 42°C. Nucleic acid molecule variants retain the functionality described herein, such as the ability of their binding domains to bind to a target molecule. "Percent sequence identity" refers to the determination of the relationship between two or more sequences by comparing the sequences. The preferred method for determining sequence identity is designed to give the best match between the compared sequences. For example, the sequences are compared for the purpose of optimal comparison (e.g., a spacer can be introduced into one or both of the first and second amino acid or nucleic acid sequences to achieve optimal comparison). In addition, non-homologous sequences can be ignored for comparison purposes. Unless otherwise indicated, the percentage sequence identity mentioned herein is calculated based on the length of the reference sequence. Methods for determining sequence identity and similarity can be found in publicly available computer programs. Sequence alignment and percentage identity calculations can be performed using BLAST programs (e.g., BLAST 2.0, BLASTP, BLASTN, or BLASTX). The mathematical algorithms used in the BLAST program can be found in Altschul et al., Nucleic Acids Res. 25:3389-3402, 1997. In the context of this disclosure, it is understood that when sequence analysis software is used for analysis, the analysis results are based on the "default values" of the program mentioned. "Default values" means any value or parameter set that is initially loaded with the software when it is first initialized. Other embodiments include Clustal W, MAFFT, Clustal Omega, AlignMe, Praline, GAP, BESTFIT, Needle (EMBOSS), Stretcher (EMBOSS), GGEARCH2SEQ, Water (EMBOSS), Matcher (EMBOSS), LALIGN, and SSEARCH2SEQ. Global alignment algorithms such as Needleman and Wunsch algorithms can be used to align two sequences based on their entire lengths to maximize the number of matches and minimize the number of gaps. Default values can be used. To generate a similarity score for two amino acid sequences, a scoring matrix that assigns positive scores to some non-identical amino acids (e.g., amino acid substitutions that are conserved, amino acids that have similar physicochemical properties, and/or amino acids that exhibit frequent substitutions in heterologs, homologs, or homologs) can be used. Non-limiting examples of scoring matrices include PAM30, PAM70, PAM250, BLOSUM45, BLOSUM50, BLOUM62, BLOSUM80, and BLOSUM90. The term "isolated" means that a substance is removed from its original environment (e.g., the natural environment if it is naturally occurring). For example, a naturally occurring nucleic acid or polypeptide present in a living animal is not isolated, but the same nucleic acid or polypeptide isolated from some or all coexisting materials in the natural system is isolated. Such a nucleic acid can be part of a vector and/or such a nucleic acid or polypeptide can be part of a composition (e.g., a cell lysate) and still be isolated in that such a vector or composition is not part of the natural environment of the nucleic acid or polypeptide. The term "gene" means a segment of a DNA or RNA chain involved in producing a polypeptide chain; in certain contexts, it includes regions preceding or following the coding region (e.g., 5' untranslated regions (UTRs) and 3' UTRs) and intervening sequences (introns) between individual coding segments (exons). "Functional variant" refers to a compound that is structurally similar or substantially similar to the parent and reference compounds disclosed herein, but slightly different in composition (e.g., a base, atom or functional group is different, added, or removed), such that the polypeptide or the encoded polypeptide is able to perform at least one function of the parent polypeptide with at least 50% efficiency, preferably at least 55%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, 99.9%, or 100% activity level. In other words, when compared to the parent or reference polypeptide, the functional variant has a higher activity in a selected assay (e.g., an assay for measuring binding affinity, such as association (Ka) or dissociation (K _D) constants) in Biacore® or tetramer staining), the polypeptide or the functional variant encoding the polypeptide disclosed herein has "similar binding", "similar affinity" or "similar activity". As used herein, "functional portion" or "functional fragment" refers to a polypeptide or polynucleotide that only comprises a domain, part or fragment of a parent or reference compound, and the polypeptide or the encoded polypeptide retains at least 50% of the activity associated with the domain, part or fragment of the parent or reference compound, preferably at least 55%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, 99.9%, or 100% of the activity level of the parent polypeptide, or provides a biological benefit (e.g., effector function). When the functional part or fragment exhibits a performance reduction of no more than 50% in the selected assay compared to the parent or reference polypeptide (in terms of affinity, preferably no more than 20% or 10%, or no more than a logarithmic difference compared to the parent or reference), the polypeptide or the "functional part" or "functional fragment" encoding the polypeptide disclosed herein has "similar binding" or "similar activity". As used herein, the term "engineered", "recombinant", or "non-natural" refers to an organism, microorganism, cell, nucleic acid molecule, or vector that includes at least one genetic alteration or has been modified by the introduction of an exogenous or heterologous nucleic acid molecule, wherein such alteration or modification is introduced by genetic engineering (i.e., human intervention). Genetic alterations include, for example, modifications that introduce expressible nucleic acid molecules encoding functional RNA, proteins, fusion proteins, or enzymes, or additions, deletions, substitutions, or other functional disruptions of the genetic material of the cell by other nucleic acid molecules. Additional modifications include, for example, non-coding regulatory regions, wherein such modifications alter the expression of a polynucleotide, gene, or operator. As used herein, "heterologous" or "non-endogenous" or "exogenous" refers to any gene, protein, compound, nucleic acid molecule, or activity that is not native to a host cell or individual, or any gene, protein, compound, nucleic acid molecule, or activity that is native to a host cell or individual that has been altered. Heterologous, non-endogenous, or exogenous includes genes, proteins, compounds, or nucleic acid molecules that have been mutated or otherwise altered such that the structure, activity, or both are different between the native and altered genes, proteins, compounds, or nucleic acid molecules. In certain embodiments, heterologous, non-endogenous, or exogenous genes, proteins, or nucleic acid molecules (e.g., receptors, ligands, etc.) may not be endogenous to the host cell or individual, but nucleic acids encoding such genes, proteins, or nucleic acid molecules may be added to the host cell by conjugation, transformation, transfection, electroporation, etc., wherein the added nucleic acid molecule may be integrated into the host cell genome or may exist as extrachromosomal genetic material (e.g., as a plasmid or other self-replicating vector). The term "homologous" or "homolog" refers to a gene, protein, compound, nucleic acid molecule, or activity found in or derived from a host cell, species, or strain. For example, a heterologous or exogenous polynucleotide or gene encoding a polypeptide may be homologous to a native polynucleotide or gene and encode a homologous polypeptide or activity, but the polynucleotide or polypeptide may have an altered structure, sequence, expression level, or any combination thereof. Non-endogenous polynucleotides or genes, and encoded polypeptides or activities may be from the same species, a different species, or a combination thereof. In certain embodiments, a nucleic acid molecule native to a host cell or a portion thereof is considered heterologous to the host cell if it has been altered or mutated, or a nucleic acid molecule native to a host cell is considered heterologous to the host cell if it has been altered by a heterologous expression control sequence or by an endogenous expression control sequence that is not normally associated with a nucleic acid molecule native to the host cell. In addition, the term "heterologous" may refer to a biological activity that is different from, altered, or not endogenous to the host cell. As described herein, more than one heterologous nucleic acid molecule may be introduced into a host cell as a single nucleic acid molecule, as a plurality of individually controlled genes, as a polycistronic nucleic acid molecule, as a single nucleic acid molecule encoding a fusion protein, or any combination thereof. As used herein, the term "endogenous" or "native" refers to a polynucleotide, gene, protein, compound, molecule, or activity that is normally present in a host cell or individual. As used herein, the term "expression" refers to the process of producing a polypeptide based on the coding sequence of a nucleic acid molecule (such as a gene). Such processes include transcription, post-transcriptional control, post-transcriptional modification, translation, post-translational control, post-translational modification, or any combination thereof. The expressed nucleic acid molecule is generally operably linked to an expression control sequence (such as a promoter). The term "operably linked" refers to the process of producing a polypeptide based on the coding sequence of a nucleic acid molecule (such as a gene). "Linked" means that two or more nucleic acid molecules are attached to a single nucleic acid fragment so that the function of one is affected by the other. For example, when a promoter is able to affect the expression of a coding sequence, the promoter is operably linked to the coding sequence (i.e., the coding sequence is under the transcriptional control of the promoter). "Unlinked" means that the related genetic elements are not closely attached to each other, and the function of one does not affect the other. As described herein, more than one heterologous nucleic acid molecule can be introduced into a host cell as a single nucleic acid molecule, as a plurality of individually controlled genes, as a polycistronic nucleic acid molecule, as a single nucleic acid molecule encoding a protein (e.g., the heavy chain of an antibody), or any combination thereof. When two or more heterologous nucleic acid molecules are introduced into a host cell, it is understood that the two or more heterologous nucleic acid molecules can be introduced as a single nucleic acid molecule (e.g., on a single vector) on a separate vector and integrated into a single site or multiple sites in the host chromosome, or any combination thereof. The number of heterologous nucleic acid molecules or protein activities mentioned refers to the number of encoding nucleic acid molecules or the number of protein activities, not the number of individual nucleic acid molecules introduced into the host cell. The term "construct" refers to any polynucleotide containing a recombinant nucleic acid molecule (or, when the context clearly indicates, a fusion protein of the present disclosure). The (polynucleotide) construct may be present in a vector (e.g., a bacterial vector, a viral vector) or may be integrated into a genome. A "vector" is a nucleic acid molecule capable of transporting another nucleic acid molecule. For example, a vector may be a plasmid, a muscisome, a virus, an RNA vector, or a linear or circular DNA or RNA molecule, which may include chromosomal, non-chromosomal, semisynthetic or synthetic nucleic acid molecules. The vectors of the present disclosure also include transposon systems (e.g., Sleeping Beauty, see, e.g., Geurts et al., Mol. Ther. 8:108, 2003: March et al., Nat. Genet.41:753, 2009). Exemplary vectors are those capable of autonomous replication (episomal vectors), capable of delivering polynucleotides to the cell genome (e.g., viral vectors), or capable of expressing nucleic acid molecules to which they are linked (expression vectors). As used herein, "expression vector" or "vector" refers to a DNA construct containing a nucleic acid molecule that is operably linked to a suitable control sequence that enables expression of the nucleic acid molecule in a suitable host. Such control sequences include promoters that enable transcription, optional operator sequences that control such transcription, sequences encoding suitable mRNA ribosome binding sites, and sequences that control transcription and translation termination. A vector may be a plasmid, a phage particle, a virus, or simply a potential genomic insert. Once transformed into a suitable host, the vector can replicate and function independently of the host genome, or can in some cases integrate into the genome itself or deliver the polynucleotide contained in the vector to a genome that does not have the vector sequence. In this specification, "plastid", "expression plasmid", "virus", and "vector" are often used interchangeably. The term "introduced" in the context of inserting a nucleic acid molecule into a cell means "transfection", "transformation", or "transduction", and includes reference to the incorporation of a nucleic acid molecule into a eukaryotic cell or a prokaryotic cell, where the nucleic acid molecule can be incorporated into the cell's genome (e.g., chromosome, plastid, chromatin, or mitochondrial DNA), converted into an autonomous replicator, or transiently expressed (e.g., transfected mRNA). In certain embodiments, the polynucleotides disclosed herein can be operably linked to certain elements of a vector. For example, a polynucleotide sequence required to achieve expression and processing of the coding sequence to which it is joined can be operably linked. Expression control sequences can include appropriate transcriptional initiation, termination, promoter, and enhancer sequences; efficient RNA processing signals, such as splicing and polyadenylation signals; sequences that stabilize cytoplasmic mRNA; sequences that enhance translation efficiency (i.e., Kozak consensus sequences); sequences that enhance protein stability; and sequences that may enhance protein secretion. An expression control sequence can be operably linked if it is adjacent to the gene of interest and the expression control sequence acts in trans or at a distance to control the gene of interest. In certain embodiments, the vector comprises a plasmid vector or a viral vector (e.g., a lentiviral vector or a γ-retroviral vector). Viral vectors include retroviruses, adenoviruses, parvoviruses (e.g., adeno-associated viruses), coronaviruses, negative-stranded RNA viruses such as orthomyxoviruses (e.g., influenza virus), rhabdoviruses (e.g., rabies and vesicular stomatitis virus), paramyxoviruses (e.g., measles and Sendai virus), positive-stranded RNA viruses such as picornaviruses and alphaviruses, and double-stranded DNA viruses including adenoviruses, herpes simplex viruses (e.g., herpes simplex virus type 1 and type 2, Epstein-Barr virus, cytomegalovirus), and poxviruses (e.g., vaccinia, fowlpox, and canarypox). Other viruses include, for example, Norwalk virus, togavirus, flavivirus, reovirus, papovavirus, hepadnavirus, and hepatitis virus. Examples of retroviruses include avian leukemic sarcoma, mammalian C-type virus, B-type virus, D-type virus, HTLV-BLV group, lentivirus, foamy virus (Coffin, J. M., Retroviridae: The viruses and their replication, In Fundamental Virology, Third Edition, B. N. Fields et al., Eds., Lippincott-Raven Publishers, Philadelphia, 1996). A "retrovirus" is a virus with an RNA genome that is reverse transcribed into DNA using a reverse transcriptase enzyme, which is then incorporated into the host cell genome. A "gammaretrovirus" refers to a genus in the Retroviridae family. Examples of gammaretroviruses include mouse stem cell virus, murine leukemia virus, feline leukemia virus, feline sarcoma virus, and avian reticuloendothelial virus. "Lentiviral vectors" include HIV-based lentiviral vectors for gene delivery that can be integrating or non-integrating, have relatively large packaging capacity, and can transduce a range of different cell types. Lentiviral vectors are typically produced after three (packaging, envelope, and transfer) or more plasmids are temporarily transfected into production cells. Like HIV, lentiviral vectors enter target cells through the interaction of viral surface glycoproteins with receptors on the cell surface. After entry, the viral RNA undergoes reverse transcription, which is mediated by the viral reverse transcriptase complex. The product of reverse transcription is double-stranded linear viral DNA, which is the substrate for viral integration into the DNA of infected cells. In certain embodiments, the viral vector may be a gamma retrovirus, such as a vector derived from Moloney murine leukemia virus (MLV). In other embodiments, the viral vector may be a more complex retrovirus-derived vector, such as a lentivirus-derived vector. HIV-1-derived vectors belong to this category. Other embodiments include lentiviral vectors derived from HIV-2, FIV, equine infectious anemia virus, SIV, and Maedi-Visna virus (ovine lentivirus). Methods for transducing mammalian host cells with viral particles containing transgenes using retrovirus and lentiviral vectors and packaging cells are known in the art and have been previously described, for example, in the following documents: U.S. Patent No. 8,119,772; Walchli et al., PLoS One 6:327930, 2011; Zhao et al., J. Immunol.174:4415, 2005; Engels et al., Hum. Gene Ther. 14:1155, 2003; Frecha et al., Mol.Ther. 18:1748, 2010; and Verhoeyen et al., Methods Mol. Biol. 506:97, 2009. Retroviral and lentiviral vector constructs and expression systems are also commercially available. Other viral vectors can also be used for polynucleotide delivery including DNA viral vectors, such as adenovirus-based vectors and adeno-associated virus (AAV)-based vectors; vectors derived from herpes simplex virus (HSV), including amplicon vectors, replication-defective HSV and attenuated HSV (Krisky et al., Gene Ther.5:1517, 1998). Other vectors that can be used with the compositions and methods disclosed herein include vectors derived from bacilli and alpha viruses. (Jolly, DJ. 1999. Emerging Viral Vectors. pp 209-40 in Friedmann T. ed. The Development of Human Gene Therapy. New York: Cold Spring Harbor Lab), or plasmid vectors (such as sleeping beauty or other transposon vectors). When the viral vector genome comprises a plurality of polynucleotides to be expressed as separate transcripts in a host cell, the viral vector may also comprise additional sequences between two (or more) transcripts that allow bicistronic or polycistronic expression. Examples of such sequences for viral vectors include an internal ribosome entry site (IRES), a furin cleavage site, a viral 2A peptide, or any combination thereof. Further described herein are plasmid vectors, including plasmid vectors encoding DNA-based antibodies or antigen-binding fragments for direct administration to an individual. As used herein, the term "host" refers to a cell or microorganism targeted for genetic modification with a heterologous nucleic acid molecule to produce a polypeptide of interest, such as an antibody of the present disclosure. A host cell may include any individual cell or cell culture that can accept a vector or incorporate a nucleic acid or express a protein. The term also encompasses progeny of the host cell, whether genetically or phenotypically identical or different. Suitable host cells may depend on the vector and may include mammalian cells, animal cells, human cells, monkey cells, insect cells, yeast cells, and bacterial cells. These cells may be induced to incorporate vectors or other substances by the use of viral vectors, transformation by calcium phosphate precipitation, DEAE-polydextrose, electroporation, microinjection, or other methods. See, e.g., Sambrook et al., Molecular Cloning: A Laboratory Manual2d ed.(Cold Spring Harbor Laboratory, 1989). In the context of SARS-betacoronavirus infection, "host" refers to a cell or individual infected with SARS-betacoronavirus. As used herein, "antigen" or "Ag" refers to an immunogenic molecule that elicits an immune response. This immune response may involve antibody production, activation of specific immunologically competent cells, activation of complements, antibody-dependent cellular cytotoxicity, or any combination thereof. Antigens (immunogenic molecules) may be, for example, peptides, glycopeptides, polypeptides, glycopolypeptides, polynucleotides, polysaccharides, lipids, etc. Obviously, antigens may be synthetic, recombinantly produced, or derived from biological samples. Exemplary biological samples that may contain one or more antigens include tissue samples, fecal samples, cells, biological fluids, or combinations thereof. Antigens may be produced by cells that have been modified or genetically engineered to express the antigen. Antigens may also be present in SARS-betacoronavirus (surface glycoproteins or portions thereof), such as in viral particles, or expressed or presented on the surface of cells infected with SARS-betacoronavirus. The term "epitope" or "antigenic epitope" includes any molecule, structure, amino acid sequence, or protein determinant that is recognized and specifically bound by a cognate binding molecule such as an immunoglobulin, or other binding molecule, domain, or protein. Epitope determinants usually contain chemically active surface molecular groups (such as amino acids or sugar side chains) and may have specific three-dimensional structural properties as well as specific charge properties. When the antigen is or comprises a peptide or protein, the epitope may comprise consecutive amino acids (e.g., a linear epitope); or may comprise amino acids from different parts or regions of the protein that are brought into close proximity by protein folding (e.g., a discontinuous or conformational epitope); or non-adjacent amino acids in close proximity that are not associated with protein folding. Antibodies, antigen-binding fragments, and compositions In one aspect, the disclosure provides an isolated antibody, or an antigen-binding fragment thereof, that is capable of binding to a surface glycoprotein of a severe acute respiratory syndrome beta coronavirus (e.g., SARS-CoV-2). In some embodiments, the antibody or antigen-binding fragment is capable of binding to a surface glycoprotein of two or more severe acute respiratory syndrome beta coronaviruses, three or more severe acute respiratory syndrome beta coronaviruses, four or more severe acute respiratory syndrome beta coronaviruses, or five or more severe acute respiratory syndrome beta coronaviruses. In some embodiments, the antibody or antigen-binding fragment comprises a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3. In some embodiments, two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses comprise or one or more, or are selected from clade 1b severe acute respiratory syndrome beta coronaviruses or naturally occurring variants thereof, and any combination thereof. In certain embodiments, the antibody or antigen-binding fragment is capable of binding to the surface glycoproteins of two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses; for example, it is capable of binding when the surface glycoproteins of severe acute respiratory syndrome beta coronaviruses are expressed on the cell surface of host cells and/or on severe acute respiratory syndrome beta coronavirus virus particles. In certain embodiments, two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses are selected from SARS-CoV-2, PANG/GD, PANG/GX, RatG13, and naturally occurring variants thereof. In some embodiments, two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses include one or more of the SARS-CoV-2 variants. In certain further embodiments, the antibody or antigen-binding fragment thereof is capable of binding to one or more SARS-CoV-2 variants. Embodiments of clade 1b also include SARS-CoV-2 variants, such as variants having any of the following mutations: A67V, Δ69-70, T95I, G142D, 137-145de, 143-145de, Y145H, N211I, Δ212, V213G, ins214TDR, ins215EPE, A222V, G339D, R346K, R346S, V367F, S371L, S373P, S375F, T376A, P384L, N394S, D405N, R408S, Q414K, K417N, K417V, K417T, N439K, N440K, G446S, Y449H, Y449N, L452R, L452Q, L452X (wherein X is any amino acid except L), Y453F, S477N, T478K, V483A, E484A, E484Q, E484K, E484X (wherein X is any amino acid except E), F490R, F486V, F490S, R493Q, Q493R, S494P, G496S, Q498R, N501Y, N501T, Y505H, E516Q, T547K, Q613H, D61 4G, A653V, H655Y, G669S, Q677H, N679K, ins679GIAL, P681H, P681R, A701V, N764K, D796Y, N856K, Q954H, N969K, L981F, D614, E340A, or variants in the following genealogies: B.1.1.7 and Q genealogies and subsequent genealogies (Alpha); B.1.351 and subsequent genealogies (Beta); B.1.429 and B.1.427 and subsequent genealogies (Epsilon); P.1 and subsequent genealogies (Gamma); B.1.1.222; C .37; B.1.617.2; AY.1, AY.2, other AY series and later series (Delta); B.1.525 and later series (Eta); B.1.526 and later series (Iota); B.1.617.1 and later series (Kappa); 1.617.3; B.1.621 and B.1.621.1 and later series (Mu); P.2 (Zeta); and B.1.1.529.1, BA.1, BA.2, BA.2.12, BA.3, BA.4, BA.5 and later series (Omicron); BQ.1.1; XBB.1. In some embodiments, two or more, three or more, four or more, or five or more SARS-CoV-2 beta coronaviruses include one or more SARS-CoV-2 variants with the following S protein mutations: D614G, Q493R, G496S, Q498R, N501Y, Y453F, N439K, K417V, E484K, or any combination thereof. In some embodiments, two or more SARS-CoV-2 beta coronaviruses include one or more SARS-CoV-2 variants with the following S protein mutations: K417N, Q493K, G496S, or any combination thereof. In certain embodiments, the antibody or antigen-binding fragment disclosed herein binds or associates with a severe acute respiratory syndrome beta coronavirus surface glycoprotein epitope or an antigen comprising the epitope, but does not significantly bind or associate with any other molecule or component in the sample. In some embodiments, the epitope is contained in the S1 subunit of the S protein. In further embodiments, the epitope is contained in the RBD of the S protein. In some embodiments, the epitope is a conformational epitope or a linear epitope. In certain embodiments, the antibody or antigen-binding fragment disclosed herein binds or associates (e.g., binds) with a first severe acute respiratory syndrome beta coronavirus surface glycoprotein epitope, and may also bind or associate with an epitope from another severe acute respiratory syndrome beta coronavirus present in the sample, but does not significantly bind or associate with any other molecule or component in the sample. In other words, in certain embodiments, the antibody or antigen-binding fragment disclosed herein is cross-reactive and specifically binds to two or more severe acute respiratory syndrome beta coronaviruses (e.g., SARS-CoV-2 Wuhan-Hu-1 and one or more variants thereof). In certain embodiments, the antibody or antigen-binding fragment disclosed herein specifically binds to severe acute respiratory syndrome beta coronavirus surface glycoprotein. As used herein, "specifically bind" refers to the affinity or K of an antibody or antigen-binding fragment to bind or associate with an antigen._a(i.e., the equilibrium constant of a specific binding interaction, expressed in 1/M) equal to or greater than 10 ⁵M ^-1(It is equal to the on-rate of this on-reaction [K _on] for the dissociation rate (off rate) [K _off] ratio), but does not significantly bind or associate with any other molecule or component in the sample. Alternatively, affinity can be defined as the equilibrium dissociation constant (K) of a specific binding interaction._d), the unit is M (for example 10 ^-5M to 10 ^-13M). Antibodies can be classified as either "high affinity" antibodies or "low affinity" antibodies. "High affinity" antibodies are antibodies with at least 10 ⁷M ^-1, at least 10 ⁸M ^-1, at least 10 ⁹M ^-1, at least 10 ¹⁰M ^-1, at least 10 ¹¹M ^-1, at least 10 ¹²M ^-1, or at least 10 ¹³M ^-1K _a"Low affinity" antibodies are antibodies with a binding affinity of at most 10 ⁷M ^-1, up to 10 ⁶M ^-1, up to 10 ⁵M ^-1K _aof those antibodies. Alternatively, affinity can be defined as the equilibrium dissociation constant (K _d), the unit is M (for example 10 ^-5M to 10 ^-13M). Various assays are known for identifying antibodies disclosed herein that bind to specific targets, and for determining the affinity of binding domains or binding proteins, such as Western blots, ELISA (e.g., direct, indirect, or sandwich), analytical ultracentrifugation, spectroscopy, and surface plasmon resonance (Biacore®) analysis (see, e.g., Scatchard et al., Ann. NY Acad. Sci. 51:660, 1949; Wilson, Science 295:2103, 2002; Wolff et al., Cancer Res.53:2560, 1993; and U.S. Patent Nos. 5,283,173, 5,468,614, or equivalents). Assays for assessing affinity or apparent affinity or relative affinity are also known. In certain embodiments, the antibodies or antigen-binding fragments of the present disclosure bind to one or more, or two or more clade 1b SARS-CoV-2 with an EC50 of about 0.5 ng/mL to about 100 ng/mL, about 1 ng/mL to about 100 ng/mL, about 2.0 ng/mL to about 100 ng/mL, about 2.5 ng/mL to about 100 ng/mL, about 5.0 ng/mL to about 100 ng/mL, about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 16.0 ng/mL to about 100 ng/mL, about 18.0 ng/mL to about 100 ng/mL, about 19.0 ng/mL to about 100 ng/mL, about 20.0 ng/mL to about 100 ng/mL, about 21.0 ng/mL to about 100 ng/mL, about 23.0 ng/mL to about 100 ng/mL, about 24.0 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 1 ng/mL to about 50 ng/mL, about 2.0 ng/mL to about 50 ng/mL, about 2.5 ng/mL to about 50 ng/mL, about 5.0 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, which can be measured by ELISA. In some embodiments, the antibody or antigen-binding fragment binds to the spike (S) protein RBD from one, two, three, four, or five severe acute respiratory syndrome beta coronaviruses. In some embodiments, the antibody or antigen-binding fragment is capable of binding to the first and second severe acute respiratory syndrome beta coronaviruses each independently selected from clade 1b, wherein the antibody or antigen-binding fragment is capable of binding to the first severe acute respiratory syndrome beta coronavirus with an EC50 of about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, and is capable of binding to SARS-CoV-2 beta coronavirus with the following EC50: about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is) S3A3, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3A3 or variants disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3A3 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of binding to SARS-CoV-2 RBD with a KD of about 1.0 x 10 ^-09M and about 1.0 x 10 ^-08M, about 1.2 x 10 ^-09M and about 1.0 x 10 ^-08M, about 1.5 x 10 ^-09M and about 1.0 x 10 ^-08M, about 2.0 x 10 ^-09M and about 1.0 x 10 ^-08M, about 2.25 x 10 ^-09M and about 1.0 x 10 ^-08M, about 2.5 x 10 ^-09M and about 1.0 x 10 ^-08M, about 3.0 x 10 ^-09M and about 1.0 x 10 ^-08M, about 3.5 x 10 ^-09M and about 1.0 x 10 ^-08M, about 4.0 x 10 ^-09M and about 1.0 x 10 ^-08M, about 4.5 x 10 ^-09M and about 1.0 x 10 ^-08M, or about 5.0 x 10 ^-09M and about 1.0 x 10 ^-08M, about 1.0 x 10 ^-09M, or about 1.2 x 10 ^-09M, about 1.5 x 10 ^-09M, about 2.0 x 10 ^-09M, about 2.25 x 10 ^-09M, about 2.5 x 10 ^-09M, about 3.0 x 10 ^-09M, about 4.0 x 10 ^-09M, about 4.5 x 10 ^-09M, or about 5.0 x 10 ^-09M, or not more than approximately 1.0 x 10 ^-09M, or about 1.2 x 10 ^-09M, about 1.5 x 10 ^-09M, about 2.0 x 10 ^-09M, about 2.25 x 10 ^-09M, about 2.5 x 10 ^-09M, about 3.0 x 10 ^-09M, about 4.0 x 10 ^-09M, about 4.5 x 10 ^-09M, or about 5.0 x 10 ^-09M, as can be determined by biotin interferometry (e.g., using Octet). In some embodiments, the antibody is (or the antigen-binding fragment is) S3A19, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S3A19 or variants disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3A19 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of binding to SARS-CoV-2 RBD with a KD of about 1.0 x 10 ^-12M and about 5.0 x 10 ^-08M, about 1.5 x 10 ^-12M and about 5.0 x 10 ^-08M, about 2.0 x 10 ^-12M and about 5.0 x 10 ^-08M, about 2.25 x 10 ^-12M and about 5.0 x 10 ^-08M, about 2.5 x 10 ^-12M and about 5.0 x 10 ^-08M, about 1.0 x 10 ^-11M and about 5.0 x 10 ^-08M, about 1.0 x 10 ^-10M and about 5.0 x 10 ^-08M, about 1.0 x 10 ^-09M and about 5.0 x 10 ^-08M, about 1.0 x 10 ^-08M and about 5.0 x 10 ^-08M, about 1.0 x 10 ^-12M, or about 1.5 x 10 ^-12M, about 2.0 x 10 ^-12M, about 2.25 x 10 ^-12M, about 2.5 x 10 ^-12M, about 1.0 x 10 ^-11M, about 1.0 x 10 ^-10M, about 1.0 x 10 ^-09M, or not more than approximately 1.0 x 10 ^-12M, or about 1.5 x 10 ^-12M, about 2.0 x 10 ^-12M, about 2.25 x 10 ^-12M, about 2.5 x 10 ^-12M, about 1.0 x 10 ^-11M, about 1.0 x 10 ^-10M, about 1.0 x 10 ^-09M, as can be determined by biotin interferometry (e.g., using Octet). In some embodiments, the antibody is (or the antigen-binding fragment is) S3I2, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S3I2 or variants disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3I2 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of binding to an antigen at about 1.0 x 10 ^-12M and about 5.0 x 10 ^-08M and bind to SARS-CoV-2 RBD with a KD in the range of about 1.0 x 10. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3O13, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S3O13 or variants disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3O13 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of binding to SARS-CoV-2 RBD at about 1.0 x 10^-12M and about 5.0 x 10 ^-08M and bind to SARS-CoV-2 RBD with a KD in the range of about 1.0 x 10 In some embodiments, the antibody is (or the antigen-binding fragment is) S3L17, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S3L17 or variants disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3L17 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of binding to SARS-CoV-2 RBD at about 1.0 x 10 ^-12M and about 5.0 x 10 ^-08M for binding to the SARS-CoV-2 RBD. In certain embodiments, binding can be determined by recombinantly expressing SARS-CoV-2 antigens in host cells (e.g., by transfection) and immunostaining the host cells with the antibody (e.g., fixed, or fixed and pre-permeabilized), and analyzing by flow cytometry (e.g., using a ZE5 cytometer (BioRad®) and FlowJo software (TreeStar)). In some specific embodiments, positive binding can be defined by differential staining of cells expressing SARS-CoV-2 versus control (e.g., mock) cells with the antibody. In some embodiments, the antibodies or antigen-binding fragments of the present disclosure bind to SARS-CoV-2 spike proteins (i.e., from two or more, three or more, four or more, or five or more SARS-CoV-2 beta-coronaviruses) expressed on the surface of host cells (e.g., Expi-CHO cells) as measured by flow cytometry. In some embodiments, the antibodies or antigen-binding fragments of the present disclosure bind to SARS-CoV-2 S protein as measured using bio-thin layer interferometry. In certain embodiments, the antibodies of the present disclosure are capable of neutralizing infection caused by one or more, or by two or more SARS-CoV-2 beta-coronaviruses. As used herein, a "neutralizing antibody" is an antibody that neutralizes, i.e., prevents, inhibits, reduces, blocks or interferes with the ability of a pathogen to initiate and/or maintain infection in a host. The terms "neutralizing antibody" and "an antibody that neutralizes/antibodies that neutralize" are used interchangeably herein. In any of the currently disclosed embodiments, the antibody or antigen-binding fragment is capable of preventing and/or neutralizing infection caused by one or more, or by two or more, SARS-beta coronaviruses in an in vitro model of infection and/or in an in vivo animal model of infection and/or in humans. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3A3, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3A3 or a variant disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S3A3 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of neutralizing infection by SARS-CoV-2 in a pseudovirus system (e.g., MLV-pp-based or VSV-pp-based) at about 0.5 ng/mL to about 100 ng/mL, about 1 ng/mL to about 100 ng/mL, about 2.0 ng/mL to about 100 ng/mL, about 2.5 ng/mL to about 100 ng/mL, about 5.0 ng/mL to about 100 ng/mL, about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 11.0 ng/mL to about 11.0 ng/mL ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 1 ng/mL to about 50 ng/mL, about 2.0 ng/mL to about 50 ng/mL, about 2.5 ng/mL to about 50 ng/mL, about 5.0 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is) S3A19, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3A19 or a variant disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S3A19 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of neutralizing infection by SARS-CoV-2 in a pseudovirus system (e.g., MLV-pp-based or VSV-pp-based) at about 7.5 ng/mL to about 100 ng/mL, about 8.0 ng/mL to about 100 ng/mL, about 9.0 ng/mL to about 100 ng/mL, about 10.0 ng/mL to about 100 ng/mL, about 12.5 ng/mL to about 100 ng/mL, about 15.0 ng/mL to about 100 ng/mL, about 17.5 ng/mL to about 100 ng/mL, about 20 ng/mL to about 100 ng/mL, about 25 ng/mL to about 100 ng/mL, about 26 ng/mL to about 100 ng/mL, about 28 ng/mL to about 100 ng/mL, about 29 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 31 ng/mL to about 100 ng/mL, about 32 ng/mL to about 100 ng/mL, about 33 ng/mL to about 100 ng/mL, about 34 ng/mL to about 100 ng/mL, about 35 ng/mL to about 100 ng/mL, about 36 ng/mL to about 100 ng/mL, about 37 ng/mL to about 100 ng/mL, about 38 ng/mL to about 100 ng/mL ng/mL, about 25.0 ng/mL to about 100 ng/mL, about 27.5 ng/mL to about 100 ng/mL, about 30 ng/mL to about 100 ng/mL, about 0.5 ng/mL to about 50 ng/mL, about 7.5 ng/mL to about 50 ng/mL, about 8.0 ng/mL to about 50 ng/mL, about 9.0 ng/mL to about 50 ng/mL, about 10.0 ng/mL to about 50 ng/mL, about 12.5 ng/mL to about 50 ng/mL, about 15.0 ng/mL to about 50 ng/mL, about 17.5 ng/mL to about 50 ng/mL, about 20 ng/mL to about 50 ng/mL, about 25.0 ng/mL to about 50 ng/mL, about 27.5 ng/mL to about 50 ng/mL, or in the range of about 30 ng/mL to about 50 ng/mL, about 0.5 ng/mL, about 0.9 ng/mL, about 1.0 ng/mL, about 1.25 ng/mL, about 1.5 ng/mL, about 1.75 ng/mL, about 2.0 ng/mL, about 2.25 ng/mL, about 2.5 ng/mL, about 3.0 ng/mL, about 4.0 ng/mL, about 5.0 ng/mL, about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL, or at least about 7.5 ng/mL, about 8.0 ng/mL, about 9.0 ng/mL, about 10.0 ng/mL, about 12.5 ng/mL, about 15.0 ng/mL, about 17.5 ng/mL, about 20.0 ng/mL, about 22.5 ng/mL, about 25.0 ng/mL, about 27.5 ng/mL, or about 30 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3I2, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3I2 or a variant disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3I2 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of neutralizing infection caused by SARS-CoV-2 in a pseudoviral system (e.g., MLV-pp-based or VSV-pp-based) in the range of about 0.5 ng/mL to about 100 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3O13, or the antibody or antigen-binding fragment comprises CDRs and, optionally, VH and VL of S3O13 or variants disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3O13 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of neutralizing infection by SARS-CoV-2 in a pseudoviral system (e.g., MLV-pp-based or VSV-pp-based) in the range of about 0.5 ng/mL to about 100 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is) S3L17, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S3L17 or variants disclosed herein. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3L17 or variants disclosed herein to confer similar specific binding, or fragments thereof, and is capable of neutralizing infection by SARS-CoV-2 in a pseudoviral system (e.g., MLV-pp-based or VSV-pp-based) in the range of about 0.5 ng/mL to about 100 ng/mL. In some embodiments, the antibody is (or the antigen-binding fragment is from) S2V29, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S2V29 or variants disclosed herein. In some embodiments, the antibodies comprise sufficient CDR, VH, and/or VL identity to S2V29 or variants disclosed herein to confer similar specific binding, or fragments thereof, and are capable of neutralizing infection by SARS-CoV-2 in a pseudovirus system (e.g., MLV-pp-based or VSV-pp-based) within a range of about 0.5 ng/mL to about 100 ng/mL. In certain embodiments, the antibody or antigen-binding fragment (i) recognizes an epitope in the spike protein of two or more severe acute respiratory syndrome beta coronaviruses; (ii) is capable of blocking the interaction between the spike protein of one or more severe acute respiratory syndrome beta coronaviruses and a cell surface receptor; (iii) recognizes an epitope retained in the spike protein of two or more severe acute respiratory syndrome beta coronaviruses; (iv) is cross-reactive against two or more severe acute respiratory syndrome beta coronaviruses; or (v) any combination of (i) to (iv). Unless otherwise expressly defined herein, terms in the field of antibody technology that are understood by a person of ordinary skill in the art each have the meaning given to them in the art. For example, the term "antibody" refers to an intact antibody comprising at least two heavy (H) chains and two light (L) chains interconnected by disulfide bonds, and any antigen-binding portion or fragment of an intact antibody that has or retains the ability to bind to an antigen target molecule recognized by the intact antibody, such as a scFv, Fab, or Fab'2 fragment. Therefore, the term "antibody" herein is used in the broadest sense and includes polyclonal and monoclonal antibodies, including intact antibodies and functional (antigen-binding) antibody fragments thereof, including fragment antigen-binding fragment (Fab) fragments, F(ab')2 fragments, Fab' fragments, Fv fragments, recombinant IgG (rIgG) fragments, single-chain antibody fragments, including single-chain variable fragments (scFv), and single-domain antibody (e.g., sdAb, sdFv, nanobody) fragments. The term covers genetically engineered and/or otherwise modified forms of immunoglobulins, such as intrabodies, peptibodies, chimeric antibodies, fully human antibodies, humanized antibodies, and heteroconjugate antibodies, multispecific (e.g., bispecific) antibodies, bifunctional antibodies, trifunctional antibodies, tetrafunctional antibodies, tandem di-scFvs, and tandem tri-scFvs. Unless otherwise specified, the term "antibody" should be understood to cover functional antibody fragments thereof. The term also covers intact or full-length antibodies, including antibodies of any class or subclass, including IgG and its subclasses (IgG1, IgG2, IgG3, IgG4), IgM, IgE, IgA, and IgD. The term "V _L" or "VL" and "V _H" or "VH" refers to the variable binding region from the antibody light chain and the antibody heavy chain, respectively. In some embodiments, the VL is of the kappa class (also referred to herein as "VK"). In some embodiments, the VL is of the lambda class. The variable binding region comprises discrete, well-defined subregions, referred to as "complementarity determining regions" (CDRs) and "framework regions" (FRs). The terms "complementarity determining region" and "CDR" are synonymous with "hypervariable region" or "HVR", and refer to amino acid sequences within the variable region of an antibody that generally together confer antigen specificity and/or binding affinity to the antibody, wherein in the primary structure, consecutive CDRs (i.e., CDR1 and CDR2, CDR2 and CDR3) are separated from each other by framework regions. There are three CDRs in each variable region (HCDR1, HCDR2, HCDR3; LCDR1, LCDR2, LCDR3; also referred to as CDRH and CDRL, respectively). In certain embodiments, the antibody VH comprises the following four FRs and three CDRs: FR1-HCDR1-FR2-HCDR2-FR3-HCDR3-FR4, and the antibody VL comprises the following four FRs and three CDRs: FR1-LCDR1-FR2-LCDR2-FR3-LCDR3-FR4. Typically, VH and VL together form an antigen binding site through their individual CDRs. In any of the currently disclosed embodiments, the antibody or antigen-binding fragment is capable of preventing and/or neutralizing infection caused by one or more, or by two or more severe acute respiratory syndrome beta coronaviruses in an in vitro model of infection and/or in an in vivo animal model of infection and/or in humans. In certain embodiments, antibodies or antigen-binding fragments comprising VH and VL are provided, wherein the VH and VL respectively comprise or consist of the following amino acid sequences: 1) SEQ ID NOs: 23 and 27; 2) SEQ ID NOs: 23 and 37; 3) SEQ ID NOs: 31 and 27; 4) SEQ ID NOs: 31 and 37; 5) SEQ ID NOs: 35 and 27; 6) SEQ ID NOs: 35 and 37; 7) SEQ ID NOs: 36 and 27; 8) SEQ ID NOs: 36 and 37; 9) SEQ ID NOs: 43 and 27; 10) SEQ ID NOs: 43 and 37; 11) SEQ ID NOs: 83 and 87; 12) SEQ ID NOs: 83 and 193; 13) SEQ ID NOs: 179 and 87; 14) SEQ ID NOs: 17) SEQ ID NO: 181 and 87; 18) SEQ ID NO: 181 and 87; 19) SEQ ID NO: 183 and 193; 20) SEQ ID NO: 185 and 87; 21) SEQ ID NO: 185 and 87; 22) SEQ ID NO: 190 and 87; 23) SEQ ID NO: 190 and 193; 24) SEQ ID NO: 93 and 97; 25) SEQ ID NO: 93 and 225; 26) SEQ ID NO: 93 and 228; 27) SEQ ID NO: 93 and 231; 28) SEQ ID NO: 41) SEQ ID NO: 207 and 225; 42) SEQ ID NO: 207 and 228; 43) SEQ ID NO: 54) SEQ ID NO: 214 and 228; 55) SEQ ID NO: 214 and 231; 56) SEQ ID NO: 216 and 97; 57) SEQ ID NO: 216 and 225; 58) SEQ ID NO: 69) SEQ ID NO: 222 and 225; 70) SEQ ID NO: 222 and 228; 71) SEQ ID NO: 222 and 231; 72) SEQ ID NO: 102 and 105; 73) SEQ ID NO: 106 and 107; 74) SEQ ID NO: 108 and 109; 75) SEQ ID NO: 112 and 113; 76) SEQ ID NO: 114 and 115; 77) SEQ ID NO: 115 and 116; 78) SEQ ID NO: 116 and 228; 79) SEQ ID NO: 216 and 231; 80) SEQ ID NO: 218 and 97; 81) SEQ ID NO: 218 and 225; 82) SEQ ID NO: 218 and 228; 83) SEQ ID NO: 218 and 231; 84) SEQ ID NO: 220 and 97; 85) SEQ ID NO: 220 and 225; 86) SEQ ID NO: 220 and 228; 87) SEQ ID NO: 220 and 231; 88) SEQ ID NO: 222 and 97; 7) SEQ ID NO: 235 and 260; 80) SEQ ID NO: 238 and 105; 81) SEQ ID NO: 238 and 254; 82) SEQ ID NO: 238 and 257; 83) SEQ ID NO: 238 and 260; 84) SEQ ID NO: 241 and 105; 85) SEQ ID NO: 241 and 254; 86) SEQ ID NO: 241 and 257; 87) SEQ ID NO: 97) SEQ ID NO: 247 and 254; 98) SEQ ID NO: 247 and 257; 99) SEQ ID NO: 247 and 260; 100) SEQ ID NO: 249 and 105; 101) SEQ ID NO: 10) SEQ ID NO: 111 and 121; 110) SEQ ID NO: 111 and 157; 111) SEQ ID NO: 111 and 272; 112) SEQ ID NO: 111 and 277; 113) SEQ ID NO: 111 and 279; 114) SEQ ID NO: 111 and 282; 115) SEQ ID NO: 111 and 282; 125) SEQ ID NO: 125 and 290; 126) SEQ ID NO: 128 and 115; 127) SEQ ID NO: 128 and 121; 128) SEQ ID NO: 128 and 157; 129) SEQ ID NO: 129 and 272; 130) SEQ ID NO: 129 and 277; 131) SEQ ID NO: 129 and 279; 132) SEQ ID NO: 129 and 282; 133) SEQ ID NO: 129 and 286; 134) SEQ ID NO: 129 and 290; 135) SEQ ID NO: 128 and 115; 136) SEQ ID NO: 128 and 121; 137) SEQ ID NO: 128 and 157; 138) SEQ ID NO: 128 and 157; 139) SEQ ID NO: 129 and 272; 140) SEQ ID NO: 129 and 277; 141) SEQ ID NO: 129 and 279; 142) SEQ ID NO: 129 and 282; 143) SEQ ID NO: 129 and 286; 144) SEQ ID NO: 129 and 290; 145) SEQ ID NO: 129 and 291; 146) SEQ ID NO: 12 136) SEQ ID NO: 131 and 272; 137) SEQ ID NO: 131 and 277; 138) SEQ ID NO: 131 and 279; 139) SEQ ID NO: 131 and 282; 140) SEQ ID NO: 131 and 286; 141) SEQ ID NO: 131 and 290; 142) SEQ ID NO: 134 and 115; 143) SEQ ID NO: 134 and 121; 144) SEQ ID NO: 134 and 157; 145) SEQ ID NO: 134 and 272; 146) SEQ ID NO: 134 and 277; 147) SEQ ID NO: 134 and 279; 148) SEQ ID NO: 134 and 282; 149) SEQ ID NO: 134 and 286; 150) SEQ ID NO: 134 and 290; 151) SEQ ID NO: 137 and 115; 152) SEQ ID NO: 137 and 121; 153) SEQ ID NO: 137 and 157; 154) SEQ ID NO: 137 and 272; 155) SEQ ID NO: 156) SEQ ID NO: 137 and 279; 157) SEQ ID NO: 137 and 282; 158) SEQ ID NO: 137 and 286; 159) SEQ ID NO: 137 and 290; 160) SEQ ID NO: 141 and 115; 161) SEQ ID NO: 141 and 121; 162) SEQ ID NO: 141 and 157; 162) SEQ ID NO: 141 and 272; 162) SEQ ID NO: 141 and 277; 163) SEQ ID NO: 141 and 279; 164) SEQ ID NO: 141 and 282; 165) SEQ ID NO: 141 and 286; 166) SEQ ID NO: 141 290; 167) SEQ ID NO: 141 176) SEQ ID NO: 145 and 290; 177) SEQ ID NO: 149 and 115; 178) SEQ ID NO: 149 and 121; 179) SEQ ID NO: 149 and 157; 170) SEQ ID NO: 149 and 272; 171) SEQ ID NO: 149 and 277; 172) SEQ ID NO: 149 and 279; 173) SEQ ID NO: 149 and 282; 174) SEQ ID NO: 149 and 282; 175) SEQ ID NO: 149 and 286; 176) SEQ ID NO: 149 and 290; 177) SEQ ID NO: 149 and 115; 178) SEQ ID NO: 149 and 121; 179) SEQ ID NO: 149 and 157; 180) SEQ ID NO: 149 and 272; 181) SEQ ID NO: 149 and 277; 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 153 and 115; 187) SEQ ID NO: 153 and 121; 188) SEQ ID NO: 153 and 157; 189) SEQ ID NO: 153 and 272; 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 264 and 115; 196) SEQ ID NO: 264 and 121; 197) SEQ ID NO: 264 and 157; 198) SEQ ID NO: 264 and 272; 199) SEQ ID NO: 264 and 277; 200) SEQ ID NO: 264 and 279; 201) SEQ ID NO: 264 and 282; 202) SEQ ID NO: 264 and 286; 203) SEQ ID NO: 264 and 290; 204) SEQ ID NO: 266 and 115; 205) SEQ ID NO: 266 and 121; 206) SEQ ID NO: 266 and 157; 207) SEQ ID NO: 266 and 272; 208) SEQ ID NO: 269 and 272; 218) SEQ ID NO: 269 and 277; 219) SEQ ID NO: 269 and 279; 220) SEQ ID NO: 269 and 282; 221) SEQ ID NO: 269 and 286; 222) SEQ ID NO: 269 and 290; 223) SEQ ID NO: 269 and 115; 224) SEQ ID NO: 269 and 121; 225) SEQ ID NO: 269 and 157; 226) SEQ ID NO: 269 and 157; 227) SEQ ID NO: 269 and 272; 228) SEQ ID NO: 269 and 277; 229) SEQ ID NO: 269 and 279; 230) SEQ ID NO: 269 and 282; 231) SEQ ID NO: 269 and 286; or 232) SEQ ID NO: 269 and 286 NO: 269 and 290. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3A3, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3A3. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3A3 to confer similar specific binding, or a fragment thereof, and the VH and VL comprise or consist of the amino acid sequences of SEQ ID NOs: 23 and 27, respectively. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3A19, or the antibody or antigen-binding fragment comprises the CDRs and optionally VH and VL of S3A19. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3A19 to confer similar specific binding, or a fragment thereof, and the VH and VL comprise or consist of the following: such as SEQ ID NO: 31 and 37, respectively; 35 and 37, respectively; 36 and 37, respectively; and any one of 43 and 37, respectively. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3I2, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S3I2. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3I2 to confer similar specific binding, or a fragment thereof, and VH and VL comprise or consist of amino acid sequences such as SEQ ID NOs: 83 and 87, respectively. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3O13, or the antibody or antigen-binding fragment comprises CDRs and, optionally, VH and VL of S3O13. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3O13 to confer similar specific binding, or a fragment thereof, and the VH and VL comprise or consist of amino acid sequences such as SEQ ID NOs: 93 and 97, respectively. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S3L17, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S3L17. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S3L17 to confer similar specific binding, or a fragment thereof, and VH and VL comprise or consist of amino acid sequences such as SEQ ID NOs: 102 and 105, respectively. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S2V29a, or the antibody or antigen-binding fragment comprises the CDRs and, optionally, VH and VL of S2V29a. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S2V29a (to confer similar specific binding), or a fragment thereof, and VH and VL comprise or consist of amino acid sequences such as SEQ ID NOs: 111 and 115, respectively. In some embodiments, the antibody is (or the antigen-binding fragment is derived from) S2V29b, or the antibody or antigen-binding fragment comprises CDRs and, optionally, VH and VL of S2V29b. In some embodiments, the antibody comprises sufficient CDR, VH, and/or VL identity to S2V29b to confer similar specific binding, or a fragment thereof, and VH and VL comprise or consist of amino acid sequences such as SEQ ID NOs: 111 and 121, respectively. In certain embodiments, an antibody or antigen-binding fragment comprising a heavy chain variable domain (VH) is provided, wherein the heavy chain variable domain comprises or consists of: an amino acid sequence of any one of SEQ ID NO: 23, 31, 35, 36, 43, 83, 93, 102, 111, 125, 128, 131, 137, 141, 145, 149, 453, 179, 181, 183, 185, 188, 190, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, 222, 235, 238, 241, 243, 245, 247, 249, 251, 264, 266, or 269. In certain embodiments, an antibody or antigen-binding fragment comprising a light chain variable domain (VL) is provided, wherein the light chain variable domain comprises or consists of an amino acid sequence of any one of SEQ ID NOs: 27, 37, 87, 97, 105, 115, 121, 157, 193, 225, 228, 231, 254, 257, 260, 272, 277, 279, 282, 286, 290. As used herein, a "variant" of a CDR refers to a functional variant of a CDR sequence having up to 1 to 3 amino acid substitutions (e.g., conserved or non-conserved substitutions), deletions, or a combination thereof. CDRs and framework regions may be coded according to any known method or scheme, such as the Kabat, Chothia, EU, IMGT, Contact, North, Martin, AbM, and AHo numbering schemes (see, e.g., Kabat et al., "Sequences of Proteins of Immunological Interest, US Dept. Health and Human Services, Public Health Service National Institutes of Health, 1991, 5th ed.; Chothia and Lesk, J. Mol. Biol. 196:901-917 (1987)); Lefranc et al., Dev. Comp. Immunol. 27:55, 2003; Honegger and Plückthun, J. Mol. Bio. 309:657-670 (2001); North et al. J Mol Biol. (2011) 406:228-56; doi:10.1016/j.jmb.2010.10.030; Abhinandan and Martin, Mol Immunol.(2008)45:3832-9. 10.1016/j.molimm.2008.05. 022). The antibody and CDR numbering systems of these references are incorporated herein by reference. Equivalent residue positions can be identified using the Antigen receptor Numbering and Receptor Classification (ANARCI) software tool (2016, Bioinformatics 15:298-300) to annotate and compare different molecules. Therefore, identifying the CDRs of the exemplary variable region (VH or VL) sequences as provided herein according to one numbering scheme does not include antibodies comprising CDRs of the same variable region as determined using a different numbering scheme. In certain embodiments, antibodies or antigen-binding fragments are provided that comprise one or more CDRs of the following VH sequences: as shown in SEQ ID NO: any of 23, 31, 35, 36, 43, 83, 93, 102, 111, 125, 128, 131, 137, 141, 145, 149, 453, 179, 181, 183, 185, 188, 190, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, 222, 235, 238, 241, 243, 245, 247, 249, 251, 264, 266, or 269; and/or one or more CDRs in the following VL sequences: such as SEQ ID NO: 27, 37, 87, 97, 105, 115, 121, 157, 193, 225, 228, 231, 254, 257, 260, 272, 277, 279, 282, 286, 290, according to any known CDR numbering method, including Kabat, Chothia, North, EU, IMGT, Martin (enhanced Chothia), Contact, AbM, and AHo numbering methods, or according to a combination of two or more of these methods (e.g., including those residues that fall within a CDR as defined by any or all of the numbering methods). In certain embodiments, the CDR is according to the IMGT numbering method (optionally using a combined definition of the CDR3 amino acid sequence). In some embodiments, the CDRs are numbered according to the antibody numbering method developed by the Chemical Computing Group (CCG); for example, using the Molecular Operating Environment (MOE) software (chemcomp.com). In some embodiments, the CDRs are numbered according to the IMGT numbering method. S3A3 Antibodies, antigen-binding fragments, and variantsIn certain embodiments, an antibody or antigen-binding fragment is provided, comprising a VH sequence such as SEQ ID NO: 23 and a VL sequence such as SEQ ID NO: 27. In certain embodiments, the amino acid sequence changes relative to SEQ ID NO: 23 or SEQ ID NO: 27 are limited to changes in one or more framework regions (FRs) relative to SEQ ID NO: 23 or SEQ ID NO: 27, respectively. The framework regions can be identified according to a numbering scheme (e.g., IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo, or a combination of two or more thereof). CDRs can be identified within variable structural domains or within heavy or light chains based on a numbering scheme or combination of numbering schemes, and preferably, FRs can be identified using the same numbering scheme or combination of numbering schemes. In certain embodiments, the antibody or antigen-binding fragment comprises a VH comprising FR1, FR2, FR3, and/or FR4 of the VH amino acid sequence set forth in SEQ ID NO: 23 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions); and a VL comprising FR1, FR2, FR3, and/or FR4 of the VL amino acid sequence set forth in SEQ ID NO: 27 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions). In some embodiments, FR is defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering system, or according to any combination thereof. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising, consisting essentially of, or consisting of the amino acid sequence described in SEQ ID NO: 23; and (ii) a light chain variable domain (VL) comprising, consisting essentially of, or consisting of the amino acid sequence described in SEQ ID NO: 27. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising the amino acid sequence described in SEQ ID NO: 23; and (ii) a light chain variable domain (VL) comprising the amino acid sequence described in SEQ ID NO: 27. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting essentially of the amino acid sequence described in SEQ ID NO: 23; and (ii) a light chain variable domain (VL) consisting essentially of the amino acid sequence described in SEQ ID NO: 27. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting of the amino acid sequence described in SEQ ID NO: 23; and (ii) a light chain variable domain (VL) consisting of the amino acid sequence described in SEQ ID NO: 27. In certain embodiments, an antibody or antigen-binding fragment is provided, comprising CDRs identified in the VH sequence of SEQ ID NO: 23 and in the VL sequence of SEQ ID NO: 27, wherein the CDRs are defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering system, or according to any combination thereof. In certain embodiments, antibodies or antigen-binding fragments are provided, comprising a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (i) CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 24 or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: (iii) the CDRH3 comprises or consists of an amino acid sequence such as SEQ ID NO: 26, or a sequence variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence such as SEQ ID NO: 28, or a sequence variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence such as SEQ ID NO: 30, or a sequence variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; NO: 29, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of the following: such as SEQ ID NO: 30, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids, wherein the antibody or antigen-binding fragment is capable of binding to one or more or two or more surface glycoproteins of severe acute respiratory syndrome beta coronaviruses expressed on the cell surface of a host cell. In certain embodiments, the antibody or antigen-binding fragment comprises the amino acid sequences of CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 as shown in SEQ ID NOs: 24 to 26 and 28 to 30, respectively. S3A19 Antibodies, antigen-binding fragments, and variantsIn certain embodiments, antibodies or antigen-binding fragments are provided, comprising a VH sequence as any one of SEQ ID NOs: 31, 35, 36, and 43 and a VL sequence as SEQ ID NO: 37. In certain embodiments, the amino acid sequence variations relative to any one of SEQ ID NOs: 31, 35, 36, and 43 or SEQ ID NO: 37 are limited to variations in one or more framework regions (FRs) relative to any one of SEQ ID NOs: 31, 35, 36, and 43 or SEQ ID NO: 37, respectively. Framework regions can be identified according to a numbering scheme (e.g., IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo, or a combination of two or more thereof). CDRs can be identified within variable structural domains or within heavy or light chains based on a numbering scheme or combination of numbering schemes, and preferably, FRs can be identified using the same numbering scheme or combination of numbering schemes. In certain embodiments, the antibody or antigen-binding fragment comprises a VH comprising the following: FR1, FR2, FR3, and/or FR4 of the VH amino acid sequence described in any one of SEQ ID NOs: 31, 35, 36, and 43 (or variants of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions); and a VL comprising FR1, FR2, FR3, and/or FR4 of the VL amino acid sequence described in SEQ ID NO: 37 (or variants of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions). In some embodiments, FR is defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering system, or according to any combination thereof. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising, consisting essentially of, or consisting of the amino acid sequence described in any one of SEQ ID NOs: 31, 35, 36, and 43; and (ii) a light chain variable domain (VL) comprising, consisting essentially of, or consisting of the amino acid sequence described in SEQ ID NO: 37. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising the following: an amino acid sequence described in any one of SEQ ID NOs: 31, 35, 36, and 43; and (ii) a light chain variable domain (VL) comprising the amino acid sequence described in SEQ ID NO: 37. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting essentially of the following: an amino acid sequence described in any one of SEQ ID NOs: 31, 35, 36, and 43; and (ii) a light chain variable domain (VL) consisting essentially of the amino acid sequence described in SEQ ID NO: 37. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting of the amino acid sequence described in any one of SEQ ID NOs: 31, 35, 36, and 43; and (ii) a light chain variable domain (VL) consisting essentially of the amino acid sequence described in SEQ ID NO: 37. The S3A19 antibody may be as described in Table 3. In certain embodiments, antibodies or antigen-binding fragments are provided, comprising CDRs identified in: a VH sequence such as any one of SEQ ID NOs: 31, 35, 36, and 43 and a VL sequence such as SEQ ID NO: 37, wherein the CDRs are defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering systems, or according to any combination thereof. In certain embodiments, antibodies or antigen-binding fragments are provided, which comprise a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (i) CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 32 or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: (iii) the CDRH3 comprises or consists of an amino acid sequence such as SEQ ID NO: 34, or a sequence variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence such as SEQ ID NO: 38, or a sequence variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence such as SEQ ID NO: 39, or a sequence variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; NO: 39, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of the following: such as SEQ ID NO: 40, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids, wherein the antibody or antigen-binding fragment is capable of binding to one or more or two or more surface glycoproteins of severe acute respiratory syndrome beta coronaviruses expressed on the cell surface of a host cell. In any of the currently disclosed embodiments, the antibody or antigen-binding fragment comprises the amino acid sequences of CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 as shown in SEQ ID NOs: 32 to 34 and 38 to 40, respectively. S3I2 Antibodies, antigen-binding fragments, and variantsIn certain embodiments, antibodies or antigen-binding fragments are provided, comprising a VH sequence as in any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190 and a VL sequence as in any one of SEQ ID NOs: 87 or 193. In certain embodiments, the amino acid sequence changes relative to any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190 or any one of SEQ ID NOs: 87 or 193 are limited to changes in one or more framework regions (FRs) relative to any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190 or any one of SEQ ID NOs: 87 or 193, respectively. Framework regions may be identified according to a numbering scheme such as IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo, or a combination of two or more of these. CDRs may be identified within variable domains or within heavy or light chains according to a numbering scheme or combination of numbering schemes, and preferably, FRs may be identified using the same numbering scheme or combination of numbering schemes. In certain embodiments, the antibody or antigen-binding fragment comprises a VH comprising the following: FR1, FR2, FR3, and/or FR4 of the VH amino acid sequence described in any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions); and a VL comprising FR1, FR2, FR3, and/or FR4 of the VL amino acid sequence described in any one of SEQ ID NOs: 87 or 193 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions). In some embodiments, FR is defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering system, or according to any combination thereof. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190; and (ii) a light chain variable domain (VL) comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 87 or 193. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising the following: an amino acid sequence described in any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190; and (ii) a light chain variable domain (VL) comprising an amino acid sequence described in any one of SEQ ID NOs: 87 or 193. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting essentially of the amino acid sequence of any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190; and (ii) a light chain variable domain (VL) consisting essentially of the amino acid sequence of any one of SEQ ID NOs: 87 or 193. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting of an amino acid sequence described in any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, 190; and (ii) a light chain variable domain (VL) consisting of an amino acid sequence described in any one of SEQ ID NOs: 87 or 193. In certain embodiments, antibodies or antigen-binding fragments are provided, comprising CDRs identified in: a VH sequence such as any one of SEQ ID NOs: 83, 179, 181, 183, 185, 190 and a VL sequence such as any one of SEQ ID NOs: 87 or 193, wherein the CDRs are defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering systems, or according to any combination thereof. In certain embodiments, antibodies or antigen-binding fragments are provided, which comprise a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (i) CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 84 or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 85, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence as any one of SEQ ID NO: 86 or 186, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence as any one of SEQ ID NO: 88 or 194, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence such as SEQ ID NO: 89, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of an amino acid sequence such as SEQ ID NO: 90, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids, wherein the antibody or antigen-binding fragment is capable of binding to one or more or two or more surface glycoproteins of severe acute respiratory syndrome beta coronaviruses expressed on the cell surface of a host cell. In certain embodiments, the antibody or antigen-binding fragment comprises the CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences of SEQ ID NO: 84 to 86 or 84, 85 and 186 and 88 to 90 or 194, 89, and 90, respectively. S3O13 Antibodies, antigen-binding fragments, and variantsIn certain embodiments, an antibody or antigen-binding fragment is provided, comprising a VH sequence as set forth in any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and a VL sequence as set forth in any one of SEQ ID NOs: 97, 225, 228, or 231. In some embodiments, the amino acid sequence changes relative to any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 or any one of SEQ ID NOs: 97, 225, 228, or 231 are limited to changes in one or more framework regions (FRs) relative to any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 or any one of SEQ ID NOs: 97, 225, 228, or 231, respectively. Framework regions may be identified according to a numbering scheme such as IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo, or a combination of two or more of these. CDRs may be identified within variable domains or within heavy or light chains according to a numbering scheme or combination of numbering schemes, and preferably, FRs may be identified using the same numbering scheme or combination of numbering schemes. In certain embodiments, the antibody or antigen-binding fragment comprises a VH comprising the following: FR1, FR2, FR3, and/or FR4 of the VH amino acid sequence described in any one of SEQ ID NO: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions); and a VL comprising the following: SEQ ID NO: 97, 225, 228, or 231 of any of the VL amino acid sequences described in FR1, FR2, FR3, and/or FR4 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions). In some embodiments, FR is defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering system, or according to any combination thereof. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising, consisting essentially of, or consisting of an amino acid sequence as set forth in any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222; and (ii) a light chain variable domain (VL) comprising, consisting essentially of, or consisting of an amino acid sequence as set forth in any one of SEQ ID NOs: 97, 225, 228, or 231. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising the following: an amino acid sequence described in any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222; and (ii) a light chain variable domain (VL) comprising the following: an amino acid sequence described in any one of SEQ ID NOs: 97, 225, 228, or 231. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting essentially of the amino acid sequence of any one of SEQ ID NO: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222; and (ii) a light chain variable domain (VL) consisting essentially of the amino acid sequence of any one of SEQ ID NO: 97, 225, 228, or 231. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting of the amino acid sequence of any one of SEQ ID NO: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222; and (ii) a light chain variable domain (VL) consisting of the amino acid sequence of any one of SEQ ID NO: 97, 225, 228, or 231. In certain embodiments, antibodies or antigen-binding fragments are provided, comprising CDRs identified in: a VH sequence such as any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and a VL sequence such as any one of SEQ ID NOs: 97, 225, 228, or 231, wherein the CDRs are defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering systems, or according to any combination thereof. In certain embodiments, antibodies or antigen-binding fragments are provided, comprising a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (i) CDRH1 comprises or consists of the following: an amino acid sequence as set forth in any one of SEQ ID NOs: 94, 198, or 208, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence as set forth in SEQ ID NOs: 95, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 96, 199, 202, or 205, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 98, 226, 229, 232, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 39, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 99, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids, wherein the antibody or antigen-binding fragment is capable of binding to one or more or two or more surface glycoproteins of severe acute respiratory syndrome beta coronaviruses expressed on the cell surface of a host cell. In certain embodiments, the antibody or antigen-binding fragment comprises the following CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences, respectively: such as SEQ ID NO: 94 to 96; 198, 95 and 96; 208, 95 and 96; 94, 95, and 199; 198, 95 and 199; 208, 95, and 199; 94, 95, and 202; 198, 95, and 205; 208, 95, and 199; 205, 95, and 202; or 208, 95, and 205, and 98, 39, and 99; 226, 39, and 99; or 229, 39, and 232. S3L17 Antibodies, antigen-binding fragments, and variantsIn certain embodiments, an antibody or antigen-binding fragment is provided, which comprises a VH sequence as shown in any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence as shown in any one of SEQ ID NOs: 105, 254, 257, or 260. In some embodiments, amino acid sequence variations relative to any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 or any one of SEQ ID NOs: 105, 254, 257, or 260 are limited to variations in one or more framework regions (FRs) relative to any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 or any one of SEQ ID NOs: 105, 254, 257, or 260, respectively. Framework regions can be identified according to a numbering scheme (e.g., IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo, or a combination of two or more thereof). CDRs can be identified within variable structural domains or within heavy or light chains based on a numbering scheme or combination of numbering schemes, and preferably, FRs can be identified using the same numbering scheme or combination of numbering schemes. In certain embodiments, the antibody or antigen-binding fragment comprises a VH comprising FR1, FR2, FR3, and/or FR4 of the VH amino acid sequence described in any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions); and a VL comprising FR1, FR2, FR3, and/or FR4 of the VL amino acid sequence described in any one of SEQ ID NOs: 105, 254, 257, or 260 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions). In some embodiments, FR is defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering system, or according to any combination thereof. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251; and (ii) a light chain variable domain (VL) comprising, consisting essentially of, or consisting of the amino acid sequence of any one of SEQ ID NOs: 105, 254, 257, or 260. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising the following: an amino acid sequence described in any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251; and (ii) a light chain variable domain (VL) comprising the following: an amino acid sequence described in any one of SEQ ID NOs: 105, 254, 257, or 260. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting essentially of the amino acid sequence of any one of SEQ ID NO: 102, 235, 238, 241, 243, 245, 247, 249, or 251; and (ii) a light chain variable domain (VL) consisting essentially of the amino acid sequence of any one of SEQ ID NO: 105, 254, 257, or 260. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting of the amino acid sequence of any one of SEQ ID NO: 102, 235, 238, 241, 243, 245, 247, 249, or 251; and (ii) a light chain variable domain (VL) consisting of the amino acid sequence of any one of SEQ ID NO: 105, 254, 257, or 260. In certain embodiments, antibodies or antigen-binding fragments are provided, comprising CDRs identified in: a VH sequence such as any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence such as any one of SEQ ID NOs: 105, 254, 257, or 260, wherein the CDRs are defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering systems, or according to any combination thereof. In certain embodiments, antibodies or antigen-binding fragments are provided, which comprise a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (i) CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 103 or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 85, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of an amino acid sequence as in any one of SEQ ID NOs: 104, 236, or 239, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as in SEQ ID NOs: 106 or 255, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence such as SEQ ID NO: 107, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of an amino acid sequence such as SEQ ID NO: An amino acid sequence of any one of 108 or 258, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids, wherein the antibody or antigen-binding fragment is capable of binding to the surface glycoproteins of one or more or two or more severe acute respiratory syndrome beta coronaviruses expressed on the cell surface of a host cell. In certain embodiments, the antibody or antigen-binding fragment comprises the following CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences, respectively: such as SEQ ID NO: 103, 85, and 104; 103, 85, and 236; or 103, 85, and 239, and 106 to 108; 106, 107, and 258; 255, 107, and 108; or 255, 107, or 258. In some embodiments, the antibody or antigen-binding fragment comprises the CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences of S3A3, S3A19 VH.1, S3A19 VH.2, S3A19 VH.3, S3A19 VH.1-VH.3 consensus antibody, S3I2, S3O13, or S3L17 as described in Table 3. In certain embodiments, the antibody or antigen-binding fragment comprises a VH and VL amino acid sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the VH and VL amino acid sequence of (each) S3A3, S3A19 VH.1, S3A19 VH.2, S3A19 VH.3, o3A19 VH.1-VH.3 consensus antibody, S3I2, S3O13, or S3L17 as described in Table 3, or comprises S3A3, S3A19 VH.1, S3A19 VH.2, S3A19 VH.3, o3A19 VH.1-VH.3 consensus antibody, S3I2, S3O13, or S3L17 as described in Table 3. VH.1-VH.3 common antibody, S3I2, S3O13, or S3L17 (each) VH and VL amino acid sequence. In certain embodiments, the antibody or antigen-binding fragment comprises the VH and VL amino acid sequence of S3A3, S3A19 VH.1, S3A19 VH.2, S3A19 VH.3, S3A19 VH.1-VH.3 common antibody, S3I2, S3O13, or S3L17 (each) as described in Table 3. S2V29 Antibodies, antigen-binding fragments, and variants In certain embodiments, an antibody or antigen-binding fragment is provided, which comprises a VH sequence as any one of SEQ ID NO: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and a VL sequence as any one of SEQ ID NO: 115, 121, 157, 272, 277, 279, 282, 286, or 290. In some embodiments, amino acid sequence variations relative to any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 or any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290 are limited to variations in one or more framework regions (FRs) relative to any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 or any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290, respectively. Framework regions can be identified according to a numbering scheme, such as IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo, or a combination of two or more of these. CDRs can be identified within variable structural domains or within heavy or light chains according to a numbering scheme or combination of numbering schemes, and preferably, FRs can be identified using the same numbering scheme or combination of numbering schemes. In certain embodiments, the antibody or antigen-binding fragment comprises a VH comprising the following: FR1, FR2, FR3, and/or FR4 of the VH amino acid sequence described in any one of SEQ ID NO: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 (or a variant of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions); and a VL comprising the following: SEQ ID NO: 115, 121, 157, 272, 277, 279, 282, 286, or 290. FR1, FR2, FR3, and/or FR4 (or variants of FR1, FR2, FR3, and/or FR4 comprising one, two, three, four, or five amino acid substitutions, insertions, and/or deletions). In some embodiments, FR is defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering system, or according to any combination thereof. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising, consisting essentially of, or consisting of the amino acid sequence depicted in any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269; and (ii) a light chain variable domain (VL) comprising, consisting essentially of, or consisting of the amino acid sequence depicted in any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) comprising the amino acid sequence of any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269; and (ii) a light chain variable domain (VL) comprising the amino acid sequence of any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting essentially of the amino acid sequence of any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269; and (ii) a light chain variable domain (VL) consisting essentially of the amino acid sequence of any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290. In some embodiments, the antibody or antigen-binding fragment comprises: (i) a heavy chain variable domain (VH) consisting of the amino acid sequence of any one of SEQ ID NO: 1 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269; and (ii) a light chain variable domain (VL) consisting of the amino acid sequence of any one of SEQ ID NO: 115, 121, 157, 272, 277, 279, 282, 286, or 290. In certain embodiments, antibodies or antigen-binding fragments are provided that comprise CDRs identified in: a VH sequence of any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and a VL sequence of any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290, wherein the CDRs are defined according to the IMGT, Kabat, Chothia, North, EU, Martin (enhanced Chothia), Contact, AbM, CCG, or AHo numbering systems, or according to any combination thereof. In certain embodiments, antibodies or antigen-binding fragments are provided, which comprise a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (i) CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 112 or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 113, 126, 129, 132, 135, 138, 142, 146, 150, 154, 267, or 270, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 114, 139, 143, 147, 151, or 155, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 116, 273, or 283, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence as described in any of SEQ ID NOs: 117, 274, or 287, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of an amino acid sequence as described in SEQ ID NOs: 118, 122, 158, 275, 280, 284, 288, or 291, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids, wherein the antibody or antigen-binding fragment is capable of binding to one or more or two or more surface glycoproteins of severe acute respiratory syndrome beta coronaviruses expressed on the cell surface of a host cell. In certain embodiments, the antibody or antigen-binding fragment comprises the following CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences, respectively: such as SEQ ID NO: 112 to 114; 112, 126, and 114; 112, 129, and 114; 112, 132, and 114; 112, 135, and 114; 112, 138, and 114; 112, 142, and 114; 112, 146, and 114; 112, 150, and 114; 112, 154, and 114; 112, 267, and 114; 112, 270, and 114; 112, 113, and 139 ; 112, 126, and 139; 112, 129, and 139; 112, 132, and 139; 112, 135, and 139; 112, 138, and 139; 112, 142, and 139; 112, 146, and 139; 112, 150, and 139; 112, 154, and 139; 112, 267, and 139; 112, 270, and 139; 112, 113, and 143; 112, 12 6, and 143; 112, 129, and 143; 112, 132, and 143; 112, 135, and 143; 112, 138, and 143; 112, 142, and 143; 112, 146, and 143; 112, 150, and 143; 112, 154, and 143; 112, 267, and 143; 112, 270, and 143; 112, 113, and 147; 112, 126, and 147; 112, 129, and 147; 112, 132, and 147; 112, 135, and 147; 112, 138, and 147; 112, 142, and 147; 112, 146, and 147; 112, 150, and 147; 112, 154, and 147; 112, 267, and 147; 112, 270, and 147; 112, 113, and 151; 112, 126, and 151; 112, 129 and 151; 112, 132, and 151; 112, 135, and 151; 112, 138, and 151; 112, 142, and 151; 112, 146, and 151; 112, 150, and 151; 112, 154, and 151; 112, 267, and 151; 112, 270, and 151; 112, 113, and 155; 1 12, 126, and 155; 112, 129, and 155; 112, 132, and 155; 112, 135, and 155; 112, 138, and 155; 112, 142, and 155; 112, 146, and 1551; 112, 150, and 155; 112, 154, and 155; 112, 267, and 155; or 112, 270 , and 155; and 116 to 118; 116, 274, and 118; 116, 287, and 118; 116, 117, and 122; 116, 274, and 122; 116, 287, and 122; 116, 117, and 158; 116, 274, and 275; 116, 287, and 275; 116, 117, and 280; 116, 2 74, and 280; 116, 287, and 280; 116, 117, and 284; 116, 274, and 284; 116, 287, and 284; 116, 117, and 288; 116, 274, and 288; 116, 287, and 288; 116, 117, and 291; 116, 274, and 291; 116, 287, and 291 ; 273, 117, and 118; 273, 274, and 118; 273, 287, and 118; 273, 117, and 122; 273, 274, and 122; 273, 287, and 122; 273, 117, and 158; 273, 274, and 275; 273, 287, and 275; 273, 117, and 280; 273, 27 4, and 280; 1273, 287, and 280; 273, 117, and 284; 273, 274, and 284; 273, 287, and 284; 273, 117, and 288; 273, 274, and 288; 273, 287, and 288; 273, 117, and 291; 273, 274, and 291; 273, 287, and 291 ; 283, 117, 118; 283, 274, and 118; 283, 287, and 118; 283, 117, and 122; 283, 274, and 122; 283, 287, and 122; 283, 117, and 158; 283, 274, and 275; 283, 287, and 275; 283, 117, and 280; 283, 274 , and 280; 283, 287, and 280; 283, 117, and 284; 283, 274, and 284; 283, 287, and 284; 283, 117, and 288; 283, 274, and 288; 283, 287, and 288; 283, 117, and 291; 283, 274, and 291; or 283, 287, and 291. In certain embodiments, the antibody or antigen-binding fragment comprises the following CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences, respectively: as SEQ ID NO: 112 to 114 and 116 to 118, respectively (S2V29a); 112 to 114 and 116, 117, and 122, respectively (S2V29b). In certain embodiments, the antibody or antigen-binding fragment comprises a VH or VL comprising or consisting of SEQ ID NOs: 111 and 157, or having at least 85%, 90%, or 95% identity to these sequences, particularly with framework mutations as disclosed herein. In still further embodiments, the antibody or antigen-binding fragment comprises the CDRs described in the VH and VL of SEQ ID NOs: 111 and 157, according to any numbering scheme as described herein. In some embodiments, the antibody or antigen-binding fragment comprises the CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences of SEQ ID NOs: 112 to 114 and 116 to 117, and 158, respectively. Any of these antibodies may include an Fc modification as described herein, or may have an unmodified human IgG1 constant region. Specifically, the antibody may have a VH as in SEQ ID NO: 111, a CH as in SEQ ID NO: 44 to 80, a VL as in SEQ ID NO: 157, and a CL as in SEQ ID NO: 292. In certain embodiments, the heavy chain of the antibody or antigen-binding fragment comprises or consists of a sequence that is at least 85%, 90%, 95%, or 99% identical to SEQ ID NO: 293, and the light chain comprises or consists of a sequence that is at least 85%, 90%, 95%, or 99% identical to SEQ ID NO: 294. In some embodiments, the heavy chain of the antibody or antigen-binding fragment comprises or consists of the amino acid sequence of SEQ ID NO: 293 and the light chain comprises or consists of the amino acid sequence of SEQ ID NO: 294. In specific embodiments, the heavy chain of the antibody or antigen-binding fragment comprises or consists of a sequence that is at least 85%, 90%, 95%, or 99% identical to SEQ ID NO: 295, and the light chain comprises or consists of a sequence that is at least 85%, 90%, 95%, or 99% identical to SEQ ID NO: 296. In some embodiments, the heavy chain of the antibody or antigen-binding fragment comprises or consists of the amino acid sequence of SEQ ID NO: 295 and the light chain comprises or consists of the amino acid sequence of SEQ ID NO: 296. The term "CL" refers to "immunoglobulin light chain constant region" or "light chain constant region", i.e., the constant region from the antibody light chain. The term "CH" refers to "immunoglobulin heavy chain constant region" or "heavy chain constant region", which can be further divided into CH1, CH2, and CH3 (IgA, IgD, IgG); or CH1, CH2, CH3, and CH4 domains (IgE, IgM) according to the antibody isotype. The Fc region of the antibody heavy chain is further described herein. In any currently disclosed specific embodiment, the antibody or antigen-binding fragment of the present disclosure comprises any one or more of CL, CH1, CH2, and CH3. In any currently disclosed specific embodiment, the antibody or antigen-binding fragment of the present disclosure may comprise any one or more of CL, CH1, CH2, and CH3. In certain embodiments, CL comprises an amino acid sequence having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity with the amino acid sequence of SEQ ID NO: 292. In certain embodiments, CL comprises an amino acid sequence having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity with the human lambda light chain constant domain. The term "CH" refers to "immunoglobulin heavy chain constant region" or "heavy chain constant region", which can be further divided into CH1, CH2, and CH3 (IgA, IgD, IgG); or CH1, CH2, CH3, and CH4 domains (IgE, IgM) according to the antibody isotype. The Fc region of the antibody heavy chain is further described herein. In any of the currently disclosed embodiments, the antibody or antigen-binding fragment of the present disclosure comprises any one or more of CL, CH1, CH2, and CH3. In some embodiments, the antibody or antigen-binding fragment comprises (e.g., human) IgG (e.g., IgG1, IgG2, IgG3, or IgG4), IgA, IgD, IgE, or IgM isotype, or comprises an amino acid sequence from two or more of these isotypes. In some embodiments, the antibody or antigen-binding fragment comprises an IgG1 isotype; it is understood that such an antibody or antigen-binding fragment may comprise one or more amino acid substitutions in the heavy chain constant domain and still be considered an "IgG1" isotype. In some embodiments, IgG1 comprises or consists of an amino acid sequence having at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity to the amino acid sequence set forth in SEQ ID NOs: 44 to 80, or comprises or consists of the amino acids set forth in SEQ ID NOs: 44 to 80. It is understood that, for example, production in mammalian cell lines can remove one or more C-terminal lysines of the antibody heavy chain (see, e.g., Liu et al. mAbs 6(5):1145-1154 (2014)). Therefore, the antibodies or antigen-binding fragments disclosed herein may include heavy chains, CH1-CH3, CH3, or Fc polypeptides in which a C-terminal lysine residue or a C-terminal glycine-lysine residue is present or absent; in other words, embodiments in which the C-terminal residue of the heavy chain, CH1-CH3, or Fc polypeptide is not lysine, and embodiments in which lysine is the C-terminal residue are encompassed. In certain embodiments, the composition comprises a plurality of antibodies and/or antigen-binding fragments of the present disclosure, wherein one or more of the antibodies or antigen-binding fragments do not contain a lysine residue or a C-terminal glycine-lysine at the C-terminal end of the heavy chain, CH1-CH3, or Fc polypeptide, and wherein one or more of the antibodies or antigen-binding fragments contain a lysine residue at the C-terminal end of the heavy chain, CH1-CH3, or Fc polypeptide. "Fab" (fragment antigen binding) is the portion of an antibody that binds to an antigen and includes the variable region and CH1 of the heavy chain linked to the light chain via an interchain disulfide bond. Each Fab fragment is monovalent with respect to antigen binding, i.e., it has a single antigen binding site. Pepsin treatment of an antibody yields a single large F(ab')2 fragment, which roughly corresponds to two disulfide-linked Fab fragments, has divalent antigen-binding activity and is still capable of cross-linking antibodies. Both Fab and F(ab')2 are examples of "antigen-binding fragments". Fab' fragments differ from Fab fragments in having an additional small number of residues at the carboxyl terminus of the CH1 domain, which includes one or more cysteines from the antibody hinge region. Fab'-SH is the designation used herein for Fab' in which the cysteine residue(s) of the invariant domains bear a free thiol group. F(ab')2 antibody fragments were originally produced as pairs of Fab' fragments with tethered cysteines between them. Other chemical couplings of antibody fragments are also known. Fab fragments can be joined, for example, by a peptide linker to form a single chain Fab, also referred to herein as "scFab". In these embodiments, the interchain disulfide bonds present in native Fab may not be present, and the linker is used completely or partially to link or connect the Fab fragments in a single polypeptide chain. A heavy chain derived Fab fragment (e.g., comprising, consisting of, or consisting essentially of VH+CH1, or "Fd") and a light chain derived Fab fragment (e.g., comprising, consisting of, or consisting essentially of VL+CL) can be linked in any arrangement to form a scFab. For example, the scFab can be arranged in the N-terminal to C-terminal direction according to (heavy chain Fab fragment-linker-light chain Fab fragment) or (light chain Fab fragment-linker-heavy chain Fab fragment). Peptide linkers and exemplary linker sequences for scFab are discussed in further detail herein. "Fv" is a small antibody fragment containing complete antigen recognition and antigen binding sites. This fragment is typically composed of a dimer of one heavy chain variable region and one light chain variable region in tight, non-covalent association. However, even a single variable domain (or half of an Fv comprising only three CDRs specific for an antigen) has the ability to recognize and bind antigen, although generally with a lower affinity than the entire binding site. "Single-chain Fv" is also abbreviated as "sFv" or "scFv" and is comprised of V and V domains linked into a single polypeptide chain._Hand V _LAntibody fragment of antibody domain. In some specific embodiments, the scFv polypeptide comprises a V _HWith V_L A polypeptide linker between and connecting the domains enables the scFv to retain or form the desired structure for antigen binding. Such a peptide linker can be incorporated into the fusion polypeptide using standard methods well known in the art. For a general description of scFv, see Pluckthun in The Pharmacology of Monoclonal Antibodies, vol. 113, Rosenburg and Moore eds., Springer-Verlag, New York, pp. 269-315 (1994); Borrebaeck 1995, see below. In certain embodiments, the antibody or antigen-binding fragment comprises an scFv comprising a VH domain, a VL domain, and a peptide linker connecting the VH domain to the VL domain. In certain embodiments, the scFv comprises a VH domain connected to a VL domain via a peptide linker, which scFv may be in a VH-linker-VL orientation or in a VL-linker-VH orientation. Any scFv disclosed herein may be engineered such that the C-terminal end of the VL domain is connected to the N-terminal end of the VH domain via a short peptide sequence, or vice versa (i.e., (N)VL(C)-linker-(N)VH(C) or (N)VH(C)-linker-(N)VL(C)). Alternatively, in some embodiments, the linker may be connected to the N-terminal portion or end of the VH domain, the VL domain, or both. The peptide linker sequence can be selected, for example, based on: (1) its ability to present a flexible extended conformation; (2) its inability or lack of ability to present a secondary structure that can interact with a functional epitope on the first and second polypeptides and/or on the target molecule; and/or (3) the lack or relative lack of hydrophobic or charged residues that may react with the polypeptides and/or the target molecule. Other considerations for linker design (e.g., length) may include the conformation or range of conformations in which VH and VL may form a functional antigen binding site. In certain embodiments, the peptide linker sequence contains, for example, Gly, Asn, and Ser residues. Other nearly neutral amino acids (such as Thr and Ala) may also be included in the linker sequence. Other amino acid sequences that may be advantageously used as linkers include those disclosed in Maratea et al., Gene 40:39 46 (1985); Murphy et al., Proc. Natl. Acad. Sci. USA 83:8258 8262 (1986); U.S. Patent No. 4,935,233; and U.S. Patent No. 4,751,180. Other illustrative and non-limiting examples of linkers can include, for example, Glu-Gly-Lys-Ser-Ser-Gly-Ser-Gly-Ser-Glu-Ser-Lys-Val-Asp (SEQ ID NO: 19) (Chaudhary et al., Proc. Natl. Acad. Sci. USA 87: 1066-1070 (1990)) and Lys-Glu-Ser-Gly-Ser-Val-Ser-Ser-Glu-Gln-Leu-Ala-Gln-Phe-Arg-Ser-Leu-Asp (SEQ ID NO: 20) (Bird et al., Science 242: 423-426 (1988)) and the pentamer Gly-Gly-Gly-Gly-Ser (SEQ ID NO: 21), when present in a single iteration or in repeats of 1 to 5 or more times, or more. Any suitable linker can be used, and will generally be about 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, 40, 50, 60, 70, 80, 90, 100 amino acids in length, or less than about 200 amino acids in length, and will preferably comprise a flexible structure (to provide flexibility and space for conformational movement between the two regions, domains, motifs, fragments, or modules connected by the linker), and will preferably be biologically inert and/or have a low risk of human immunogenicity. Exemplary linkers include or consist of the amino acid sequences described in any one or more of SEQ ID NOs: 4 to 13 and linkers SEQ A and B. In certain embodiments, the linker comprises or consists of an amino acid sequence that is at least 75% (i.e., at least about 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more) identical to the amino acid sequence described in any one of SEQ ID NOs: 4 to 13 and linkers SEQ A and B. scFvs can be constructed using any combination of VH and VL sequences disclosed herein or any combination of CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 sequences. In some embodiments, a linker sequence is not required; for example, when the first and second polypeptides have non-essential N-terminal (or C-terminal) amino acid regions that can be used to separate the functional domains and prevent stereointerference. During antibody development, DNA in the germline variable (V), joining (J), and diversity (D) gene loci may rearrange, and insertions and/or deletions of nucleotides may occur in the coding sequence. Somatic mutations may be encoded by the resulting sequence and may be identified by reference to corresponding known germline sequences. In some cases, a somatic mutation that is not essential for a desired property of the antibody (e.g., binding to a SARS-CoV-2 antigen), or that imparts an undesirable property to the antibody (e.g., increases the risk of immunogenicity in an individual to whom the antibody is administered), or both, can be replaced by a corresponding germline-encoded amino acid, or by a different amino acid, such that the desired property of the antibody is improved or maintained and the undesirable property of the antibody is reduced or eliminated. Thus, in some embodiments, the antibodies or antigen-binding fragments of the present disclosure comprise at least one additional germline-encoded amino acid in the variable region as compared to the parent antibody or antigen-binding fragment, provided that the parent antibody or antigen-binding fragment comprises one or more somatic mutations. The variable region and CDR amino acid sequences of the exemplary anti-severe acute respiratory syndrome beta coronavirus antibodies disclosed herein are provided in Table 1 and Table 3 herein. In certain embodiments, the antibody or antigen-binding fragment comprises amino acid modifications (e.g., substitution mutations) to remove the risk of undesired oxidation, deamination, and/or isomerization. Variants comprising one or more amino acid changes in a variable region (e.g., VH, VL, framework, or CDR) are provided herein, which are compared to the currently disclosed S3A3, S3A19, S3I2, S3O13, S3L17, or S2V29 ("parent") antibodies, wherein the variant antibody is capable of binding to a SARS-CoV-2 antigen. In certain embodiments, VH comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to the amino acid sequence of SEQ ID NO: 23, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline-encoded amino acids; and/or (ii) VL comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to the amino acid sequence of SEQ ID NO: An amino acid sequence having at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identity to an amino acid sequence of 27, wherein the variations are optionally limited to one or more framework regions and/or the variations comprise one or more substitutions to germline encoded amino acids. In certain embodiments, VH comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as one or more of SEQ ID NOs: 31, 35, 36, and 43, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline-encoded amino acids; and/or (ii) VL comprises or consists of an amino acid sequence as one or more of SEQ ID NOs: An amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence of SEQ ID NO: 37, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline encoded amino acids. In certain embodiments, VH comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as set forth in one or more of SEQ ID NOs: 83, 179, 181, 183, 185, 188, and 190, wherein the alterations are optionally confined to one or more framework regions and/or the alterations comprise one or more substitutions of germline-encoded amino acids; and/or (ii) VL comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as set forth in SEQ ID NOs: An amino acid sequence having at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identity to one or more of 87 and 193, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline encoded amino acids. In certain embodiments, VH comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as one or more of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, and 222, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline encoded amino acids; and/or (ii) VL comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as SEQ ID NOs: An amino acid sequence having at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identity to one or more of 97, 225, 228, and 231, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline encoded amino acids. In certain embodiments, VH comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as one or more of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, and 251, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline encoded amino acids; and/or (ii) VL comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as SEQ ID NOs: An amino acid sequence having at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identity to one or more of 105, 254, 257, and 260, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline encoded amino acids. In certain embodiments, VH comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as one or more of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, and 269, wherein the changes are optionally limited to one or more framework regions and/or the changes comprise one or more substitutions of germline encoded amino acids; and/or (ii) VL comprises or consists of an amino acid sequence that is at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical to an amino acid sequence as SEQ ID NOs: In some embodiments, the antibody or antigen-binding fragment is an IgG (e.g., IgG1, IgG2, IgG3, or IgG4), IgA, IgM, IgE, or IgD isotype, or comprises an amino acid sequence from two or more of these. In some embodiments, the antibody or antigen-binding fragment thereof is human, humanized, or chimeric. The antibody or antigen-binding fragment may be any allotype or combination of allotypes. "Isotype" refers to the allelic variation found within the IgG subclass. For example, an allotype may include G1m1 (or G1m(a)), G1m2 (or G1m(x)), G1m3 (or G1m(f)), G1m17 (or Gm(z))m), G1m27, and/or G1m28 (G1m27 and G1m28 have been described as "alloallotypes"). The G1m3 and G1m17 allotypes are located at the same position in the CH1 domain (position 214 according to EU numbering). G1m3 includes R214 (EU), and G1m17 includes K214 (EU). The G1m1 isoform is located in the CH3 domain (at positions 356 and 358 (EU)) and refers to the substitutions of E356D and M358L. The G1m2 isoform refers to the substitution of alanine for glycine at position 431 (EU). G1m allotypes, isomeric isoforms, and their properties are known in the art and described, for example, in www.imgt.org/IMGTrepertoire/Proteins/allotypes/human/IGH/IGHC/G1m_allotypes.html and Lefranc, M.-P. and Lefranc, G.Human Gm, Km and Am allotypes and their molecular characterization: a remarkable demonstration of polymorphism In: B.Tait, F.Christiansen (Eds.), Immunogenetics, chap.34, Humana Press, Springer, New York, USA.Methods Mol.Biol.2012; 882, 635-680.PMID: 22665258, LIGM: 406, the contents of which and information on isotypes and isoforms are incorporated herein by reference. The G1m1 allotype can be combined, for example, with G1m3, G1m17, G1m27, G1m2, and/or G1m28 allotypes. In some embodiments, the allotype is G1m3, and there is no G1m1 (G1m3,-1). In some embodiments, the allotype is the G1m17,1 allotype. In some embodiments, the allotype is G1m3,1. In some embodiments, the allotype is G1m17, and there is no G1m1 (G1m17,-1). Optionally, these allotypes can be combined (or not combined) with G1m2, G1m27, or G1m28 allotypes. For example, the allotype can be G1m17,1,2. In some embodiments, the antibodies or antigen-binding fragments disclosed herein comprise a G1m3 allotype or a G1m3,1 allotype. In some embodiments, the antibodies or antigen-binding fragments disclosed herein comprise a G1m3 allotype and comprise M428L and N434S or M428L and N434A mutations or any other one or more mutations that enhance binding to human FcRn, as described herein. In some embodiments, the antibodies or antigen-binding fragments disclosed herein comprise a G1m3,1 allotype and comprise M428L and N434S or M428L and N434A mutations or any other one or more mutations that enhance binding to human FcRn, as described herein. In some embodiments, the antibodies or antigen-binding fragments disclosed herein comprise the G1m17,1 allotype. In some embodiments, the antibodies or antigen-binding fragments disclosed herein comprise the G1m17,1 allotype and comprise the M428L and N434S or M428L and N434A mutations or any other one or more mutations that enhance binding to human FcRn, as further described herein. In some embodiments, the antibodies or antigen-binding fragments disclosed herein comprise human antibodies, monoclonal antibodies, purified antibodies, single-chain antibodies, Fab, Fab', F(ab')2, Fv, scFv, or scFab. In certain embodiments, the antibodies or antigen-binding fragments disclosed herein are monospecific (e.g., bind to a single epitope) or multispecific (e.g., bind to multiple epitopes and/or target molecules). Antibodies and antigen-binding fragments can be constructed in a variety of formats. Exemplary antibody formats are disclosed in Spiess et al., Mol. Immunol. 67(2):95 (2015), and in Brinkmann and Kontermann, mAbs 9(2):182-212 (2017), which formats and methods of making the same are incorporated herein by reference, and include, for example, bispecific T cell engagers (BiTEs), DARTs, knobs-into-holes (KIH) assemblies, scFv-CH3-KIH assemblies, KIH common light chain antibodies, TandAbs, triplet, TriBi minibody, Fab-scFv, scFv-CH-CL-scFv, F(ab')2-scFv2, tetravalent HCab, endobody, CrossMab, dual action Fab, DAF) (two-in-one or four-in-one), DutaMab, DT-IgG, charge pairing, Fab-arm exchange, strand exchange engineered body (SEEDbody), trifunctional antibody (Triomab), LUZ-Y assembly, Fcab, κλ body, orthogonal Fab, DVD-Igs (e.g., U.S. Patent No. 8,258,268, the entire text of which is incorporated herein by reference), IgG(H)-scFv, scFv-(H)IgG, IgG(L)-scFv, scFv-(L)IgG, IgG(L,H)-Fv, IgG(H)-V, V(H)-IgG, IgG(L)-V, V(L)-IgG, KIH IgG-scFab, 2scFv-IgG, IgG-2scFv, scFv4-Ig, Zybody, and DVI-IgG (four-in-one), and so-called FIT-Ig (e.g., PCT Publication No. WO 2015/103072, the form of which is incorporated herein by reference in its entirety), the so-called WuxiBody form (e.g., PCT Publication No. WO 2019/057122, the form of which is incorporated herein by reference in its entirety), and the so-called In-Elbow-Insert Ig form (IEI-Ig; e.g., PCT Publication Nos. WO 2019/024979 and WO 2019/025391, the form of which is incorporated herein by reference in its entirety). In certain embodiments, the antibody or antigen-binding fragment comprises two or more VH domains, two or more VL domains, or both (i.e., two or more VH domains and two or more VL domains). In certain embodiments, the antigen-binding fragment comprises the format (N-terminal to C-terminal direction) VH-linker-VL-linker-VH-linker-VL, wherein the two VH sequences may be the same or different and the two VL sequences may be the same or different. Such linked scFvs may include any combination of VH and VL domains arranged to bind to a given target, and in a format comprising two or more VH and/or two or more VL, may bind to one, two, or more different epitopes or antigens. It should be understood that formats incorporating multiple antigen-binding domains may include VH and/or VL sequences in any combination or orientation. For example, the antigen-binding fragment may comprise the form VL-linker-VH-linker-VL-linker-VH, VH-linker-VL-linker-VL-linker-VH, or VL-linker-VH-linker-VH-linker-VL. The monospecific or multispecific antibodies or antigen-binding fragments of the present disclosure constructed comprise any combination of VH and VL sequences disclosed herein and/or any combination of CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 sequences. In some embodiments, the bispecific or multispecific antibodies or antigen-binding fragments may comprise one, two, or more antigen-binding domains (e.g., VH and VL) of the present disclosure. There may be two or more binding domains that bind to the same or different SARS-CoV-2 epitopes, and in some embodiments, a bispecific or multispecific antibody or antigen-binding fragment as provided herein may comprise additional SARS-CoV-2 binding domains, and/or may comprise binding domains that bind to different antigens or pathogens. In any of the presently disclosed embodiments, the antibody or antigen-binding fragment may be multispecific; e.g., bispecific, trispecific, etc. In certain embodiments, the antibody or antigen-binding fragment comprises: (i) a first VH and a first VL; and (ii) a second VH and a second VL, wherein the first VH and the second VH are different. In some embodiments, the first VH and VL comprise i) an amino acid sequence that is at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identical to the amino acid sequence depicted in SEQ ID NOs: 23 and 27, respectively; ii) an amino acid sequence that is at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identical to the amino acid sequence depicted in SEQ ID NOs: The amino acid sequence of NO. has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 31, 35, 36, or 43 and 37, respectively; 14 and 15, respectively; 16 and 17, respectively; 18 and 19, respectively; 20 and 21, respectively; 20 and 22, respectively; iii) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 83, 179, 181, 183, 185, 188, or 190 and any one of 87 or 193; iv) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and any one of 97, 225, 228, or 231; v) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 102, 235, 238, 241, 243, 245, 247, 249, or 251 and any one of 105, 254, 257, or 260; or vi) with the following SEQ ID NO. The amino acid sequence described has at least 85% (i.e. 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with an amino acid sequence: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of 115, 121, 157, 272, 277, 279, 282, 286, or 290; and wherein the second VH and VL comprise i) respectively with SEQ ID NO: 23 and 27 have at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs.; ii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs.: 31, 35, 36, or 43, respectively, and 37; 14 and 15, respectively; 16 and 17, respectively; 18 and 19, respectively; 20 and 21, respectively; 20 and 22, respectively; iii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs. NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 83, 179, 181, 183, 185, 188, or 190 and any one of 87 or 193; iv) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and any one of 97, 225, 228, or 231; v) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 102, 235, 238, 241, 243, 245, 247, 249, or 251 and any one of 105, 254, 257, or 260; or vi) with the following SEQ ID NO. has an amino acid sequence with at least 85% (i.e. 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity: any one of 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of 115, 121, 157, 272, 277, 279, 282, 286, or 290, respectively; wherein the first VH and the second VL are different from the second VH and VL, and wherein the first VH and the first VL together form a first antigen-binding site, and wherein the second VH and the second VL together form a second antigen-binding site. In some embodiments, the antibody or antigen-binding fragment may further comprise an Fc polypeptide or fragment thereof, comprising or consisting of an amino acid sequence having at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity to the amino acid sequence set forth in SEQ ID NOs: 44 to 80, or comprising or consisting of the amino acids set forth in SEQ ID NOs: 44 to 80. In certain embodiments, the antibody or antigen-binding fragment comprises an Fc polypeptide, or fragment thereof. An "Fc" fragment or Fc polypeptide comprises the carboxyl terminal portion of two antibody H chains (i.e., the CH2 and CH3 domains of IgG) held together by disulfide bonds. Fc may comprise a dimer composed of two Fc polypeptides (i.e., two CH2-CH3 polypeptides). Antibody "effector functions" refer to those biological activities attributable to the Fc region (a native sequence Fc region or an amino acid sequence variant Fc region) of an antibody, and vary with the antibody isotype. Examples of antibody effector functions include: C1q binding and complement-dependent cytotoxicity; Fc receptor binding; antibody-dependent cell-mediated cytotoxicity (ADCC); phagocytosis; downregulation of cell surface receptors (e.g., B cell receptors); and B cell activation. As discussed herein, the Fc domain may be modified (e.g., amino acid substitutions) to modify (e.g., improve, reduce, or ablate) one or more functionalities of an Fc-containing polypeptide (e.g., an antibody of the present disclosure). Such functions include, for example, Fc receptor (FcR) binding, antibody half-life modulation (e.g., by binding to FcRn), ADCC function, protein A binding, protein G binding, and complement binding. Amino acid modifications that modify (e.g., improve, reduce, or ablate) Fc functionality include, for example, T250Q/M428L, M252Y/S254T/T256E, H433K/N434F, M428L/N434S, M428L/N434A, E233P/L234V/L235A/ G236+A327G/A330S/P331S, E333A, S239D/A330L/I332E, P257I/Q311, K326W/E333S, S239D/I332E/G236A, N297Q, K322A, S228P, L235E+E318A/K320A/K322A, L234A/L235A (also referred to herein as "LALA"), and L234A/L235A/P329G mutations, which are summarized and annotated in "Engineered Fc Regions" and is available online at: invivogen.com/PDF/review/review-Engineered-Fc-Regions-invivogen.pdf?utm_source=review&utm_medium=pdf&utm_campaign=review&utm_content=Engineered-Fc-Regions, and is incorporated herein by reference. For example, to activate the complement cascade, when one or more immunoglobulin molecules are attached to the antigen target, the C1q protein complex can bind to at least two IgG1 molecules or one IgM molecule (Ward, E. S., and Ghetie, V., Ther. Immunol. 2 (1995) 77-94). Burton, D. R. described (Mol. Immunol. 22 (1985) 161-206) that a heavy chain region containing amino acid residues 318 to 337 is involved in complement fixation. Duncan, A. R. and Winter, G. (Nature 332 (1988) 738-740) used site-directed mutagenesis to report that Glu318, Lys320, and Lys322 form a binding site for C1q. The role of the Glu318, Lys320, and Lys322 residues in the binding of C1q was confirmed by the ability of short synthetic peptides containing these residues to inhibit complement-mediated cleavage. For example, FcR binding can be mediated by the interaction of the Fc portion (of an antibody) with an Fc receptor (FcR), which is a specialized cell surface receptor on cells including hematopoietic cells. Fc receptors belong to the immunoglobulin superfamily and have been shown to mediate the removal of antibody-coated pathogens by phagocytosis of immune complexes and the lysis of erythrocytes and various other cellular targets (e.g., tumor cells) coated with the corresponding antibody by antibody-dependent cell-mediated cytotoxicity (ADCC; Van de Winkel, J. G., and Anderson, C. L., J. Leukoc. Biol. 49 (1991) 511-524). FcRs are defined by their specificity for immunoglobulin classes; the Fc receptor for IgG antibodies is called FcγR, the Fc receptor for IgE is called FcεR, the Fc receptor for IgA is called FcαR, and so on, and the neonatal Fc receptor is called FcRn. Fc receptor binding is described, for example, in Ravetch, J. V., and Kinet, J. P., Annu. Rev. Immunol. 9 (1991) 457-492; Capel, P. J., et al., Immunomethods 4 (1994) 25-34; de Haas, M., et al., J Lab. Clin. Med. 126 (1995) 330-341; and Gessner, J. E., et al., Ann. Hematol. 76 (1998) 231-248. Crosslinking of receptors by the Fc domain of native IgG antibodies (FcγRs) triggers various effector functions, including phagocytosis, antibody-dependent cellular cytotoxicity, and release of inflammatory mediators, as well as regulation of immune complex clearance and antibody production. It is contemplated herein to provide a crosslinked Fc portion of a receptor (e.g., FcγR). In humans, three types of FcγRs have been characterized so far, which are: (i) FcγRI (CD64), which binds monomeric IgG with high affinity and is expressed on macrophages, monocytes, neutrophils, and eosinophils; (ii) FcγRII (CD32), which binds complexed IgG with moderate to low affinity, is widely expressed, especially on leukocytes, is believed to be a central player in antibody-mediated immunity, and can be divided into FcγRIIA, FcγRIIB, and FcγRIIC, which play different functions in the immune system but bind to IgG-Fc with similar low affinity, and the extracellular domains of these receptors are highly homologous; and (iii) FcγRIII (CD16), which binds IgG with medium to low affinity and has been found in two forms: FcγRIIIA, which has been found on NK cells, macrophages, eosinophils, and some monocytes and T cells, and is believed to mediate ADCC; and FcγRIIIB, which is highly expressed on neutrophils. FcγRIIA is found on many cells involved in killing (e.g., macrophages, monocytes, neutrophils) and appears to be able to activate the killing process. FcγRIIB appears to play a role in the inhibitory process and is found on B cells, macrophages, and on mast cells and eosinophils. Importantly, 75% of all FcγRIIB has been shown to be found in the liver (Ganesan, L. P. et al., 2012: "FcγRIIb on liver sinusoidal endothelium clears small immune complexes," Journal of Immunology 189: 4981-4988). FcγRIIB is abundantly expressed on liver sinusoidal endothelial cells called LSECs and in Kupffer cells in the liver, and LSECs are the major site of clearance of small immune complexes (Ganesan, L. P. et al., 2012: FcγRIIb on liver sinusoidal endothelium clears small immune complexes. Journal of Immunology 189: 4981-4988). In some embodiments, the antibodies and antigen-binding fragments thereof disclosed herein comprise an Fc polypeptide or fragment thereof that binds to FcγRIIb, in particular the Fc region, such as, for example, an IgG-type antibody. Furthermore, the Fc portion can be engineered by introducing mutations S267E and L328F to enhance FcγRIIB binding, as described by Chu, S. Y. et al., 2008: Inhibition of B cell receptor-mediated activation of primary human B cells by coengagement of CD19 and FcgammaRIIb with Fc-engineered antibodies. Molecular Immunology 45, 3926-3933. Thereby, the clearance of immune complexes can be enhanced (Chu, S., et al., 2014: Accelerated Clearance of IgE In Chimpanzees Is Mediated By Xmab7195, An Fc-Engineered Antibody With Enhanced Affinity For Inhibitory Receptor FcγRIIb. Am J Respir Crit, American Thoracic Society International Conference Abstracts). In some specific embodiments, the antibody or antigen-binding fragment thereof disclosed herein comprises an engineered Fc portion having mutations S267E and L328F, in particular as described by Chu, S. Y. et al., 2008: Inhibition of B cell receptor-mediated activation of primary human B cells by coengagement of CD19 and FcgammaRIIb with Fc-engineered antibodies. Molecular Immunology 45, 3926-3933. On B cells, FcγRIIB may act to suppress further immunoglobulin production and switch isotypes to, for example, the IgE class. On macrophages, FcγRIIB is thought to inhibit phagocytosis mediated by FcγRIIA. On eosinophils and mast cells, the B form may help suppress activation of these cells by binding of IgE to its independent receptors. With respect to FcγRI binding, modifications in native IgG of at least one of E233 to G236, P238, D265, N297, A327, and P329 reduce binding to FcγRI. Substitution of IgG2 residues at positions 233 to 236 into the corresponding positions in IgG1 and IgG4 reduced the binding of IgG1 and IgG4 to FcγRI by 103-fold and abolished the response of human monocytes to antibody-sensitized erythrocytes (Armour, K. L., et al. Eur. J. Immunol. 29 (1999) 2613-2624). With regard to FcγRII binding, IgG mutations such as E233 to G236, P238, D265, N297, A327, P329, D270, Q295, A327, R292, and K414 were found to reduce binding to FcγRIIA. The two allelic forms of human FcγRIIA are the "H131" variant, which binds to IgG1 Fc with higher affinity, and the "R131" variant, which binds to IgG1 Fc with lower affinity. See, e.g., Bruhns et al., Blood 113:3716-3725 (2009). With respect to FcγRIII binding, mutations in, e.g., at least one of E233 to G236, P238, D265, N297, A327, P329, D270, Q295, A327, S239, E269, E293, Y296, V303, A327, K338, and D376 were found to reduce binding to FcγRIIIA. The location of binding sites for Fc receptors on human IgG1, the mutation sites mentioned above, and methods for measuring binding to FcγRI and FcγRIIA are described in Shields, R. L., et al., J. Biol. Chem. 276 (2001) 6591-6604. The two allelic forms of human FcγRIIA are the "F158" variant, which binds to IgG1 Fc with lower affinity and the "V158" variant, which binds to IgG1 Fc with higher affinity. See, e.g., Bruhns et al., Blood 113: 3716-3725 (2009). With regard to binding to FcγRII, two regions of native IgG Fc appear to be involved in the interaction between FcγRII and IgG, namely (i) the lower hinge site of IgG Fc, particularly amino acid residues L, L, G, G (234 to 237, EU numbering), and (ii) adjacent regions of the CH2 domain of IgG Fc, particularly the upper CH2 domain adjacent to the lower hinge region, such as the loop and strand in the region of P331 (Wines, B.D., et al., J. Immunol. 2000; 164: 5313 - 5318). Furthermore, FcγRI appears to bind to the same site on IgG Fc, while FcRn and protein A bind to different sites on IgG Fc, which appear to be located at the CH2 to CH3 interface (Wines, B.D., et al., J. Immunol. 2000; 164: 5313-5318). Mutations that increase the binding affinity of the Fc polypeptides or fragments thereof disclosed herein to (i.e., one or more) Fcγ receptors are also contemplated (e.g., as compared to a reference Fc polypeptide or fragment thereof or containing a reference Fc polypeptide or fragment thereof that does not contain one or more mutations). See, e.g., Delillo and Ravetch, Cell 161(5):1035-1045(2015) and Ahmed et al., J. Struc. Biol. 194(1):78(2016), Fc mutations and techniques thereof are incorporated herein by reference. In any of the embodiments disclosed herein, the antibody or antigen-binding fragment may comprise an Fc polypeptide or fragment thereof comprising a mutation selected from the group consisting of G236A; S239D; A330L; and I332E; or a combination of any two or more of these mutations; for example, S239D/I332E; S239D/A330L/I332E; G236A/S239D/I332E; G236A/A330L/I332E (also referred to herein as "GAALIE"); or G236A/S239D/A330L/I332E. In some embodiments, the Fc polypeptide or fragment thereof does not comprise S239D. In some embodiments, the Fc polypeptide or fragment thereof comprises S at position 239 (EU numbering). In some embodiments, the Fc polypeptide or fragment thereof comprises an amino acid sequence set forth in SEQ ID NOs: 52 to 58. In certain embodiments, the Fc polypeptide or fragment thereof may comprise or consist of at least a portion of an Fc polypeptide or fragment thereof that participates in FcRn binding. In certain embodiments, the Fc polypeptide or fragment thereof comprises one or more amino acid modifications that improve (e.g., enhance binding to) FcRn (e.g., at a pH of about 6.0) and, in some embodiments, thereby extend the in vivo half-life of a molecule comprising the Fc polypeptide or fragment thereof (e.g., compared to an otherwise identical reference Fc polypeptide or fragment thereof or antibody that does not comprise the modification(s)). In certain embodiments, the Fc polypeptide or fragment thereof comprises or is derived from IgG Fc and the half-life-extending mutation comprises any one or more of the following: M428L; N434S; N434H; N434A; N434S; M252Y; S254T; T256E; T250Q; P257I; Q311I; D376V; T307A; E380A (EU numbering). In certain embodiments, the half-life-extending mutation comprises M428L/N434S (also referred to herein as "MLNS", "LS", "-LS", and "-LS"). In certain embodiments, the half-life-extending mutation is in an Fc polypeptide or fragment thereof comprising or consisting of the amino acid sequence set forth in SEQ ID NOs: 59 to 64. In some embodiments, the half-life-extending mutations comprise M252Y/S254T/T256E. In some embodiments, the half-life-extending mutations comprise T250Q/M428L. In some embodiments, the mutation that extends the half-life comprises P257I/Q311I. In some embodiments, the mutation that extends the half-life comprises P257I/N434H. In some embodiments, the mutation that extends the half-life comprises D376V/N434H. In some embodiments, the mutation that extends the half-life comprises T307A/E380A/N434A. In some embodiments, the mutation that extends the half-life comprises M428L/N434A (also referred to herein as "MLNA", "LA", "-LA", and "-LA"). In some embodiments, the mutation that extends the half-life is in an Fc polypeptide or a fragment thereof comprising the amino acid sequence described in SEQ ID NO: 65 to 70 or consisting of the amino acid sequence described in SEQ ID NO: 65 to 70. In some embodiments, the antibody or antigen-binding fragment comprises an Fc portion comprising the substitution mutations M428L/N434S or M428L/N434A. In some embodiments, the antibody or antigen-binding fragment comprises an Fc polypeptide or fragment thereof comprising the substitution mutations G236A/A330L/I332E. In certain embodiments, the antibody or antigen-binding fragment comprises an (e.g., IgG) Fc portion comprising a G236A mutation, an A330L mutation, and an I332E mutation (GAALIE), and does not comprise an S239D mutation (e.g., comprising a native S at position 239). In a specific embodiment, the antibody or antigen-binding fragment comprises an Fc polypeptide or fragment thereof comprising the following substitution mutations: M428L/N434S and G236A/A330L/I332E, (and may comprise or consist of the amino acid sequence set forth in SEQ ID NOs: 71 to 75), and optionally does not comprise S239D (e.g., comprises S at 239). In a specific embodiment, the antibody or antigen-binding fragment comprises an Fc polypeptide or fragment thereof comprising the following substitution mutations: M428L/N434A and G236A/A330L/I332E, (and may comprise or consist of the amino acid sequence set forth in SEQ ID NOs: 76 to 80), and optionally does not comprise S239D (e.g., comprises S at 239). In certain embodiments, the antibody or antigen-binding fragment comprises an Fc polypeptide or fragment thereof comprising the following substitution mutations: M428L/N434S (or M428L/N434A) and G236A/S239D/A330L/I332E. In some embodiments, antibodies or antigen-binding fragments (described further herein) are provided that comprise one or more amino acid mutations described in any one of (i) to (xviii) in a (e.g., human) IgG1 heavy chain: (i) G236A, L328V, and Q295E; (ii) G236A, P230A, and Q295E; (iii) G236A, R292P, and I377N; (iv) G236A, K334A, and Q295E; (v) G236S, R292P, and Y300L; (vi) G236A and Y300L; (vii) G236A, R292P, and Y300L; (viii) G236S, G420V, G446E, and L309T; (ix) (x) R292P and Y300L; (xi) G236A and R292P; (xii) Y300L; (xiii) E345K, G236S, L235Y, and S267E; (xiv) E272R, L309T, S219Y, and S267E; (xv) G236Y; (xvi) G236W; (xvii) F243L, G446E, P396L, and S267E; (xviii) G236A, S239D, and H268E, wherein the numbering of the amino acid residues is according to the EU index as described in Kabat. In certain embodiments, the antibody or antigen-binding fragment is afucosylated. In some embodiments, the antibody or antigen-binding fragment further comprises one or more mutations that enhance binding to human FcRn, such as M428L and N434S mutations or M428L and N434A mutations (EU numbering) or any other mutation(s) that enhance binding to human FcRn, such as those described herein. In certain embodiments, the antibody or antigen-binding fragment is defucosylated. In certain embodiments, the antibody or antigen-binding fragment comprises I) VH and VL having an amino acid sequence as set forth in any one of the following SEQ ID NOs: 23 and 27, respectively; 31 and 37, respectively; 35 and 37, respectively; and 36 and 37, respectively; II) CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 as set forth in VH and VL having an amino acid sequence as set forth in any one of the following: 1) SEQ ID NOs: 23 and 27, respectively; 2) SEQ ID NOs: 23 and 37; 3) SEQ ID NOs: 31 and 27; 4) SEQ ID NOs: 31 and 37; 5) SEQ ID NOs: 35 and 27; 6) SEQ ID NOs: 35 and 37; 7) SEQ ID NOs: 36 and 27; 8) SEQ ID NOs: 36 and 37; 9) SEQ ID NOs: 87; 21) SEQ ID NO: 188 and 193; 22) SEQ ID NO: 190 and 87; 23) SEQ ID NO: 191 and 87; 24) SEQ ID NO: 192 and 87; 25) SEQ ID NO: 193 and 87; 26) SEQ ID NO: 194 and 87; 27) SEQ ID NO: 195 and 87; 28) SEQ ID NO: 196 and 87; 29) SEQ ID NO: 197 and 87; 30) SEQ ID NO: 198 and 87; 31) SEQ ID NO: 198 and 87; 32) SEQ ID NO: 199 and 87; 33) SEQ ID NO: 190 and 193; 24) SEQ ID NOs: 93 and 97; 25) SEQ ID NOs: 93 and 225; 26) SEQ ID NOs: 93 and 228; 27) SEQ ID NOs: 93 and 231; 28) SEQ ID NOs: 197 and 97; 29) SEQ ID NOs: 197 and 225; 30) SEQ ID NOs: 197 and 228; 31) SEQ ID NOs: 197 and 231; 32) SEQ ID NOs: 201 and 97; 33) SEQ ID NOs: 201 and 225; 34) SEQ ID NOs: 201 and 228; 35) SEQ ID NOs: 201 and 231; 36) SEQ ID NOs: 204 and 97; 37) SEQ ID NOs: 204 and 225; 38) SEQ ID NOs: 49) SEQ ID NO: 212 and 225; 50) SEQ ID NO: 212 and 228; 51) SEQ ID NO: 212 and 231; 52) SEQ ID NO: 214 and 97; 53) SEQ ID NO: 64) SEQ ID NO: 220 and 97; 65) SEQ ID NO: 220 and 225; 66) SEQ ID NO: 220 and 228; 67) SEQ ID NO: 220 and 231; 68) SEQ ID NO: 220 and 231; 79) SEQ ID NO: 235 and 260; 80) SEQ ID NO: 238 and 105; 81) SEQ ID NO: 238 and 254; 82) SEQ ID NO: 238 and 257; 83) SEQ ID NO: 238 and 260; 84) SEQ ID NO: 241 and 105; 85) SEQ ID NO: 241 and 254; 86) SEQ ID NO: 241 and 257; 87) SEQ ID NO: 241 and 260; 88) SEQ ID NO: 243 and 105; 89) SEQ ID NO: 243 and 254; 90) SEQ ID NO: 243 and 257; 91) SEQ ID NO: 243 and 260; 92) SEQ ID NO: 245 and 105; 93) SEQ ID NO: 245 and 254; 94) SEQ ID NO: 245 and 257; 95) SEQ ID NO: 245 and 260; 96) SEQ ID NO: 247 and 105; 97) SEQ ID NO: 108) SEQ ID NO: 111 and 115; 109) SEQ ID NO: 111 and 121; 110) SEQ ID NO: 111 and 157; 111) SEQ ID NO: 111 and 157; 112) SEQ ID NO: 111 and 157; 113) SEQ ID NO: 111 and 157; 114) SEQ ID NO: 111 and 157; 115) SEQ ID NO: 111 and 157; 116) SEQ ID NO: 111 and 157; 117) SEQ ID NO: 111 and 157; 118) SEQ ID NO: 111 and 157; 119) SEQ ID NO: 112 and 113; 120) SEQ ID NO: 113 and 114; 121) SEQ ID NO: 114 and 1157; 115) SEQ ID NO: 115 11) SEQ ID NO: 111 and 272; 112) SEQ ID NO: 111 and 277; 113) SEQ ID NO: 111 and 279; 114) SEQ ID NO: 111 and 282; 115) SEQ ID NO: 111 and 286; 116) SEQ ID NO: 111 and 290; 117) SEQ ID NO: 125 and 115; 118) SEQ ID NO: 125 and 121; 119) SEQ ID NO: 125 and 157; 120) SEQ ID NO: 125 and 272; 121) SEQ ID NO: 125 and 277; 122) SEQ ID NO: 125 and 279; 123) SEQ ID NO: 125 and 282; 124) SEQ ID NO: 125 and 286; 125) SEQ ID 134) SEQ ID NO: 131 and 121; 135) SEQ ID NO: 131 and 157; 136) SEQ ID NO: 131 and 272; 137) SEQ ID NO: 131 and 277; 138) SEQ ID NO: 131 and 279; 139) SEQ ID NO: 128 and 282; 140) SEQ ID NO: 128 and 286; 141) SEQ ID NO: 128 and 290; 142) SEQ ID NO: 128 and 115; 143) SEQ ID NO: 131 and 121; 144) SEQ ID NO: 131 and 121; 145) SEQ ID NO: 131 and 157; 146) SEQ ID NO: 131 and 272; 147) SEQ ID NO: 131 and 277; 148) SEQ ID NO: 131 and 279 147) SEQ ID NO: 134 and 279; 148) SEQ ID NO: 134 and 282; 149) SEQ ID NO: 134 and 286; 150) SEQ ID NO: 134 and 290; 151) SEQ ID NO: 137 and 115; 152) SEQ ID NO: 137 and 121; 153) SEQ ID NO: 137 and 157; 154) SEQ ID NO: 137 and 272; 155) SEQ ID NO: 137 and 277; 156) SEQ ID NO: 137 and 279; 157) SEQ ID NO: 137 and 282; 158) SEQ ID NO: 137 and 286; 159) SEQ ID NO: 137 and 290; 160) SEQ ID NO: 141 and 115; 161) SEQ ID NO: 141 and 121; 162) SEQ ID NO: 141 and 157; 162) SEQ ID NO: 141 and 272; 162) SEQ ID NO: 141 and 277; 163) SEQ ID NO: 164) SEQ ID NO: 141 and 282; 165) SEQ ID NO: 141 and 286; 166) SEQ ID NO: 141 and 290; 167) SEQ ID NO: 145 and 115; 168) SEQ ID NO: 145 and 121; 169) SEQ ID NO: 145 and 157; 170) SEQ ID NO: 145 and 272; 171) SEQ ID NO: 145 and 277; 172) SEQ ID NO: 145 and 279; 173) SEQ ID NO: 145 and 282; 174) SEQ ID NO: 145 and 282; 175) SEQ ID NO: 145 and 286; 176) SEQ ID NO: 145 and 290; 177) SEQ ID NO: 145 and 115; 168) SEQ ID NO: 145 and 121; 169) SEQ ID NO: 145 and 157; 170) SEQ ID NO: 145 and 272; 171) SEQ ID NO: 145 and 277; 172) SEQ ID NO: 145 and 279; 173) SEQ ID NO: 145 and 282; 174) SEQ ID NO: 145 and 282; 175) SEQ ID NO: 145 and 286; 176) SEQ ID NO: 145 and 290; 177) SEQ ID 186) SEQ ID NO: 149 and 290; 187) SEQ ID NO: 153 and 115; 188) SEQ ID NO: 153 and 121; 189) SEQ ID NO: 153 and 157; 180) SEQ ID NO: 149 and 272; 181) SEQ ID NO: 149 and 277; 182) SEQ ID NO: 149 and 279; and 183) SEQ ID NO: 149 and 282; 184) SEQ ID NO: 149 and 286; 185) SEQ ID NO: 149 and 290; 186) SEQ ID NO: 153 and 115; 187) SEQ ID NO: 153 and 121; 188) SEQ ID NO: 153 and 157; 189) SEQ ID NO: 153 and 272; 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 264 and 115; 196) SEQ ID NO: 264 and 121; 197) SEQ ID NO: 264 and 157; 198) SEQ ID NO: 264 and 272; 199) SEQ ID NO: 264 and 277; 200) SEQ ID NO: 264 and 279; 201) SEQ ID NO: 264 and 282; 202) SEQ ID NO: 264 and 286; 203) SEQ ID NO: 264 and 290; 204) SEQ ID NO: 20) SEQ ID NO: 266 and 115; 205) SEQ ID NO: 266 and 121; 206) SEQ ID NO: 266 and 157; 207) SEQ ID NO: 266 and 272; 208) SEQ ID NO: 266 and 277; 209) SEQ ID NO: 266 and 279; 210) SEQ ID NO: 266 and 282; 211) SEQ ID NO: 266 and 286; 212) SEQ ID NO: 266 and 290; 213) SEQ ID NO: 269 and 115; 214) SEQ ID NO: 269 and 121; 215) SEQ ID NO: 269 and 157; 216) SEQ ID NO: 269 and 157; 217) SEQ ID NO: 269 and 272; 218) SEQ ID NO: 269 and 277; 219) SEQ ID NO: 269 and 279; 219) SEQ ID NO: 269 and 282; 220) SEQ ID NO: 269 and 286; or 221) SEQ ID NO: 269 and 290, as determined by any CDL determination scheme disclosed herein; or (III) CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 having an amino acid sequence as follows (i) SEQ ID NO: 24 to 26 or 32 to 34 and 28 to 30 or 38 to 40, respectively; (ii) SEQ ID NO: 32 to 34 and 38 to 40, respectively; (iii) SEQ ID NO: 84 to 86 or 84, 85 and 186 and 88 to 90 or 194, 89, and 90, respectively; (iv) SEQ ID NO: 94 to 96; 198, 95 and 96; 208, 95 and 96; 94, 95, and 199; 198, 95 and 199; 208, 95, and 199; 94, 95, and 202; 198, 95, and 205; 208, 95, and 199; 205, 95, and 202; or 208, 95, and 205, and 98, 39, and 99; 226, 39, and 99; or 229, 39, and 232; (v) * SEQ ID NO: 112 to 114; 112, 126, and 114; 112, 129, and 114; 112, 132, and 114; 112, 135, and 114; 112, 138, and 114; 112, 142, and 114; 112, 146, and 114; 112, 150, and 114; 112, 154, and 114; 112, 267, and 114; 112, 270, and 114; 112, 113, and 139 ; 112, 126, and 139; 112, 129, and 139; 112, 132, and 139; 112, 135, and 139; 112, 138, and 139; 112, 142, and 139; 112, 146, and 139; 112, 150, and 139; 112, 154, and 139; 112, 267, and 139; 112, 270, and 139; 112, 113, and 143; 112, 12 6, and 143; 112, 129, and 143; 112, 132, and 143; 112, 135, and 143; 112, 138, and 143; 112, 142, and 143; 112, 146, and 143; 112, 150, and 143; 112, 154, and 143; 112, 267, and 143; 112, 270, and 143; 112, 113, and 147; 112, 126, and 147; 112, 129, and 147; 112, 132, and 147; 112, 135, and 147; 112, 138, and 147; 112, 142, and 147; 112, 146, and 147; 112, 150, and 147; 112, 154, and 147; 112, 267, and 147; 112, 270, and 147; 112, 113, and 151; 112, 126, and 151; 112, 129 and 151; 112, 132, and 151; 112, 135, and 151; 112, 138, and 151; 112, 142, and 151; 112, 146, and 151; 112, 150, and 151; 112, 154, and 151; 112, 267, and 151; 112, 270, and 151; 112, 113, and 155; 11 2, 126, and 155; 112, 129, and 155; 112, 132, and 155; 112, 135, and 155; 112, 138, and 155; 112, 142, and 155; 112, 146, and 1551; 112, 150, and 155; 112, 154, and 155; 112, 267, and 155; or 112, 270, and 155; and 116 to 118; 116, 274, and 118; 116, 287, and 118; 116, 117, and 122; 116, 274, and 122; 116, 287, and 122; 116, 117, and 158; 116, 274, and 275; 116, 287, and 275; 116, 117, and 280; 116, 27 4, and 280; 116, 287, and 280; 116, 117, and 284; 116, 274, and 284; 116, 287, and 284; 116, 117, and 288; 116, 274, and 288; 116, 287, and 288; 116, 117, and 291; 116, 274, and 291; 116, 287, and 291; 2 73, 117, and 118; 273, 274, and 118; 273, 287, and 118; 273, 117, and 122; 273, 274, and 122; 273, 287, and 122; 273, 117, and 158; 273, 274, and 275; 273, 287, and 275; 273, 117, and 280; 273, 274, and 280; 1273, 287, and 280; 273, 117, and 284; 273, 274, and 284; 273, 287, and 284; 273, 117, and 288; 273, 274, and 288; 273, 287, and 288; 273, 117, and 291; 273, 274, and 291; 273, 287, and 291; 28 3, 117, 118; 283, 274, and 118; 283, 287, and 118; 283, 117, and 122; 283, 274, and 122; 283, 287, and 122; 283, 117, and 158; 283, 274, and 275; 283, 287, and 275; 283, 117, and 280; 283, 274, and 2 80; 283, 287, and 280; 283, 117, and 284; 283, 274, and 284; 283, 287, and 284; 283, 117, and 288; 283, 274, and 288; 283, 287, and 288; 283, 117, and 291; 283, 274, and 291; or 283, 287, and 291; and (A) The Fc portion comprises the following substitution mutations: (i) G236A, L328V, and Q295E; (ii) G236A, P230A, and Q295E; (iii) G236A, R292P, and I377N; (iv) G236A, K334A, and Q295E; (v) G236S, R292P, and Y300L; (vi) G236A and Y300L; (vii) G236A, R292P, and Y300L; (viii) G236S, G420V, G446E, and L309T; (ix) G236A and R292P; (x) R292P and Y300L; (xi) G236A and R292P; (xii) Y300L; (xiii) E345K, G236S, L235Y, and S267E; (xiv) E272R, L309T, S219Y, and S267E; (xv) G236Y; (xvi) G236W; (xvii) F243L, G446E, P396L, and S267E; (xviii) G236A, S239D, and H268E; (xix) M428L/N434S; (xx) M428L/N434A; (xxi) G236A/A330L/I332E/ M428L/N434S; (xxii) or (xxiii) any two or more of (i) to (xxii); or (B) an Fc portion comprising or consisting of an Fc polypeptide or fragment thereof comprising or consisting of an amino acid sequence having at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity to SEQ ID NOs: 44 to 80, optionally not a naturally occurring variant thereof, or comprising or consisting of an amino acid sequence as set forth in SEQ ID NOs: 52 to 80. In certain embodiments, the antibody or antigen-binding fragment comprises a mutation that alters glycosylation, wherein the mutation that alters glycosylation comprises N297A, N297Q, or N297G, and/or the antibody or antigen-binding fragment is partially or completely aglycosylated and/or partially or completely defucosylated. Host cell cell lines and methods for producing partially or completely deglycosylated or partially or completely defucosylated antibodies and antigen-binding fragments are known (see, e.g., PCT Publication No. WO 2016/181357; Suzuki et al. Clin. Cancer Res. 13(6): 1875-82 (2007); Huang et al. MAbs 6: 1-12 (2018)). The antibodies or antigen-binding fragments of the present disclosure may be fucosylated (e.g., comprise one or more fucosyl moieties, and generally comprise a native (wild-type) fucosylation pattern or a fucosylation pattern comprising one or more additional, or fewer, fucosyl moieties than native), or may be defucosylated. In particular, native IgG1 antibodies carry a glycan site at N297, and this is generally the only site in the antibody where a core fucosyl moiety can be found, although some glycan sites may be generated by mutation during antibody development (e.g., in a variable domain). Fucosylation of Fc polypeptides or fragments thereof, or antibodies can be achieved by introducing amino acid mutations to introduce or disrupt the fucosylation site (e.g., mutations at N297, such as N297Q or N297A, to disrupt the formation of a glycan that may include a core fucosylation portion), however it is generally preferred to maintain N297 and its glycans, such as by expressing the polypeptide in a host cell that has been genetically engineered to lack the ability to fucosylate the polypeptide (or to have an inhibitory or impaired ability); by expressing the polypeptide under conditions in which the host cell's ability to fucosylate the polypeptide is impaired (e.g., in the presence of 2-fluoro-L-fucose (2FF)), or similar conditions. The defucosylated polypeptide may comprise a fucosylation moiety, or substantially a fucosylation moiety, and/or may be expressed by a host cell that is genetically engineered to lack the ability to fucosylate the polypeptide (or to have an inhibitory ability or an impaired ability) and/or may be expressed under conditions in which the host cell's ability to fucosylate the polypeptide is impaired (e.g., in the presence of 2-fluoro-L-fucose (2FF)). In some embodiments, the polypeptide does not comprise a core fucosylation moiety at Asn297. In some embodiments, the defucosylated polypeptide has increased binding to FcγRIIIA. In some cases, adding 2FF to a culture medium comprising host cells expressing an antibody produces about 85% or more of the antibody without the fucosylation moiety. Thus, when a plurality of antibodies are produced in the presence of 2FF or a similar reagent, the plurality of antibodies may be described as "defucosylated". In some cases, a plurality of polypeptides or antibodies may be described as, for example, defucosylated, meaning that about 85% or more of the individual polypeptides or antibody molecules of the plurality of polypeptides or antibodies do not contain a fucosyl moiety. In certain preferred embodiments, the defucosylated antibody or polypeptide or a population or plurality of antibodies or polypeptides thereof comprises asparagine (N) at EU position 297. Fucosylation or lack of fucosylation may be assessed using, for example, mass spectrometry, such as electrospray mass spectrometry (ESI-MS). In some embodiments, a composition comprising any one or more of a plurality of the presently disclosed polypeptides is provided, wherein the composition comprises a defucosylated polypeptide. In certain embodiments, the antibody or antigen-binding fragment is able to induce sustained protection in an individual even once no detectable levels of the antibody or antigen-binding fragment are found in the individual (i.e., when the antibody or antigen-binding fragment has been cleared from the individual after administration). Such protection is referred to herein as a vaccine effect. Without wishing to be bound by theory, it is believed that dendritic cells can internalize the complex of antibody and antigen and then induce or promote an endogenous immune response to the antigen. In certain embodiments, the antibody or antigen-binding fragment comprises one or more modifications, such as, for example, mutations in Fc, which comprise G236A, A330L, and I332E, which can activate dendritic cells that can induce, for example, T cell immunity to the antigen. In certain embodiments, the antibodies or antigen-binding fragments of the present disclosure comprise an Fc variant selected from the Fc variants summarized in Table 1 (see also PCT Publication No. WO 2022/251119). In certain embodiments, the Fc variant, or antibody or antigen-binding fragment is fucosylated. In other embodiments, the Fc variant, or antibody or antigen-binding fragment is defucosylated. Table 1. Fc variants (fucosylated unless otherwise indicated) and their properties Variants ( one or more substitution mutations vs. wild-type human IgG1 Fc) Certain properties of one or more of the variants shown, such as compared to fucosylated wild-type human IgG1 G236A_L328V_Q295E Increased binding to human FcγRIIa (H131 allele and R131 allele); comparable or reduced binding to human FcγRIIb (e.g., as determined by MSD and/or surface plasmon resonance); increased ratio of binding to human FcγRIIa (H131 allele or R131 allele) to binding to human FcγRIIb; comparable binding to human FcRn; comparable production titer; increased signaling through FcγRIIa in host cells and/or decreased signaling through FcγRIIb in host cells; Tm differs by 12 ^⸰ C or less from wild type; G236S_R292P_Y300L has improved binding to C1q G236A_P230A_Q295E G236A_R292P_I377N G236A_K334A_Q295E G236S_R292P_Y300L G236A_Y300L Increased binding to human FcγRIIa (H131 (greater than 18-fold) and R131 (greater than 4-fold)); similar binding to human FcγRIIb or decreased binding to human FcγRIIb (e.g., as measured by surface plasmon resonance); increased ratio of binding to human FcγRIIa (H131 or R131) versus binding to human FcγRIIb; comparable binding to human FcRn; comparable production titer; increased signaling through FcγRIIa in host cells and/or decreased signaling through FcγRIIb in host cells; Tm differs by 4.5 ^⸰ C from wild-type G236A_R292P_Y300L Increased binding to human FcγRIIa (H131 (over 14-fold) and R131 (over 2.7-fold)); similar binding to human FcγRIIb; increased ratio of binding to human FcγRIIa (H131 or R131) to human FcγRIIb; binding to human FcγRIIIa (V158 allele and F158 allele); comparable binding to human FcRn; comparable production titer; increased signaling via FcγRIIa and/or FcγRIIIa in host cells and/or reduced signaling via FcγRIIb in host cells; increased signaling via FcγRIIa in host cells and/or reduced signaling via FcγRIIb in host cells; Tm differs by 4 ^⸰ C from wild type; comparable binding to human C1q G236S_G420V_G446E_L309T Increased binding to human FcγRIIa; decreased binding to human FcγRIIb (less than 0.5-fold); increased ratio of binding to human FcγRIIa (H131 or R131) to binding to human FcγRIIb; comparable binding to human FcRn; comparable production titer; increased signaling through FcγRIIa and/or FcγRIIIa in host cells, and/or decreased signaling through FcγRIIb in host cells; Tm differs by 4 ^⸰ C or less from wild type G236A_R292P R292P_Y300L Increased binding to human FcγRIIIa (V158 and F158); increased binding to human C1q; Tm differs by 4 ^⸰ C from wild type Y300L Increased binding to human C1q E345K_G236S_L235Y_S267E E272R_L309T_S219Y_S267E G236Y G236W F243L_G446E_P396L_S267E G236A (defucosylated) Increased binding to human FcγRIIa (H131) and mouse FcγRIIa (R131), decreased binding to human FcγRIIb, increased binding to human FcγRIIIa (V158) and mouse FcγRIIIa (F158), increased binding to human FcγRIIIb, somewhat decreased binding to human FcRn, Tm 0.15 ^⸰ C different from wild type or 0.9 ^⸰ C different from wild type or 0.8 ^⸰ C different from wild type or 0.7 ^⸰ C different from wild type S239D_H268E_G236A Increased binding to and signaling through all tested human FcγRs: FcγRIIA (H131); FcγRIIA (R131); FcγRIIB; FcγRIIIA (V158); FcγRIIIA (F158); FcγRIIIB; In addition, when anti-HBV antibodies with S239D_H268E_G236A_M428L_N434S were bound to hBsAg, the resulting immune complexes were incubated with MoDCs; MoDCs were subsequently incubated with donor CD4+ T cells, resulting in an increase in the percentage of NFAT+CD69+CD3+CD4+ T cells compared to antibodies with M428L_N434S alone. In some embodiments, an anti-parvovirus antibody or antigen-binding fragment is provided, which comprises one or more amino acid mutations described in any of the following (i) to (xviii) in the (e.g., human) IgG1 heavy chain: (i) G236A, L328V, and Q295E; (ii) G236A, P230A, and Q295E; (iii) G236A, R292P, and I377N; (iv) G236A, K334A, and Q295E; (v) G236S, R292P, and Y300L; (vi) G236A and Y300L; (vii) G236A, R292P, and Y300L; (viii) G236S, G420V, G446E, and L309T; (ix) G236A and R292P; (x) R292P and Y300L; (xi) G236A and R292P; (xii) Y300L; (xiii) E345K, G236S, L235Y, and S267E; (xiv) E272R, L309T, S219Y, and S267E; (xv) G236Y; (xvi) G236W; (xvii) F243L, G446E, P396L, and S267E; (xviii) G236A, S239D, and H268E, wherein the numbering of the amino acid residues is according to the EU index as described in Kabat. In certain embodiments, the antibody or antigen-binding fragment is defucosylated. In some embodiments, the antibody or antigen-binding fragment further comprises one or more mutations that enhance binding to human FcRn, such as M428L and N434S mutations or M428L and N434A mutations (EU numbering) or any other mutation or mutations that enhance binding to human FcRn, such as those described herein. In certain embodiments, the antibody or antigen-binding fragment is defucosylated. In any of the currently disclosed embodiments, the antibody or antigen-binding fragment comprises an Fc polypeptide or fragment thereof, which includes CH2 (or a fragment thereof), CH3 (or a fragment thereof), or CH2 and CH3, wherein the CH2, the CH3, or both may be of any isotype and may contain amino acid substitutions or other modifications as compared to the corresponding wild-type CH2 or CH3, respectively. In certain embodiments, the Fc disclosed herein comprises two CH2-CH3 polypeptides that are combined to form a dimer. In any of the currently disclosed embodiments, the antibody or antigen-binding fragment comprises an Fc polypeptide or a fragment thereof, which includes CH2 (or a fragment thereof), CH3 (or a fragment thereof), or CH2 and CH3, wherein the CH2, the CH3, or both may be of any isotype and may contain amino acid substitutions or other modifications as compared to the corresponding wild-type CH2 or CH3, respectively. In certain embodiments, the Fc disclosed herein comprises two CH2-CH3 polypeptides that are combined to form a dimer. In any of the currently disclosed embodiments, the antibody or antigen-binding fragment may be monoclonal. As used herein, the term "monoclonal antibody" (mAb) refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the individual antibodies comprising the population are identical except for possible naturally occurring mutations that may be present (in some cases in small amounts). Monoclonal antibodies are highly specific for being directed to a single antigenic site. Furthermore, in contrast to polyclonal antibody preparations that include different antibodies directed to different epitopes, each monoclonal antibody is directed to a single epitope of the antigen. In addition to their specificity, monoclonal antibodies are advantageous in that they can be synthesized without contamination by other antibodies. The term "monoclonal" should not be interpreted as requiring that the antibody be produced by any particular method. For example, monoclonal antibodies useful in the present invention may be prepared by first synthesizing the monoclonal antibody described by Kohler et al., Nature256:495 (1975), or can be prepared using recombinant DNA methods in bacteria, eukaryotic animals, or plant cells (see, e.g., U.S. Patent No. 4,816,567). Monoclonal antibodies can also be prepared using methods described, e.g., in Clacksonet al., Nature, 352:624-628(1991) and Marks et al., J. Mol. Biol., 222:581-597 (1991) from the phage antibody library. Monoclonal antibodies can also be obtained using the method disclosed in PCT Publication No. WO 2004/076677A2. The antibodies and antigen-binding fragments disclosed herein include "chimeric antibodies" in which a portion of the heavy chain and/or light chain is identical or homologous to a corresponding sequence in an antibody derived from a specific species or belonging to a specific antibody class or subclass, and the remaining portion of the chain(s) is identical or homologous to a corresponding sequence in an antibody derived from another species or belonging to another antibody class or subclass, as well as fragments of such antibodies, as long as they exhibit the desired biological activity (see U.S. Patent Nos. 4,816,567; 5,530,101 and 7,498,415; and Morrison et al., Proc.Natl.Acad.Sci.USA, 81:6851-6855(1984)). For example, chimeric antibodies can contain human and non-human residues. In addition, chimeric antibodies can contain residues that are not found in the recipient antibody or in the donor antibody. Such modifications are made to further improve the performance of the antibody. For further details, see Jones et al., Nature321:522-525(1986); Riechmann et al., Natur e332:323-329(1988); and Presta,Curr. Op. Struct. Biol. 2:593-596(1992). Chimeric antibodies also include primatized and humanized antibodies. "Humanized antibodies" are generally considered to be human antibodies that have one or more amino acid residues introduced into them from non-human sources. These non-human amino acid residues are generally taken from variable domains. Humanization can be carried out according to the method of Winter and colleagues (Jones et al., Nature, 321:522-525(1986); Reichmann et al., Nature, 332:323-327(1988); Verhoeyen et al., Science, 239:1534-1536(1988)), by replacing the corresponding sequence of a human antibody with a non-human variable sequence. Therefore, such "humanized" antibodies are chimeric antibodies (U.S. Patents Nos. 4,816,567; 5,530,101 and 7,498,415) in which substantially less than the entire human variable domain has been replaced by the corresponding sequence from a non-human species. In some cases, a "humanized" antibody is an antibody produced by non-human cells or animals and contains human sequences, such as H _Cdomain. A "human antibody" is an antibody that contains only sequences present in antibodies produced by humans. However, as used herein, a human antibody may include residues or modifications not found in naturally occurring human antibodies (e.g., antibodies isolated from humans), including those modifications and variant sequences described herein. These generally further improve or enhance antibody performance. In some cases, human antibodies are produced by genetically modified animals. For example, see U.S. Patents Nos. 5,770,429; 6,596,541 and 7,049,426. In certain embodiments, the antibodies or antigen-binding fragments disclosed herein are chimeric, humanized, or human. Polynucleotides, vectors, and host cells In another aspect, the present disclosure provides isolated polynucleotides encoding any of the antibodies disclosed herein or their antigen-binding fragments, or portions thereof (e.g., CDR, VH, VL, heavy chain, or light chain). In certain embodiments, the polynucleotide sequence is codon-optimized for expression in a host cell. Once the coding sequence is known or identified, codon optimization can be performed using known techniques and tools, such as using GenScript® Optimium Gene^TMTool; see also Scholten et al., Clin.Immunol.119:135, 2006). Codon-optimized sequences include partially codon-optimized sequences (i.e., one or more codons are optimized for expression in host cells) and fully codon-optimized sequences. It should be understood that, due to, for example, the degeneracy of genetic coding, splicing, etc., the polynucleotides encoding the antibodies and antigen-binding fragments disclosed herein may have different nucleotide sequences while still encoding the same antibodies and antigen-binding fragments. In some specific embodiments, the polynucleotide comprises or consists of the following: and SEQ ID NO: 81, 82, 91, 92, 100, 101, 109, 110, 119, 120, 123, 127, 130, 133, 136, 140, 144, 148, 152, 156, 159, 180, 182, 184, 187, 189, 191, 192, 195, 196, 200, 203, 206, 209, 211, 213, 94, 95, 96, 97, 98, 99, or 100%) identity to one or more of SEQ ID NOs: 123 and 159, in particular to a nucleic acid sequence having at least 85% (i.e. 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identity. In more specific embodiments, the single polynucleotide comprises or consists of: and one or more of SEQ ID NOs: 81, 91, 100, 109, 119, 123, 127, 130, 133, 136, 140, 144, 152, 180, 182, 184, 187, 189, 191, 196, 200, 203, 206, 209, 211, 213, 215, 217, 219, 221, 223, 262, 263, 265, and 268 and SEQ ID NO: 82, 92, 101, 110, 120, 159, 192, 195, 224, 227, 230, 233, 234, 237, 240, 242, 244, 246, 248, 250, 252, 253, 256, 259, 261, 271, 276, 278, 281, 285, and 289, in particular a nucleic acid sequence having at least 85% (i.e. 85%, 86, 87, 88, 89, 90, 91, 92, 92, 101, 110, 120, 159, 192, 195, 224, 227, 230, 233, 234, 237, 240, 242, 244, 246, 248, 250, 252, 253, 256, 259, 261, 271, 276, 278, 281, 285, and 289, in particular a nucleic acid sequence of SEQ ID NO: 123 and 159. In other more specific embodiments, at least two polynucleotides are provided, wherein the first polynucleotide comprises or consists of: and one or more of SEQ ID NO: 81, 91, 100, 109, 119, 123, 127, 130, 133, 136, 140, 144, 152, 180, 182, 184, 187, 189, 191, 196, 200, 203, 206, 209, 211, 213, 215, 217, 219, 221, 223, 262, 263, 265, and 268, in particular SEQ ID NO: 82, 92, 101, 110, 120, 159, 192, 195, 224, 227, 230, 233, 234, 237, 240, 242, 244, 246, 248, 250, 252, 253, 256, 259, 261, 271, 276, 278, 281, 285, and 289, in particular SEQ ID NO: 159 has at least 85% (i.e. 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identity with the nucleic acid sequence. In some embodiments, a single polynucleotide or a combination of polynucleotides comprises or consists of a combination of two nucleic acid sequences, which are as follows: i) 81 and 82; ii) any one of 91, 180, 182, 184, 187, 189, or 191 and any one of 92, 192, or 195; iii) any one of 100, 196, 200, 203, 206, 209, 211, 213, 215, 217, 219, 221, or 223 and any one of 101, 224, 227, 230, or 233; iv) 109 and any one of 110, 234, 237, 240, 242, 244, 246, 248, 250, 252, 253, 256, 259, or 261; or v) any one of 119, 123, 127, 130, 133, 136, 140, 144, 148, 152, 156, 262, 263, 265, or 268 and any one of 120, 159, 271, 276, 178, 281, 285, or 289, in particular 123 and 159, the nucleic acid sequences are at least 85% (i.e. 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identical. In any of the currently disclosed embodiments, the polynucleotide may comprise deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). In some embodiments, the RNA comprises a messaging RNA (mRNA). Also provided are vectors, wherein the vector comprises or contains a polynucleotide as disclosed herein (e.g., a polynucleotide encoding an antibody or antigen binding fragment that binds to two or more severe acute respiratory syndrome beta coronaviruses). The vector may comprise any one or more of the vectors disclosed herein. In a specific embodiment, a vector comprising a DNA plasmid construct encoding an antibody or antigen binding fragment, or a portion thereof (e.g., a so-called "DMAb", see, e.g., Muthumani et al., J Infect Dis.214(3):369-378(2016);Muthumani et al., Hum Vaccin Immunother 9:2253-2262 (2013)); Flingai et al., Sci Rep.5:12616(2015); and Elliott et al., NPJ Vaccines18 (2017), which antibody-encoding DNA constructs and methods of use thereof, including administration thereof, are incorporated herein by reference. In certain embodiments, the DNA plasmid construct comprises a single open reading frame encoding the heavy chain and light chain (or VH and VL) of the antibody or antigen-binding fragment, wherein the sequence encoding the heavy chain and the sequence encoding the light chain are optionally separated by a polynucleotide encoding a protease cleavage site and/or by a polynucleotide encoding a self-cleaving peptide. In some embodiments, the substituent component of the antibody or antigen-binding fragment is encoded by a polynucleotide contained in a single plasmid. In other embodiments, the substituent components of the antibody or antigen-binding fragment are encoded by polynucleotides contained in two or more plasmids (e.g., the first plasmid contains a polynucleotide encoding a heavy chain, VH, or VH+CH, and the second plasmid contains a polynucleotide encoding a cognate light chain, VL, or VL+CL). In certain embodiments, a single plasmid contains polynucleotides encoding heavy chains and/or light chains of two or more antibodies or antigen-binding fragments from the present disclosure. An exemplary expression vector is pVax1, available from Invitrogen®. The DNA plasmids of the present disclosure can be delivered to an individual by, for example, electroporation (e.g., intramuscular electroporation), or with an appropriate formulation (e.g., hyaluronidase). In another aspect, the present disclosure also provides host cells expressing antibodies or antigen-binding fragments according to the present disclosure; or containing or comprising vectors or polynucleotides according to the present disclosure. Examples of such cells include, but are not limited to, eukaryotic cells, such as yeast cells, animal cells, insect cells, plant cells; and prokaryotic cells, including Escherichia coli. In some specific embodiments, the cell is a mammalian cell. In certain such specific embodiments, the cell is a mammalian cell line, such as a CHO cell (e.g., a DHFR-CHO cell (Urlaub et al., PNAS 77:4216 (1980)), human embryonic kidney cells (e.g., HEK293T cells), PER.C6 cells, Y0 cells, Sp2/0 cells. NS0 cells, human liver cells, such as Hepa RG cells, myeloma cells, or fusion tumor cells. Other examples of mammalian host cell lines include mouse Sertoli cells (e.g., TM4 cells); monkey kidney CV1 line transformed by SV40 (COS-7); baby hamster kidney cells (BHK); African green monkey kidney cells (VERO-76); monkey kidney cells (CV1); human cervical carcinoma cells (HELA); human lung cells (W138); human liver cells (Hep G2); canine kidney cells (MDCK; buffalo rat liver cells (BRL 3A); mouse mammary tumor (MMT 060562); TRI cells; MRC5 cells; and FS4 cells. Mammalian host cell lines suitable for antibody production are also included in, for example, Yazaki and Wu, Methods in Molecular Biology, Vol. 248 (B. K. C. Lo, ed., Humana Press, Totowa, N.J.), pp. 255-268 (2003). In certain embodiments, the host cell is a prokaryotic cell, such as E. coli. The expression of peptides in prokaryotic cells such as E. coli is well established (see, e.g., Pluckthun, A. Bio/Technology 9:545-551 (1991). For example, antibodies can be produced in bacteria, particularly when glycosylation and Fc effector functions are not required. For expression of antibody fragments and polypeptides in bacteria, see, e.g., U.S. Patent Nos. 5,648,237; 5,789,199; and 5,840,523. In certain embodiments, cells can be transfected with expression vectors according to the present description. The term "transfection" refers to the introduction of a nucleic acid molecule, such as a DNA or RNA (e.g., mRNA) molecule, into a cell, such as into a eukaryotic cell. In the context of this specification, the term "transfection" encompasses any method known to those skilled in the art for introducing nucleic acid molecules into cells, such as into eukaryotic cells, including into mammalian cells. Such methods include, for example, electroporation, lipofection (e.g., based on cationic lipids and/or liposomes), calcium phosphate precipitation, nanoparticle-based transfection, virus-based transfection, or cationic polymer-based transfection (such as DEAE-dextran or polyethyleneimine). In certain specific embodiments, the introduction is non-viral. Furthermore, the host cells of the present disclosure can be stably or temporarily transfected with the vectors according to the present disclosure, for example, for expressing antibodies, or antigen-binding fragments thereof, according to the present disclosure. In such embodiments, the cells may be stably transfected with a vector as described herein. Alternatively, as disclosed herein, the cells may be temporarily transfected with a vector according to the present disclosure encoding an antibody or antigen binding fragment. In any of the presently disclosed embodiments, the polynucleotide may be heterologous to the host cell. Thus, the present disclosure also provides recombinant host cells heterologously expressing an antibody or antigen binding fragment of the present disclosure. For example, the cell may be a species different from the species from which the antibody is obtained in whole or in part (e.g., a CHO cell expressing a human antibody or an engineered human antibody). In some embodiments, the cell type of the host cell does not essentially express the antibody or antigen binding fragment. Furthermore, host cells may impart post-translational modifications (PTMs; e.g., glycosylation or fucosylation) to antibodies or antigen-binding fragments that are not present in the native state of the antibody or antigen-binding fragment (or in the native state of the parent antibody from which the antibody or antigen-binding fragment is engineered or derived). Such PTMs may result in functional differences (e.g., reduced immunogenicity). Thus, antibodies or antigen-binding fragments of the present disclosure produced by host cells as disclosed herein may include one or more post-translational modifications that are different from the antibody (or parent antibody) in its native state (e.g., human antibodies produced by CHO cells may contain more post-translational modifications than antibodies when isolated from humans and/or produced by native human B cells or plasma cells). Insect cells that can be used to express the binding proteins disclosed herein are known in the art and include, for example, Spodoptera frugiperda ( Spodoptera frugipera)Sf9 cells, Trichoplusia in BTI-TN5B1-4 cells, and Spodoptera frugiperda SfSWT01 "Mimic ^TM"Cell. See for example Palmberger et al., J. Biotechnol.152(3-4):160-166(2011). A number of bacillivirus strains have been identified that can be used with insect cells, particularly for transfection of Spodoptera frugiperda cells. Eukaryotic microorganisms (such as filamentous fungi or yeast) are also suitable hosts for the propagation or expression of protein-encoding vectors, and include fungal and yeast strains with "humanized" glycosylation pathways, resulting in the production of antibodies with partially or fully human glycosylation patterns. See Gerngross, Nat. Biotech.22: 1409-1414(2004); Li et al., Nat. Biotech.24:210-215 (2006). Plant cells can also be used as hosts for expressing the binding proteins disclosed herein. For example, the PLANTIBODIES™ technology (described in, e.g., U.S. Patent Nos. 5,959,177; 6,040,498; 6,420,548; 7,125,978; and 6,417,429) employs genetically modified plants to produce antibodies. In certain embodiments, the host cell comprises a mammalian cell. In certain specific embodiments, the host cell is a CHO cell, a HEK293 cell, a PER.C6 cell, a Y0 cell, a Sp2/0 cell, a NS0 cell, a human liver cell, a myeloma cell, or a fusion tumor cell. In a related aspect, the present disclosure provides a method for producing an antibody or an antigen binding fragment, wherein the method comprises culturing a host cell disclosed herein under conditions and for a time sufficient to produce the antibody or the antigen binding fragment. For example, a method for isolating and purifying a recombinantly produced antibody may include obtaining a supernatant from a suitable host cell/vector system that secretes the recombinant antibody into a culture medium, and then concentrating the culture medium using a commercially available filter. After concentration, the concentrate may be applied to a single suitable purification matrix or a series of suitable matrices, such as an affinity matrix or an ion exchange resin. One or more reverse phase HPLC steps may be used to further purify the recombinant polypeptide. These purification methods can also be used when isolating an immunogen from its natural environment. Methods for large-scale production of one or more of the isolated/recombinant antibodies described herein include batch cell cultures that are monitored and controlled to maintain appropriate culture conditions. Purification of soluble antibodies can be performed according to methods described herein and known in the art, and in accordance with the laws and guidelines of domestic and foreign regulatory agencies. Composition Also provided herein are compositions comprising any one or more of the antibodies, antigen-binding fragments, polynucleotides, vectors, or host cells disclosed herein, alone or in any combination, and may further comprise a pharmaceutically acceptable carrier, excipient, or diluent. Carriers, excipients, and diluents are discussed in further detail herein. In certain embodiments, the composition comprises two or more different antibodies or antigen-binding fragments according to the present disclosure. In certain embodiments, the antibodies or antigen-binding fragments used in the combination each independently have one or more of the following properties: neutralize one, two, three, four, five, or more naturally occurring SARS beta coronavirus variants; do not compete with each other for spike protein binding; bind to different SARS beta coronavirus spike protein epitopes; reduce the development of resistance to SARS beta coronavirus; when combined, reduce the ability to resist SARS beta coronavirus; The invention relates to a novel composition comprising an antibody or antigen binding fragment of the present invention that is effective in neutralizing one, two, three, four, five or more live SARS beta coronaviruses; when used in combination, exhibits an additive or synergistic effect on neutralizing one, two, three, four, five or more live SARS beta coronaviruses; exhibits effector function; is protective in one or more relevant animal models of infection; and can be produced in sufficient quantities for large-scale production. In certain embodiments, the composition comprises two or more different antibodies or antigen binding fragments according to the present disclosure. In certain embodiments, the first antibody or antigen-binding fragment and the second antibody or antigen-binding fragment may be A) both an antibody or antigen-binding fragment of S3A3, an antibody or antigen-binding fragment having sufficient CDR, VH, and/or VH identity to S3A3 to confer similar specific binding, or a fragment thereof, such as comprising: i) a VH sequence as in SEQ ID NO: 23 and a VL sequence as in SEQ ID NO: 27, ii) CDRs as described in SEQ ID NOs: 23 and 27, according to any numbering system disclosed herein, or iii) a VH sequence as in SEQ ID NO: 23 and 27, according to any numbering system disclosed herein, or iv) a VH sequence as in SEQ ID NO: 23 and 27, according to any numbering system disclosed herein. 24 to 26 (H1 to H3) and 28 to 30 (L1 to L3); B) an antibody or antigen-binding fragment of S3A19, an antibody or fragment thereof having sufficient CDR, VH, and/or VH identity to S3A19 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 31, 35, 36 or 43 and a VL sequence as SEQ ID NO: 37, iii) a CDR as set forth in any one of SEQ ID NOs: 31, 35, 36, or 43 and SEQ ID NO: 37, according to any numbering system disclosed herein, or as set forth in SEQ ID NO: C) an antibody or antigen-binding fragment of S3I2, an antibody or fragment thereof having sufficient CDR, VH, and/or VH identity to S3I2 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, or 190 and a VL sequence as any one of SEQ ID NOs: 87 or 194, ii) a CDR as described in any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, or 190, and any one of SEQ ID NOs: 87 or 193, according to any numbering system disclosed herein, or iii) a VH sequence as described in SEQ ID NOs: 83, 179, 181, 183, 185, 188, or 190, and a VL sequence as described in SEQ ID NOs: 87 or 194, 84 (H1), 85 (H2), and 86 or 186 (H3), and 88 or 194 (L1), 89 (L2), and 90 (L3); D) are antibodies or antigen-binding fragments of S3O13, antibodies or fragments thereof having sufficient CDR, VH, and/or VH identity with S3O13 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and a VL sequence as any one of SEQ ID NOs: 97, 225, 228, or 231, ii) a VL sequence as in SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and the CDRs described in any of SEQ ID NOs: 97, 225, 228, or 231, according to any numbering system disclosed herein, or iii) as described in SEQ ID NO: 94, 198, or 208 (H1), 95 (H2), and 96, 199, 202, or 205 (H3), and 98, 226, 229, or 232 (L1), 39 (L2), and 99 (L3); E) are antibodies or antigen-binding fragments of S3L17, antibodies or fragments thereof having sufficient CDR, VH, and/or VH identity to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence as any one of SEQ ID NOs: 105, 254, 257, or 260, ii) a VL sequence as in SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and the CDRs described in any of SEQ ID NOs: 105, 254, 257, or 260, according to any numbering system disclosed herein, or iii) as described in SEQ ID NO: 103 (H1), 85 (H2), and 104, 236, or 239 (H3), and the CDRs described in 106 or 255 (L1), 107 (L2), and 108 or 258 (H3); F) are antibodies or antigen-binding fragments of S2V29 (or both S2V29a or S2V29b), antibodies or fragments thereof having sufficient CDR, VH, and/or VH identity with S2V29 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NO: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and a VH sequence as SEQ ID NO: 115, 121, 157, 272, 277, 279, 282, 286, or 290, ii) any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290, according to any numbering system disclosed herein, or iii) any one of SEQ ID NOs: 112 (H1), 113 (H2), 114 (H3), 115 (H4), 116 (H5), 117 (H6), 118 (H7), 119 (H8), 120 (H9), 121 (H10), 122 (H111), 123 (H124), 125 (H25 126, 129, 132, 135, 138, 142, 146, 150, 154, 267, or 270 (H2), and 114, 139, 143, 147, 151, or 155 (H3) and 116, 273, or 283 (L1), 117, 274, or 287 (L2), and 118, 122, 158, 275, 280, 284, 288, or 192 (L3); G) is an antibody or antigen-binding fragment according to A), B), C), D), E), or F) and a different antibody or antigen-binding fragment according to A), B), C), D), E), or F). In certain embodiments, the composition comprises two or more different antibodies or antigen-binding fragments according to the present disclosure. In certain embodiments, the first antibody or antigen-binding fragment may be A) an antibody or antigen-binding fragment of S3A3, an antibody or fragment thereof having sufficient CDR, VH, and/or VH identity to S3A3 to confer similar specific binding, such as comprising: i) a VH sequence as in SEQ ID NO: 23 and a VL sequence as in SEQ ID NO: 27, ii) CDRs as described in SEQ ID NOs: 23 and 27, according to any numbering system disclosed herein, or iii) CDRs as described in SEQ ID NOs: 24 to 26 (H1 to H3) and 28 to 30 (L1 to L3); B) Antibodies or antigen-binding fragments of S3A19, antibodies or fragments thereof having sufficient CDR, VH, and/or VH identity to S3A19 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 31, 35, 36 or 43 and a VL sequence as SEQ ID NO: 37, iii) CDRs as described in any one of SEQ ID NOs: 31, 35, 36, or 43 and SEQ ID NO: 37, according to any numbering system disclosed herein, or CDRs as described in SEQ ID NOs: 32 to 34 (H1 to H3) and 37 to 40 (L1 to L3); C) Antibodies or antigen-binding fragments of S3I2, antibodies or fragments thereof having sufficient CDR, VH, and/or VH identity to S3I2 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, or 190 and a VL sequence as any one of SEQ ID NOs: 87 or 194, ii) CDRs as described in any one of SEQ ID NOs: 83, 179, 181, 183, 185, 188, or 190, and any one of SEQ ID NOs: 87 or 193, according to any numbering system disclosed herein, or iii) a VL sequence as described in SEQ ID NOs: 84 (H1), 85 (H2), and 86 or 186 (H3) and 88 or 194 (L1), 89 (L2), and 90 (L3); D) an antibody or antigen-binding fragment of S3O13, an antibody or fragment thereof having sufficient CDR, VH, and/or VH identity to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and a VL sequence as any one of SEQ ID NOs: 97, 225, 228, or 231, ii) a VL sequence as in SEQ ID NOs: 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and any one of SEQ ID NOs: 97, 225, 228, or 231, according to any numbering system disclosed herein, or iii) CDRs as described in SEQ ID NOs: 94, 198, or 208 (H1), 95 (H2), and 96, 199, 202, or 205 (H3), and 98, 226, 229, or 232 (L1), 39 (L2), and 99 (L3); E) Antibodies or antigen-binding fragments of S3L17, antibodies or fragments thereof having sufficient CDR, VH, and/or VH identity to S3L17 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence as any one of SEQ ID NOs: 105, 254, 257, or 260, ii) CDRs as described in any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and any one of SEQ ID NOs: 105, 254, 257, or 260, according to any numbering system disclosed herein, or iii) a VH sequence as described in any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence as any one of SEQ ID NOs: 105, 254, 257, or 260. 103 (H1), 85 (H2), and 104, 236, or 239 (H3), and the CDRs described in 106 or 255 (L1), 107 (L2), and 108 or 258 (H3); F) an antibody or antigen-binding fragment of S2V29 (or both S2V29a or S2V29b), an antibody or fragment thereof having sufficient CDR, VH, and/or VH identity to S2V29 to confer similar specific binding, such as comprising the following: i) a VH sequence as any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and a VH sequence as described in SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290, ii) any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290, according to any numbering system disclosed herein, or iii) any one of SEQ ID NOs: 112 (H1), 113 (H2), 114 (H3), 115 (H4), 116 (H5), 117 (H6), 118 (H7), 119 (H8), 120 (H9), 121 (H10), 122 (H111), 123 (H124), 125 (H25 126, 129, 132, 135, 138, 142, 146, 150, 154, 267, or 270 (H2), and 114, 139, 143, 147, 151, or 155 (H3) and 116, 273, or 283 (L1), 117, 274, or 287 (L2), and 118, 122, 158, 275, 280, 284, 288, or 192 (L3); and the second antibody or antigen-binding fragment may be sotorovimab, S2K146, S2X259, S2X324, S2X324-v3.1, or S309 or an antigen-binding fragment thereof, particularly having: a VH having the amino acid sequence of SEQ ID NO: 14 and having: a VH having the amino acid sequence of SEQ ID NO: 14 NO: 15, an antibody or antigen-binding fragment having a VH having an amino acid sequence of SEQ ID NO: 16 and a VL having an amino acid sequence of SEQ ID NO: 17, an antibody or antigen-binding fragment having a VH having an amino acid sequence of SEQ ID NO: 18 and a VL having an amino acid sequence of SEQ ID NO: 19, an antibody or antigen-binding fragment having a VH having an amino acid sequence of SEQ ID NO: 20 and a VL having an amino acid sequence of SEQ ID NO: 22, an antibody or antigen-binding fragment having a VH having an amino acid sequence of SEQ ID NO: 21 and a VL having an amino acid sequence of SEQ ID NO: 22, or a VH having an amino acid sequence of SEQ ID NO: 41 and a VL having an amino acid sequence of SEQ ID NO: 42, or an antibody or antigen-binding fragment having a VL with a CDR as found in any of the aforementioned VH and VL combinations according to any numbering system disclosed herein. In a specific embodiment, the second antibody or antigen-binding fragment thereof may be sotoviromab or S2K146. In some embodiments, the composition may comprise or may comprise: an antibody or antigen-binding fragment comprising or consisting of: A) a first antibody or antigen-binding fragment, which may be an antibody or antigen-binding fragment of S3L17, an antibody or antigen-binding fragment having sufficient CDR, VH, and/or VH identity to S3L17 to confer similar specific binding, or a fragment thereof, such as comprising: i) a VH sequence as any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence as any one of SEQ ID NOs: 105, 254, 257, or 260, ii) a VL sequence as any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence as any one of SEQ ID NOs: 105, 254, 257, or 260; NO: 105, 254, 257, or 260, according to any numbering system disclosed herein, or iii) the CDRs described in SEQ ID NO: 103 (H1), 85 (H2), and 104, 236, or 239 (H3), and 106 or 255 (L1), 107 (L2), and 108 or 258 (H3); and B) a second antibody or antigen-binding fragment, which may be an antibody or antigen-binding fragment of S2V29 (or both S2V29a or S2V29b), an antibody or antigen-binding fragment having sufficient CDR, VH, and/or VH identity with S2V29 to confer similar specific binding, or a fragment thereof, such as comprising the following: i) the CDR of SEQ ID NO: 115, 121, 157, 272, 277, 279, 282, 286, or 290, ii) the CDRs depicted in any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290, according to any numbering system disclosed herein, or iii) the CDRs depicted in any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290, according to any numbering system disclosed herein, or 112 (H1), 113 126, 129, 132, 135, 138, 142, 146, 150, 154, 267, or 270 (H2), and 114, 139, 143, 147, 151, or 155 (H3), and 116, 273, or 283 (L1), 117, 274, or 287 (L2), and 118, 122, 158, 275, 280, 284, 288, or 192 (L3). In some embodiments, a composition is provided comprising a first antibody or antigen-binding fragment and a second antibody or antigen-binding fragment (a multispecific (e.g., bispecific) antibody or antigen-binding fragment) or a combination therapy is provided comprising a first antibody or antigen-binding fragment and a second antibody or antigen-binding fragment, wherein the first antibody or antigen-binding fragment and the second antibody or antigen-binding fragment respectively comprise, or the multispecific antibody or antigen-binding fragment comprises CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3, and optionally VH and VL, are based on: (i) any S3A3 antibody and any S3A19 antibody; (ii) any S3A3 antibody and sotoviromab; (iii) any S3A3 antibody and S2K146; (iv) any S3A3 antibody and S2X259; (v) any S3A3 antibody and any S2X324 antibody; vi) any S3A3 antibody and S309; (vi) any S3A19 antibody and sotoviromab; (vii) any S3A19 antibody and S2K146; (viii) any S3A19 antibody and S2X259; (ix) any S3A19 antibody and any S2X324 antibody; (x) any S3A19 antibody and S309; (xi) any S3I2 antibody and any S3A3 antibody; (xii) any any S3I2 antibody and any S3A19 antibody; (xiii) any S3I2 antibody and sotoviromab; (xiv) any S3I2 antibody and S2K146; (xv) any S3I2 antibody and S2X259; (xvi) any S3I2 antibody and any S2X324 antibody; (xvii) any S3I2 antibody and S309; (xviii) any S3I2 antibody and any S3O13 antibody; (xviii) any S3I2 antibody and any S3O13 antibody; ix) any S3I2 antibody and any S3L17 antibody; (xx) any S3O13 antibody and any S3A3 antibody; (xxi) any S3O13 antibody and any S3A19 antibody; (xxii) any S3O13 antibody and sotoviromab; (xxiii) any S3O13 antibody and S2K146; (xxiv) any S3O13 antibody and S2X259; (xxv) any S3O13 antibody and any S2X324 antibody; (xxvi) any S3O13 antibody and S309; (xxvii) any S3O13 antibody and any S3L17 antibody; (xxviii) any S3L17 antibody and any S3A3 antibody; (xxix) any S3L17 antibody and any S3A19 antibody; (xxx) any S3L17 antibody and sotovir; (xxxi) any S3L17 antibody and S2K 146; (xxxii) any S3L17 antibody and S2X259; (xxxiii) any S3L17 antibody and any S2X324 antibody; (xxxiv) any S3L17 antibody and S309; (xxxv) any S2V29 antibody and any S3A3 antibody; (xxxvi) any S2V29 antibody and any S3A19 antibody; (xxxvii) any S2V29 antibody and sotovir Antibody; (xxxviii) any S2V29 antibody and S2K146; (xxxix) any S2V29 antibody and S2X259; (xl) any S2V29 antibody and any S2X324 antibody; (xli) any S2V29 antibody and S309; (lxlii) any S2V29 antibody and any S3L17 antibody; and (xliii) any S2V29 antibody and any S3O13 antibody. In certain embodiments, the composition comprises a first vector and a second vector, the first vector comprising a first plasmid and the second vector comprising a second plasmid, wherein the first plasmid comprises a polynucleotide encoding a heavy chain, VH, or VH+CH of an antibody or an antigen-binding fragment thereof, and the second plasmid comprises a polynucleotide encoding a cognate light chain, VL, or VL+CL of an antibody or an antigen-binding fragment thereof. In certain embodiments, the composition comprises a polynucleotide (e.g., mRNA) coupled to a suitable delivery vehicle or carrier. Exemplary vehicles or carriers for administration to human subjects include lipids or lipid-derived delivery vehicles, such as liposomes, solid lipid nanoparticles, oily suspensions, submicron lipid emulsions, lipid microbubbles, inverse lipid micelles, cochlear liposomes, lipid microtubules, lipid microcylinders, or lipid nanoparticles (LNPs) or nanoscale platforms (see, e.g., Li et al. Wilery Interdiscip Rev. Nanomed Nanobiotechnol. 11(2):e1530 (2019)). The principles, reagents and techniques for designing appropriate mRNA and formulating mRNA-LNPs and delivering the mRNA-LNPs are described in, for example, Pardi et al.( J Control Release 217345-351(2015)); Thess et al.( Mol Ther 23: 1456-1464(2015));Thran et al.( EMBO Mol Med 9(10):1434-1448(2017);Kose et al.( Sci. Immunol.4eaaw6647 (2019); and Sabnis et al.( Mol. Ther. 26:1509-1519 (2018)), the techniques include capping, codon optimization, nucleoside modification, purification of mRNA, incorporation of mRNA into stable lipid nanoparticles (e.g., ionizable cationic lipids/phosphatidylcholine/cholesterol/PEG-lipids; ionizable lipids: distearyl PC: cholesterol: polyethylene glycol lipids), and subcutaneous, intramuscular, intradermal, intravenous, intraperitoneal, and intratracheal administration of the mRNA-LNP, and are incorporated herein by reference. Methods and uses Also provided herein are methods for using the antibodies or antigen-binding fragments, nucleic acids, vectors, cells, or compositions disclosed herein for diagnosing severe acute respiratory syndrome beta coronavirus infection (e.g., in a human individual or in a sample obtained from a human individual). The diagnostic method (e.g., in vitro, ex vivo) may include contacting the antibody, antibody fragment (e.g., antigen-binding fragment) with the sample. Such a sample may be isolated from an individual, such as an isolated tissue sample taken from, for example, the nasal passages, sinus cavities, salivary glands, lungs, liver, pancreas, kidneys, ears, eyes, placenta, digestive tract, heart, ovaries, pituitary glands, adrenal glands, thyroid glands, brain, skin, or blood. The method of diagnosis may also include detecting antigen/antibody complexes, particularly after the antibody or antibody fragment has come into contact with the sample. Such a detection step can be performed on a bench, i.e. without any contact with the human or animal body. Embodiments of the detection method are well known to those of ordinary skill in the art and include, for example, ELISA (enzyme-linked immunosorbent assay), including direct, indirect and sandwich ELISA. Also provided herein is a method for treating an individual using the antibody or antigen-binding fragment disclosed herein, or a composition comprising the same, wherein the individual has, is believed to have, or is at risk of having an infection caused by a severe acute respiratory syndrome beta coronavirus. "Treatment" or "ameliorate" refers to the medical management of a disease, disorder or condition in a subject (e.g., a human or non-human mammal, such as a primate, horse, cat, dog, goat, mouse, or rat). Generally, an appropriate dose or treatment regimen comprising an antibody or composition of the present disclosure is administered in an amount sufficient to induce a therapeutic or prophylactic benefit. A therapeutic or prophylactic benefit includes improved clinical prognosis; reduction or alleviation of symptoms associated with the disease; reduction in the occurrence of symptoms; improved quality of life; longer disease-free state; reduction in disease severity, stabilization of disease state; delay or prevention of disease progression; remission; survival; prolonged survival; or any combination thereof. In some embodiments, the therapeutic or preventive benefit includes reducing or preventing hospitalization for SARS-CoV-2 infection (i.e., in a statistically significant manner). In some embodiments, the therapeutic or preventive benefit includes reducing the duration of hospitalization for SARS-CoV-2 infection (i.e., in a statistically significant manner). In some embodiments, the therapeutic or preventive benefit includes reducing or eliminating the need for respiratory interventions, such as intubation and/or the use of a ventilator. In some embodiments, the therapeutic or preventive benefit includes reversing advanced disease pathology and/or reducing mortality. The "therapeutically effective amount" or "effective amount" of the antibody, antigen binding fragment, polynucleotide, vector, host cell, or composition disclosed herein refers to the amount of the composition or molecule sufficient to produce a therapeutic effect, including improving clinical prognosis in a statistically significant manner; reducing or alleviating symptoms associated with the disease; reducing the occurrence of symptoms; improving quality of life; longer disease-free state; reducing disease severity, stabilizing disease state; delaying disease progression; remission; survival; or prolonging survival. When referring to the administration of an individual active ingredient alone, the therapeutically effective amount refers to the effect of that ingredient or a cell expressing that ingredient alone. When referring to a combination, whether administered sequentially, sequentially or simultaneously, a therapeutically effective amount refers to the combined amount of active ingredients that produce a therapeutic effect, or a combination of adjuvant active ingredients and cells expressing the active ingredients. The combination may include, for example, two different antibodies that specifically bind to SARS-CoV-2 antigens, which in certain embodiments may be the same or different SARS-CoV-2 antigens, and/or may include the same or different epitopes. Therefore, in certain embodiments, methods for treating SARS-CoV-2 infection in an individual are provided, wherein the methods comprise administering to the individual an effective amount of an antibody, antigen-binding fragment, polynucleotide, vector, host cell, or composition disclosed herein. Individuals that can be treated by the present disclosure are typically humans and other primate individuals, such as monkeys and apes for veterinary medical purposes. Other model organisms, such as mice and rats, can also be treated according to the present disclosure. In any of the foregoing specific examples, the individual can be a human individual. The individual can be male or female, and can be of any appropriate age, including infants, teenagers, adolescents, adults, and elderly individuals. It is believed that many criteria will cause a high risk of severe symptoms or death associated with severe acute respiratory syndrome beta coronavirus infection. These include but are not limited to age, occupation, general health condition, previous health conditions, and lifestyle. In some specific embodiments, the individual treated according to the present disclosure includes one or more risk factors. In certain embodiments, the human subject treated according to the present disclosure is an infant, a child, a young person, a middle-aged person, or an elderly person. In certain embodiments, the human subject treated according to the present disclosure is less than 1 year old, or is 1 to 5 years old, or is between 5 and 125 years old (e.g., 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, or 125 years old, including any and all ages therein or therebetween). In certain embodiments, the human subject treated according to the present disclosure is 0 to 19 years old, 20 to 44 years old, 45 to 54 years old, 55 to 64 years old, 65 to 74 years old, 75 to 84 years old, or 85 years old, or older. Middle-aged people, and especially the elderly, are believed to be particularly at risk. In specific embodiments, the human subject is 45 to 54 years old, 55 to 64 years old, 65 to 74 years old, 75 to 84 years old, or 85 years old, or older. In some embodiments, the human subject is male. In some embodiments, the human subject is female. In certain embodiments, the human subject treated according to the present disclosure is a resident of a nursing home or long-term care facility, a hospice worker, a healthcare provider or healthcare worker, a first responder, a family member or other close contact of an individual diagnosed with or suspected of having severe acute respiratory syndrome beta coronavirus infection, an overweight or clinically obese person, a smoker or a former smoker, a person who has or has had chronic obstructive pulmonary disease (COPD), a person with asthma (e.g., moderate to severe asthma), a person with an autoimmune disease or condition (e.g., diabetes), and/or a person with an immune Individuals with impaired or depleted immune systems (e.g., due to AIDS/HIV infection, cancer (e.g., leukemia), lymphodepleting therapy (e.g., chemotherapy), bone marrow or organ transplants, or genetic immune conditions), chronic liver disease, cardiovascular disease, lung or heart defects, or those who work or spend a long time in close contact with others (e.g., in factories, transportation centers, hospital environments, etc.). In certain embodiments, the individual treated according to the present disclosure has received a severe acute respiratory syndrome beta coronavirus vaccine and the vaccine was determined to be ineffective, for example, by infection or symptoms after vaccination of the individual, by clinical diagnosis, or by scientific or regulatory guidelines. In certain embodiments, the treatment is administered as peri-exposure prophylaxis. In certain embodiments, the treatment is administered to individuals with mild to moderate disease, which may be in an outpatient setting. In certain embodiments, the treatment is administered to individuals with moderate to severe disease, such as those requiring hospitalization. Typical routes of administration of the presently disclosed compositions thus include, but are not limited to, oral, topical, transdermal, inhalation, parenteral, sublingual, buccal, rectal, vaginal, and intranasal. The term "parenteral" as used herein includes subcutaneous injections, intravenous, intramuscular, intrasternal injection or infusion techniques. In certain embodiments, administration comprises administration by a route selected from the group consisting of oral, intravenous, parenteral, intragastric, intrapleural, intrapulmonary, intrarectal, intradermal, intraperitoneal, intratumoral, subcutaneous, topical, transdermal, intracisternal, intrathecal, intranasal, and intramuscular. In certain embodiments, the method comprises orally administering an antibody, an antigen binding fragment, a polynucleotide, a vector, a host cell, or a composition to a subject. The pharmaceutical compositions according to certain embodiments of the present invention are formulated so that the active ingredients contained therein are bioavailable after the composition is administered to a patient. The composition to be administered to an individual or patient may be in the form of one or more dosage units, where, for example, a tablet may be a single dosage unit, and the container of the antibody or antigen binding agent described herein in the form of an aerosol may accommodate multiple dosage units. Actual methods for preparing such dosage forms are known or will be apparent to those of ordinary skill in the art; see, for example, Remington: The Science and Practice of Pharmacy, 20th Edition (Philadelphia College of Pharmacy and Science, 2000). The composition to be administered will in any case contain an effective amount of the antibody or antigen binding fragment, polynucleotide, vector, host cell, or composition disclosed herein for use in treating the disease or condition of interest according to the teachings herein. The composition may be in the form of a solid or liquid. In some embodiments, one or more carriers are microparticles, so that the composition is, for example, in the form of tablets or powders. One or more carriers may be liquids, and the composition is, for example, an oral oil, an injectable liquid, or an aerosol that can be used, for example, for inhalation administration. When oral administration is intended, the pharmaceutical composition is preferably in solid or liquid form, wherein semi-solid, semi-liquid, suspension, and gel forms are included in the forms considered as solid or liquid herein. As a solid composition for oral administration, the pharmaceutical composition can be formulated into powders, granules, compressed tablets, pills, capsules, chewable tablets, powder tablets, etc. Such solid compositions will generally contain one or more inert diluents or edible carriers. In addition, one or more of the following may be present: binders such as carboxymethylcellulose, ethylcellulose, microcrystalline cellulose, tragacanth gum or gelatin; formulators such as starch, lactose or dextrin; disintegrants such as alginic acid, sodium alginate, starch sodium hydroxyacetate (Primogel), corn starch, etc.; lubricants such as magnesium stearate or hydrogenated vegetable oil (Sterotex); glidants such as colloidal silicon dioxide; sweeteners such as sucrose or saccharin; flavorings such as mint, methyl salicylate or citrus flavoring; and coloring agents. When the composition is in the form of a capsule, such as a gelatin capsule, it may contain, in addition to the above types of materials, a liquid carrier such as polyethylene glycol or oil. The composition may be in the form of a liquid, such as an elixir, syrup, solution, emulsion or suspension. As two examples, the liquid may be used for oral administration or for delivery by injection. When intended for oral administration, in addition to the compounds of the present invention, the preferred composition also contains one or more of a sweetener, a preservative, a dye/colorant and a flavor enhancer. In a composition intended for administration by injection, one or more of surfactants, preservatives, wetting agents, dispersants, suspending agents, buffers, stabilizers and isotonic agents may be included. Liquid pharmaceutical compositions, whether in the form of solutions, suspensions or other similar forms, may include one or more of the following adjuvants: sterile diluents such as water for injection, saline solutions (preferably physiological saline), Ringer's solution, solution), isotonic sodium chloride, nonvolatile oils (such as synthetic mono- or di-glycerides that can serve as solvents or suspending media), polyethylene glycol, glycerol, propylene glycol or other solvents; antibacterial agents such as benzyl alcohol or methyl paraben; antioxidants such as ascorbic acid or sodium bisulfite; chelating agents such as ethylenediaminetetraacetic acid; buffers such as acetates, citrates or phosphates; and agents for tonicity adjustment such as sodium chloride or dextrose. Parenteral preparations can be enclosed in ampoules made of glass or plastic, disposable syringes or multi-dose vials. Physiological saline is a preferred adjuvant. Injectable pharmaceutical compositions are preferably sterile. Liquid compositions intended for parenteral or oral administration should contain an amount of an antibody or antigen binding fragment as disclosed herein so that a suitable dosage is obtained. Generally speaking, this amount is at least 0.01% of the antibody or antigen binding fragment in the composition. When intended for oral administration, this amount may vary between 0.1% and about 70% of the weight of the composition. Certain oral pharmaceutical compositions contain between about 4% and about 75% of the antibody or antigen binding fragment. In certain specific embodiments, pharmaceutical compositions and formulations according to the present invention are prepared so that the parenteral dosage unit contains between 0.01 and 10% by weight of the antibody or antigen binding fragment before dilution. The composition may be intended for topical administration, in which case the carrier may suitably comprise a solution, emulsion, ointment or gel base. For example, the base may comprise one or more of: wax, lanolin, polyethylene glycol, beeswax, mineral oil, diluents such as water and alcohol, and emulsifiers and stabilizers. A thickening agent may be present in the composition for topical administration. If intended for transdermal administration, the composition may include a transdermal patch or an iontophoresis device. The pharmaceutical composition may be intended for rectal administration in the form of, for example, a suppository, which will melt in the rectum and release the drug. Compositions for rectal administration may contain an oily base as a suitable non-irritating formulation. Suitable bases include, but are not limited to, lanolin, cocoa butter, and polyethylene glycol. Compositions may include various materials that change the physical form of a solid or liquid dosage unit. For example, a composition may include a material that forms a coating shell around an active ingredient. The material forming the coating shell is generally inert and may be selected from, for example, sugar, wormwood, and other enteric coating agents. Alternatively, the active ingredient may be packaged in a gelatin capsule. Compositions in solid or liquid form may include agents that bind to the antibodies or antigen binding fragments disclosed herein and thereby assist in the delivery of compounds. Suitable agents that may function in this capacity include single or multiple antibodies, one or more proteins, or liposomes. The composition may consist essentially of dosage units that can be administered as an aerosol. The term aerosol is used to denote a variety of systems ranging from those systems of colloidal nature to systems consisting of pressurized packages. Delivery may be by liquefying or compressing a gas or by a suitable pump system for dispensing the active ingredient. Aerosols may be delivered in the form of a single-phase, two-phase, or three-phase system to deliver one or more active ingredients. The delivery of an aerosol includes necessary containers, activators, valves, sub-containers, etc., which together may form a set. A person of ordinary skill in the art may determine the preferred aerosol without undue experimentation. It should be understood that the compositions of the present disclosure also encompass carrier molecules (e.g., lipid nanoparticles, nanoscale delivery platforms, etc.) for polynucleotides as described herein. Pharmaceutical compositions can be prepared by methods well known in the art of pharmaceutical technology. For example, a composition intended for administration by injection can be prepared by combining a composition comprising an antibody, an antigen-binding fragment thereof, or an antibody conjugate as described herein and, as required, one or more of a salt, a buffer, and/or a stabilizer with sterile distilled water to form a solution. A surfactant may be added to promote the formation of a homogeneous solution or suspension. A surfactant is a compound that non-covalently interacts with a peptide composition to promote dissolution or homogeneous suspension of the antibody or its antigen-binding fragment in an aqueous delivery system. In general, appropriate dosages and treatment regimens provide one or more components in an amount sufficient to provide a therapeutic and/or preventive benefit, as described herein, including improved clinical outcomes (e.g., reduced frequency, duration, or severity of diarrhea or related dehydration, or inflammation, or longer disease-free and/or overall survival, or reduced severity of symptoms). For preventive uses, the dosage should be sufficient to Preventing disease, delaying the onset of, or reducing the severity of a disease or condition associated with the disease or condition. The prophylactic benefit of the compositions administered according to the methods described herein can be determined by conducting preclinical (including in vitro and in vivo animal studies) and clinical studies, and analyzing the data obtained therefrom by appropriate statistical, biological, and clinical methods and techniques, all of which are readily practiced by those having ordinary knowledge in the art. The compositions are administered in an effective amount (e.g., to treat SARS-CoV-2 infection), which will vary depending on a variety of factors, including the activity of the specific compound employed; the metabolic stability and duration of action of the compound; the age, weight, general health, sex, and diet of the individual; the mode of administration and time; excretion rate; drug combination; severity of the particular disease or condition; and the therapy the subject is undergoing. In certain embodiments, after administration of therapy according to the formulations and methods of the present disclosure, the test subject will exhibit from about 10% to up to about 99% reduction in one or more symptoms associated with the disease or condition being treated, as compared to a placebo-treated or other appropriate control subject. Generally speaking, the therapeutically effective daily dose of an antibody or antigen-binding fragment is about 0.001 mg/kg (i.e., 0.07 mg) to about 100 mg/kg (i.e., 7.0 g) (for a 70 kg mammal); preferably, the therapeutically effective dose is about 0.01 mg/kg (i.e., 0.7 mg) to about 50 mg/kg (i.e., 3.5 g) (for a 70 kg mammal); more preferably, the therapeutically effective dose is about 1 mg/kg (i.e., 70 mg) to about 25 mg/kg (i.e., 1.75 g) (for a 70 kg mammal). For the polynucleotides, vectors, host cells, and related compositions disclosed herein, the therapeutically effective dose may be different from the therapeutically effective dose of an antibody or antigen-binding fragment. A single intramuscular (IM) administration of an age- and/or weight-appropriate dose of a S2V29-v1.2 antibody or fragment thereof as described herein, particularly S2V29-v1.2-IgG1m17_Lamda or S2V29-v1.2-IgG1m17,1-LS antibody, may be sufficient to treat SARS-CoV-2 infection or have a prophylactic benefit of between three and six months or up to six months. In certain embodiments, the method comprises administering the antibody, antigen-binding fragment, polynucleotide, vector, host cell, or composition to a subject 2, 3, 4, 5, 6, 7, 8, 9, 10 times, or more. In certain embodiments, the method comprises administering an antibody, an AF, or a composition to an individual multiple times, wherein the second or consecutive administration is performed about 6, about 7, about 8, about 9, about 10, about 11, about 12, about 24, about 48, about 74, about 96 hours, or longer after the first or previous administration. In certain embodiments, the method comprises administering an antibody, an AF, a polynucleotide, a vector, a host cell, or a composition at least once before the individual is infected with severe acute respiratory syndrome beta coronavirus. Compositions comprising antibodies, AF, polynucleotides, vectors, host cells, or compositions disclosed herein may also be administered simultaneously with, before, or after the administration of one or more other therapeutic agents. Such combination therapy may include administration of a single pharmaceutical dosage formulation containing a compound of the invention and one or more additional active agents, as well as administration of a composition comprising an antibody or antigen-binding fragment of the present disclosure and each active agent in its own separate dosage formulation. For example, an antibody or antigen-binding fragment thereof as described herein and other active agents may be administered to a patient together in a single oral dosage formulation (such as a tablet or capsule), or each dose may be administered in a separate oral dosage formulation. Similarly, an antibody or antigen-binding fragment thereof as described herein and other active agents may be administered to a patient together in a single parenteral dosage formulation (such as a saline solution or other physiologically acceptable solution), or each dose may be administered in a separate parenteral dosage formulation. In the case of using independent dosage formulations, the composition comprising the antibody or antigen binding fragment and one or more additional active agents can be administered substantially simultaneously, i.e., concurrently, or separately staggered, i.e., sequentially and in any order; combination therapy should be understood to include all such regimens. In certain embodiments, combination therapy is provided, which comprises one or more anti-severe acute respiratory syndrome beta coronavirus antibodies (or one or more nucleic acids, host cells, vectors, or compositions) disclosed herein and one or more anti-inflammatory agents and/or one or more antiviral agents. In specific embodiments, one or more anti-inflammatory agents comprise corticosteroids, such as, for example, dexamethasone, prednisone, etc. In some embodiments, one or more anti-inflammatory agents include an interleukin antagonist, such as, for example, an antibody that binds to IL6 (such as siltuximab), or to IL-6R (such as tocilizumab), or to IL-1β, IL-7, IL-8, IL-9, IL-10, FGF, G-CSF, GM-CSF, IFN-γ, IP-10, MCP-1, MIP-1A, MIP1-B, PDGR, TNF-α, or VEGF. In some embodiments, an anti-inflammatory agent such as leronlimab, ruxolitinib, and/or anakinra is used. In some embodiments, one or more antiviral agents include nucleotide analogs or nucleotide analog prodrugs, such as, for example, remdesivir, sofosbuvir, acyclovir, and zidovudine. In certain embodiments, the antiviral agent includes lopinavir, ritonavir, favipiravir, or any combination thereof. Other anti-inflammatory agents used in the combination therapy of the present disclosure include non-steroidal anti-inflammatory drugs (NSAIDS). It should be understood that in such combination therapy, one or more antibodies (or one or more nucleic acids, host cells, vectors, or compositions) and one or more anti-inflammatory agents and/or one or more antiviral agents can be administered in any order and in any order, or administered together. In some embodiments, the antibodies (or one or more nucleic acids, host cells, vectors, or compositions) are administered to an individual who has previously received one or more anti-inflammatory agents and/or one or more antiviral agents. In some embodiments, the one or more anti-inflammatory agents and/or one or more antiviral agents are administered to an individual who has previously received the antibodies (or one or more nucleic acids, host cells, vectors, or compositions). In certain embodiments, combination therapies are provided that include two or more anti-severe acute respiratory syndrome beta coronavirus antibodies disclosed herein. The method may include administering a first antibody to an individual who has received a second antibody, or may include administering two or more antibodies together. For example, in a particular embodiment, a method is provided that includes administering to an individual (a) a first antibody or antigen-binding fragment when the individual has received a second antibody or antigen-binding fragment; (b) a second antibody or antigen-binding fragment when the individual has received a first antibody or antigen-binding fragment; or (c) a first antibody or antigen-binding fragment, and a second antibody or antigen-binding fragment. In a related aspect, uses of the antibodies, antigen-binding fragments, vectors, host cells, and compositions disclosed herein are provided. The present disclosure further provides a kit comprising one or more of any antibody, antigen binding fragment, polynucleotide, nucleic acid, vector, or other composition disclosed herein. The kit may further include one or more of a container (such as a test tube, vial, or syringe), an activator, a valve, a subcontainer, or instructions for use (such as administration to an individual). In certain embodiments, antibodies, antigen binding fragments, polynucleotides, vectors, host cells, or compositions are provided, which are used in methods for treating severe acute respiratory syndrome beta-coronavirus infection in an individual. In certain embodiments, antibodies, antigen binding fragments, or compositions are provided, which are used in methods for manufacturing or preparing a drug for treating severe acute respiratory syndrome beta-coronavirus infection in an individual. The present disclosure provides the following specific embodiments: Embodiment 1. An antibody, or an antigen-binding fragment thereof, comprising a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (A) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 24, or a functional variant thereof, wherein the functional variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: (iii) the CDRH3 comprises or consists of an amino acid sequence such as SEQ ID NO: 26, or a functional variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence such as SEQ ID NO: 28, or a functional variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence such as SEQ ID NO: 30, or a functional variant thereof, which comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; NO: 29, or a functional variant thereof, the functional variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 30, or a functional variant thereof, the functional variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids, (B) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 32 or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of an amino acid sequence such as SEQ ID NO: 33, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of an amino acid sequence such as SEQ ID NO: 34, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence such as SEQ ID NO: (v) the CDRL2 comprises or consists of an amino acid sequence as described in SEQ ID NO: 39, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of an amino acid sequence as described in SEQ ID NO: 39, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; 40, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids, (C) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 84, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 85, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 86, or a sequence variant thereof NO: 86 or 186, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence as in any one of SEQ ID NO: 88 or 194, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of the following: an amino acid sequence as in any one of SEQ ID NO: 86 or 186, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; 89, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 90, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (D) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 94, 198, or 208, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 95, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 96, 199, 202, or 205, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as described in any one of SEQ ID NOs: 98, 226, 229, 232, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence as described in any one of SEQ ID NOs: 39, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 99, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (e) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 103 or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) said CDRH2 comprising or consisting of: an amino acid sequence such as SEQ ID NO: 85, or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) said CDRH3 comprising or consisting of: an amino acid sequence such as SEQ ID NO: 104, 236, or 239, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as in SEQ ID NO: 106 or 255, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence as in SEQ ID NO: 107, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of an amino acid sequence such as SEQ ID NO: 258, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; or (F) (i) the CDRH1 comprises or consists of an amino acid sequence such as SEQ ID NO: 112, or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) said CDRH2 comprising or consisting of an amino acid sequence as in any one of SEQ ID NOs: 113, 126, 129, 132, 135, 138, 142, 146, 150, 154, 267, or 270, or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) said CDRH3 comprising or consisting of an amino acid sequence as in any one of SEQ ID NOs: 114, 139, 143, 147, 151, or 155, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 116, 273, or 283, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 117, 274, or 287, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence as described in any one of SEQ ID NOs: 118, 122, 158, 275, 280, 284, 288, or 291, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of germline-encoded amino acids, wherein the substitutions are optionally substitutions as described in Table 2 or Table 3, and wherein the antibody or antigen-binding fragment can bind to the surface glycoprotein of severe acute respiratory syndrome beta coronavirus. Specific embodiment 2. An antibody, or an antigen-binding fragment thereof, comprising a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein the CDRH1, CDRH2, and CDRH3 and the CDRL1, CDRL2, and CDRL3 have the following amino acid sequences: (A) SEQ ID NOs: 24 to 26 and 28 to 30, respectively; (B) SEQ ID NOs: 32 to 34 and 38 to 40, respectively; (C) SEQ ID NOs: 84 to 86 or 84, 85 and 186 and 88 to 90 or 194, 89, and 90, respectively; (D) SEQ ID NOs: 94 to 96; 198, 95 and 96; 208, 95 and 96; 94, 95, and 199; 198, 95 and 199; 208, 95, and 199; 94, 95, and 202; 198, 95, and 205; 208, 95, and 199; 205, 95, and 202; or 208, 95, and 205, and 98, 39, and 99; 226, 39, and 99; or 229, 39, and 232; (E) are SEQ ID NOs: 103, 85, and 104; 103, 85, and 236; or 103, 85, and 239, and 106 to 108; 106, 107, and 258; 255, 107, and 108; or 255, 107, or 258; and (F) are SEQ ID NOs: 112 to 114; 112, 126, and 114; 112, 129, and 114; 112, 132, and 114; 112, 135, and 114; 112, 138, and 114; 112, 142, and 114; 112, 146, and 114; 112, 150, and 114; 112, 154, and 114; 112, 267, and 114; 112, 270, and 114; 112, 113, and 139 ; 112, 126, and 139; 112, 129, and 139; 112, 132, and 139; 112, 135, and 139; 112, 138, and 139; 112, 142, and 139; 112, 146, and 139; 112, 150, and 139; 112, 154, and 139; 112, 267, and 139; 112, 270, and 139; 112, 113, and 143; 112, 12 6, and 143; 112, 129, and 143; 112, 132, and 143; 112, 135, and 143; 112, 138, and 143; 112, 142, and 143; 112, 146, and 143; 112, 150, and 143; 112, 154, and 143; 112, 267, and 143; 112, 270, and 143; 112, 113, and 147; 112, 126, and 147; 112, 129, and 147; 112, 132, and 147; 112, 135, and 147; 112, 138, and 147; 112, 142, and 147; 112, 146, and 147; 112, 150, and 147; 112, 154, and 147; 112, 267, and 147; 112, 270, and 147; 112, 113, and 151; 112, 126, and 151; 112, 129 and 151; 112, 132, and 151; 112, 135, and 151; 112, 138, and 151; 112, 142, and 151; 112, 146, and 151; 112, 150, and 151; 112, 154, and 151; 112, 267, and 151; 112, 270, and 151; 112, 113, and 155; 1 12, 126, and 155; 112, 129, and 155; 112, 132, and 155; 112, 135, and 155; 112, 138, and 155; 112, 142, and 155; 112, 146, and 1551; 112, 150, and 155; 112, 154, and 155; 112, 267, and 155; or 112, 270 , and 155; and 116 to 118; 116, 274, and 118; 116, 287, and 118; 116, 117, and 122; 116, 274, and 122; 116, 287, and 122; 116, 117, and 158; 116, 274, and 275; 116, 287, and 275; 116, 117, and 280; 116, 2 74, and 280; 116, 287, and 280; 116, 117, and 284; 116, 274, and 284; 116, 287, and 284; 116, 117, and 288; 116, 274, and 288; 116, 287, and 288; 116, 117, and 291; 116, 274, and 291; 116, 287, and 291 ; 273, 117, and 118; 273, 274, and 118; 273, 287, and 118; 273, 117, and 122; 273, 274, and 122; 273, 287, and 122; 273, 117, and 158; 273, 274, and 275; 273, 287, and 275; 273, 117, and 280; 273, 27 4, and 280; 1273, 287, and 280; 273, 117, and 284; 273, 274, and 284; 273, 287, and 284; 273, 117, and 288; 273, 274, and 288; 273, 287, and 288; 273, 117, and 291; 273, 274, and 291; 273, 287, and 291 ; 283, 117, 118; 283, 274, and 118; 283, 287, and 118; 283, 117, and 122; 283, 274, and 122; 283, 287, and 122; 283, 117, and 158; 283, 274, and 275; 283, 287, and 275; 283, 117, and 280; 283, 274 , and 280; 283, 287, and 280; 283, 117, and 284; 283, 274, and 284; 283, 287, and 284; 283, 117, and 288; 283, 274, and 288; 283, 287, and 288; 283, 117, and 291; 283, 274, and 291; or 283, 287, and 291. Specific embodiment 3. The antibody or antigen-binding fragment of specific embodiment 1 or 2, wherein the SARS beta coronavirus is a clade 1b SARS beta coronavirus. Embodiment 4. The antibody or antigen binding fragment of Embodiment 3, wherein the severe acute respiratory syndrome beta coronavirus is SARS-CoV-2 WT, SARS-CoV-2 BA.1, RATG13, PANG/GD, or PAND/GX. Embodiment 5. The antibody or antigen binding fragment of any one of Embodiments 1 to 4, wherein the antibody or antigen binding fragment is capable of binding to the surface glycoprotein when the surface glycoprotein is expressed on the cell surface of the host cell and/or contained on the virus particle. Embodiment 6. The antibody or antigen binding fragment of any one of Embodiments 1 to 5, which is capable of binding to the surface glycoprotein from two or more (e.g., two, three, four, five, or more) severe acute respiratory syndrome beta coronaviruses. Specific embodiment 7. An antibody or antigen binding fragment as described in any one of Specific Embodiments 1 to 6, which is capable of neutralizing an infection caused by one or more severe acute respiratory syndrome beta coronaviruses in an in vitro model of infection and/or in an in vivo animal model of infection and/or in humans. Specific embodiment 8. An antibody or antigen binding fragment as described in any one of Specific Embodiments 1 to 7, which is capable of neutralizing an infection caused by two or more severe acute respiratory syndrome beta coronaviruses in an in vitro model of infection and/or in an in vivo animal model of infection and/or in humans. Specific embodiment 9. The antibody or antigen-binding fragment of any one of embodiments 1 to 8, wherein the VH and VL each comprise or consist of an amino acid sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the amino acid sequence described below; or each comprise or consist of the amino acid sequence described below: (I) 1) SEQ ID NOs: 23 and 27; 2) SEQ ID NOs: 23 and 37; 3) SEQ ID NOs: 31 and 27; 4) SEQ ID NOs: 31 and 37; 5) SEQ ID NOs: 35 and 27; 6) SEQ ID NOs: 35 and 37; 7) SEQ ID NOs: 36 and 27; 8) SEQ ID NOs: 19) SEQ ID NO: 185 and 87; 20) SEQ ID NO: 185 and 87; 21) SEQ ID NO: 185 and 193; 22) SEQ ID NO: 190 and 87; 23) SEQ ID NO: 190 and 193; 24) SEQ ID NO: 93 and 97; 25) SEQ ID NO: 93 and 225; 26) SEQ ID NO: 93 and 228; 27) SEQ ID NO: 93 and 231; 28) SEQ ID NO: 197 and 97; 29) SEQ ID NO: 197 and 225; 30) SEQ ID NO: 197 and 228; 31) SEQ ID NO: 197 and 231; 32) SEQ ID NO: 201 and 97; 33) SEQ ID NO: 201 and 225; 34) SEQ ID NO: 201 and 228; 35) SEQ ID NO: 201 and 231; 36) SEQ ID NO: 204 and 97; 37) SEQ ID NO: 204 and 225; 38) SEQ ID 49) SEQ ID NO: 212 and 225; 50) SEQ ID NO: 212 and 228; 51) SEQ ID NO: 212 and 231; 52) SEQ ID NO: 214 and 97; 53) SEQ ID NO: 214 and 97; 54) SEQ ID NO: 216 and 97; 55) SEQ ID NO: 216 and 97; 56) SEQ ID NO: 216 and 97; 57) SEQ ID NO: 216 and 97; 58) SEQ ID NO: 216 and 97; 59) SEQ ID NO: 216 and 97; 60) SEQ ID NO: 216 and 97; 61) SEQ ID NO: 216 and 97; 62) SEQ ID NO: 216 and 97; 63) SEQ ID NO: 216 and 97; 64) SEQ ID NO: 220 and 97; 65) SEQ ID NO: 220 and 225; 66) SEQ ID NO: 220 and 228; 67) SEQ ID NO: 220 and 231; 68) SEQ ID NO: 220 and 97; 69) SEQ ID NO: 220 and 231; 70) SEQ ID NO: 220 and 231; 71) SEQ ID NO: 220 and 231; 72) SEQ ID NO: 220 and 231; 73) SEQ ID NO: 220 and 231; 74) SEQ ID NO: 221 and 97; 75) SEQ ID NO: 221 and 231; 76) SEQ ID NO: 221 and 231; 77) SEQ ID NO: 221 and 231; 78) SEQ ID NO: 221 and 231; 79) SEQ ID NO: 222 and 97; 80) SEQ ID NO: 222 and 231; 81) SEQ ID NO: 222 and 97; 82) SEQ ID NO: 222 and 231; 83) SEQ ID NO: 222 and 231; 84) SEQ ID NO: 223 54) SEQ ID NO: 102 and 257; 75) SEQ ID NO: 102 and 260; 76) SEQ ID NO: 235 and 105; 77) SEQ ID NO: 235 and 254; 78) SEQ ID NO: 235 and 257; 79) SEQ ID NO: 235 and 260; 80) SEQ ID NO: 238 and 105; 81) SEQ ID NO: 238 and 254; 82) SEQ ID NO: 92) SEQ ID NO: 245 and 105; 93) SEQ ID NO: 245 and 254; 94) SEQ ID NO: 245 and 257; 95) SEQ ID NO: 245 and 260; 96) SEQ ID NO: 247 and 105; 97) SEQ ID NO: 247 and 105; 98) SEQ ID NO: 247 and 105; 99) SEQ ID NO: 248 and 254; 100) SEQ ID NO: 248 and 257; 101) SEQ ID NO: 248 and 254; 102) SEQ ID NO: 248 and 254; 103) SEQ ID NO: 248 and 254; 104) SEQ ID NO: 248 and 257; 105) SEQ ID NO: 248 and 254; 106) SEQ ID NO: 248 and 257; 107) SEQ ID NO: 248 and 254; 108) SEQ ID NO: 248 and 254; 109) SEQ ID NO: 248 and 257 SEQ ID NOs: 247 and 254; 98) SEQ ID NOs: 247 and 257; 99) SEQ ID NOs: 247 and 260; 100) SEQ ID NOs: 249 and 105; 101) SEQ ID NOs: 249 and 254; 102) SEQ ID NOs: 249 and 257; 103) SEQ ID NOs: 249 and 260; 104) SEQ ID NOs: 251 and 105; 105) SEQ ID NOs: 251 and 254; 106) SEQ ID NOs: 251 and 257; 107) SEQ ID NOs: 251 and 260; 108) SEQ ID NOs: 111 and 115; 109) SEQ ID NOs: 111 and 121; 110) SEQ ID NOs: 111 and 157; 111) SEQ ID NO: 111 and 272; 112) SEQ ID NO: 111 and 277; 113) SEQ ID NO: 111 and 279; 114) SEQ ID NO: 111 and 282; 115) SEQ ID NO: 111 and 286; 116) SEQ ID NO: 111 and 290; 117) SEQ ID NO: 125 and 115; 118) SEQ ID NO: 125 and 121; 119) SEQ ID NO: 125 and 157; 120) SEQ ID NO: 125 and 272; 121) SEQ ID NO: 125 and 277; 122) SEQ ID NO: 125 and 279; 123) SEQ ID NO: 125 and 282; 124) SEQ ID NO: 134) SEQ ID NO: 131 and 115; 135) SEQ ID NO: 131 and 157; 136) SEQ ID NO: 131 and 272; 137) SEQ ID NO: 131 and 279; 138) SEQ ID NO: 132 and 279; 139) SEQ ID NO: 133 and 115; 140) SEQ ID NO: 134 and 115; 141) SEQ ID NO: 134 and 115; 142) SEQ ID NO: 134 and 115; 143) SEQ ID NO: 134 and 115; 144) SEQ ID NO: 134 and 115; 145) SEQ ID NO: 134 and 115; 146) SEQ ID NO: 134 and 115 147) SEQ ID NO: 134 and 279; 148) SEQ ID NO: 134 and 282; 149) SEQ ID NO: 134 and 286; 150) SEQ ID NO: 134 and 290; 151) SEQ ID NO: 134 and 115; 152) SEQ ID NO: 134 and 121; 153) SEQ ID NO: 134 and 121; 154) SEQ ID NO: 134 and 157; 155) SEQ ID NO: 134 and 272; 156) SEQ ID NO: 134 and 277; 157) SEQ ID NO: 134 and 279; 158) SEQ ID NO: 134 and 282; 159) SEQ ID NO: 134 and 286; 160) SEQ ID NO: 134 and 290; 161) SEQ ID NO: 134 and 291; 154) SEQ ID NO: 137 and 272; 155) SEQ ID NO: 137 and 277; 156) SEQ ID NO: 137 and 279; 157) SEQ ID NO: 137 and 282; 158) SEQ ID NO: 137 and 286; 159) SEQ ID NO: 137 and 290; 160) SEQ ID NO: 141 and 115; 161) SEQ ID NO: 141 and 121; 162) SEQ ID NO: 141 and 157; 162) SEQ ID NO: 141 and 272; 162) SEQ ID NO: 141 and 277; 163) SEQ ID NO: 141 and 279; 164) SEQ ID NO: 141 and 282; 165) SEQ ID NO: 141 and 286; 166) SEQ ID NO: 141 and 290; 167) SEQ ID NO: 145 and 115; 168) SEQ ID NO: 145 and 121; 169) SEQ ID NO: 145 and 157; 170) SEQ ID NO: 145 and 272; 171) SEQ ID NO: 145 and 277; 172) SEQ ID NO: 145 and 279; 173) SEQ ID NO: 145 and 282; 174) SEQ ID NO: 145 and 282; 175) SEQ ID NO: 145 and 286; 176) SEQ ID NO: 177) SEQ ID NO: 149 and 115; 178) SEQ ID NO: 149 and 121; 179) SEQ ID NO: 149 and 157; 180) SEQ ID NO: 149 and 272; 181) SEQ ID NO: 149 and 277; 182) SEQ ID NO: 149 and 279; and 183) SEQ ID NO: 149 and 282; 184) SEQ ID NO: 149 and 286; 185) SEQ ID NO: 149 and 290; 186) SEQ ID NO: 153 and 115; 187) SEQ ID NO: 153 and 121; 188) SEQ ID NO: 153 and 157; 189) SEQ ID NO: 153 and 272; 190) SEQ ID 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 264 and 115; 196) SEQ ID NO: 264 and 121; 197) SEQ ID NO: 264 and 157; 198) SEQ ID NO: 264 and 272; 199) SEQ ID NO: 264 and 277; 200) SEQ ID NO: 264 and 279; 201) SEQ ID NO: 264 and 282; 202) SEQ ID NO: 264 and 286; 203) SEQ ID NO: 264 and 290; 204) SEQ 205) SEQ ID NO: 266 and 121; 206) SEQ ID NO: 266 and 157; 207) SEQ ID NO: 266 and 272; 208) SEQ ID NO: 266 and 277; 209) SEQ ID NO: 266 and 279; 210) SEQ ID NO: 266 and 282; 211) SEQ ID NO: 266 and 286; 212) SEQ ID NO: 266 and 290; 213) SEQ ID NO: 269 and 115; 214) SEQ ID NO: 269 and 121; 215) SEQ ID NO: 269 and 157; 216) SEQ ID NO: 269 and 157; 217) SEQ ID NO: 269 and 272; 218) SEQ ID NOs: 269 and 277; 219) SEQ ID NOs: 269 and 279; 219) SEQ ID NOs: 269 and 282; 220) SEQ ID NOs: 269 and 286; or 221) SEQ ID NOs: 269 and 290, or (II) any other combination of the same antibody types as described in Tables 2 and 3. Specific embodiment 10. The antibody or antigen-binding fragment of any one of embodiments 1 to 9, wherein the VH and the VL respectively comprise or consist of the amino acid sequences described below: 1) SEQ ID NOs: 23 and 27; 2) SEQ ID NOs: 23 and 37; 3) SEQ ID NOs: 31 and 27; 4) SEQ ID NOs: 31 and 37; 5) SEQ ID NOs: 35 and 27; 6) SEQ ID NOs: 35 and 37; 7) SEQ ID NOs: 36 and 27; 8) SEQ ID NOs: 36 and 37; 9) SEQ ID NOs: 43 and 27; 10) SEQ ID NOs: 43 and 37; 11) SEQ ID NOs: 83 and 87; 12) SEQ ID NOs: 83 and 193; 13) SEQ ID NOs: 179 and 87; 14) SEQ ID NO: 179 and 193; 15) SEQ ID NO: 181 and 87; 16) SEQ ID NO: 181 and 193; 17) SEQ ID NO: 183 and 87; 18) SEQ ID NO: 183 and 193; 18) SEQ ID NO: 185 and 87; 19) SEQ ID NO: 185 and 193; 20) SEQ ID NO: 188 and 87; 21) SEQ ID NO: 188 and 193; 22) SEQ ID NO: 190 and 87; 23) SEQ ID NO: 190 and 193; 24) SEQ ID NO: 93 and 97; 25) SEQ ID NO: 93 and 225; 26) SEQ ID NO: 93 and 228; 27) SEQ ID NO: 93 and 231; 28) SEQ ID NO: 41) SEQ ID NO: 207 and 225; 42) SEQ ID NO: 207 and 228; 43) SEQ ID NO: 54) SEQ ID NO: 214 and 228; 55) SEQ ID NO: 214 and 231; 56) SEQ ID NO: 216 and 97; 57) SEQ ID NO: 216 and 225; 58) SEQ ID NO: 69) SEQ ID NO: 222 and 225; 70) SEQ ID NO: 222 and 228; 71) SEQ ID NO: 222 and 231; 72) SEQ ID NO: 102 and 105; 73) SEQ ID NO: 106 and 107; 74) SEQ ID NO: 108 and 109; 75) SEQ ID NO: 112 and 113; 76) SEQ ID NO: 114 and 115; 77) SEQ ID NO: 115 and 116; 78) SEQ ID NO: 116 and 228; 79) SEQ ID NO: 216 and 231; 80) SEQ ID NO: 218 and 97; 81) SEQ ID NO: 218 and 225; 82) SEQ ID NO: 218 and 228; 83) SEQ ID NO: 218 and 231; 84) SEQ ID NO: 220 and 97; 85) SEQ ID NO: 220 and 225; 86) SEQ ID NO: 220 and 228; 87) SEQ ID NO: 220 and 231; 88) SEQ ID NO: 222 and 97; 7) SEQ ID NO: 235 and 260; 80) SEQ ID NO: 238 and 105; 81) SEQ ID NO: 238 and 254; 82) SEQ ID NO: 238 and 257; 83) SEQ ID NO: 238 and 260; 84) SEQ ID NO: 241 and 105; 85) SEQ ID NO: 241 and 254; 86) SEQ ID NO: 241 and 257; 87) SEQ ID NO: 97) SEQ ID NO: 247 and 254; 98) SEQ ID NO: 247 and 257; 99) SEQ ID NO: 247 and 260; 100) SEQ ID NO: 249 and 105; 101) SEQ ID NO: 10) SEQ ID NO: 111 and 121; 110) SEQ ID NO: 111 and 157; 111) SEQ ID NO: 111 and 272; 112) SEQ ID NO: 111 and 277; 113) SEQ ID NO: 111 and 279; 114) SEQ ID NO: 111 and 282; 115) SEQ ID NO: 111 and 282; 125) SEQ ID NO: 125 and 290; 126) SEQ ID NO: 128 and 115; 127) SEQ ID NO: 128 and 121; 128) SEQ ID NO: 128 and 157; 129) SEQ ID NO: 129 and 272; 130) SEQ ID NO: 129 and 277; 131) SEQ ID NO: 129 and 279; 132) SEQ ID NO: 129 and 282; 133) SEQ ID NO: 129 and 286; 134) SEQ ID NO: 129 and 290; 135) SEQ ID NO: 128 and 115; 136) SEQ ID NO: 128 and 121; 137) SEQ ID NO: 128 and 157; 138) SEQ ID NO: 128 and 157; 139) SEQ ID NO: 129 and 272; 140) SEQ ID NO: 129 and 277; 141) SEQ ID NO: 129 and 279; 142) SEQ ID NO: 129 and 282; 143) SEQ ID NO: 129 and 286; 144) SEQ ID NO: 129 and 290; 145) SEQ ID NO: 129 and 291; 146) SEQ ID NO: 12 136) SEQ ID NO: 131 and 272; 137) SEQ ID NO: 131 and 277; 138) SEQ ID NO: 131 and 279; 139) SEQ ID NO: 131 and 282; 140) SEQ ID NO: 131 and 286; 141) SEQ ID NO: 131 and 290; 142) SEQ ID NO: 134 and 115; 143) SEQ ID NO: 134 and 121; 144) SEQ ID NO: 134 and 157; 145) SEQ ID NO: 134 and 272; 146) SEQ ID NO: 134 and 277; 147) SEQ ID NO: 134 and 279; 148) SEQ ID NO: 134 and 282; 149) SEQ ID NO: 134 and 286; 150) SEQ ID NO: 134 and 290; 151) SEQ ID NO: 137 and 115; 152) SEQ ID NO: 137 and 121; 153) SEQ ID NO: 137 and 157; 154) SEQ ID NO: 137 and 272; 155) SEQ ID NO: 156) SEQ ID NO: 137 and 279; 157) SEQ ID NO: 137 and 282; 158) SEQ ID NO: 137 and 286; 159) SEQ ID NO: 137 and 290; 160) SEQ ID NO: 141 and 115; 161) SEQ ID NO: 141 and 121; 162) SEQ ID NO: 141 and 157; 162) SEQ ID NO: 141 and 272; 162) SEQ ID NO: 141 and 277; 163) SEQ ID NO: 141 and 279; 164) SEQ ID NO: 141 and 282; 165) SEQ ID NO: 141 and 286; 166) SEQ ID NO: 141 290; 167) SEQ ID NO: 141 176) SEQ ID NO: 145 and 290; 177) SEQ ID NO: 149 and 115; 178) SEQ ID NO: 149 and 121; 179) SEQ ID NO: 149 and 157; 170) SEQ ID NO: 149 and 272; 171) SEQ ID NO: 149 and 277; 172) SEQ ID NO: 149 and 279; 173) SEQ ID NO: 149 and 282; 174) SEQ ID NO: 149 and 282; 175) SEQ ID NO: 149 and 286; 176) SEQ ID NO: 149 and 290; 177) SEQ ID NO: 149 and 115; 178) SEQ ID NO: 149 and 121; 179) SEQ ID NO: 149 and 157; 180) SEQ ID NO: 149 and 272; 181) SEQ ID NO: 149 and 277; 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 153 and 115; 187) SEQ ID NO: 153 and 121; 188) SEQ ID NO: 153 and 157; 189) SEQ ID NO: 153 and 272; 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 264 and 115; 196) SEQ ID NO: 264 and 121; 197) SEQ ID NO: 264 and 157; 198) SEQ ID NO: 264 and 272; 199) SEQ ID NO: 264 and 277; 200) SEQ ID NO: 264 and 279; 201) SEQ ID NO: 264 and 282; 202) SEQ ID NO: 264 and 286; 203) SEQ ID NO: 264 and 290; 204) SEQ ID NO: 266 and 115; 205) SEQ ID NO: 266 and 121; 206) SEQ ID NO: 266 and 157; 207) SEQ ID NO: 266 and 272; 208) SEQ ID NO: 269 and 272; 218) SEQ ID NO: 269 and 277; 219) SEQ ID NO: 269 and 279; 220) SEQ ID NO: 269 and 282; 221) SEQ ID NO: 269 and 286; 222) SEQ ID NO: 269 and 290; 223) SEQ ID NO: 269 and 115; 224) SEQ ID NO: 269 and 121; 225) SEQ ID NO: 269 and 157; 226) SEQ ID NO: 269 and 157; 227) SEQ ID NO: 269 and 272; 228) SEQ ID NO: 269 and 277; 229) SEQ ID NO: 269 and 279; 230) SEQ ID NO: 269 and 282; 231) SEQ ID NO: 269 and 286; or 232) SEQ ID NO: 269 and 286 NO: 269 and 290. Specific embodiment 11. The antibody or antigen-binding fragment of any one of embodiments 1 to 10, wherein: i) the VH and the VL comprise or consist of an amino acid sequence having at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity with the amino acid sequence depicted in SEQ ID NO: 111 and 157, respectively, or comprise or consist of the amino acids depicted in SEQ ID NO: 111 and 157, respectively. ii) the VH and the VL comprise the amino acid sequences described in SEQ ID NOs: 111 and 157, respectively, or consist of the amino acids described in SEQ ID NOs: 111 and 157; iii) the VH of i) or ii) comprises CDRH1, CDRH2, and CDRH3, and the VL of i) or ii) comprises CDRL1, CDRL2, and CDRL3, which have amino acid sequences determined by any VH and VL numbering scheme; iii) the VH comprises CDRH1, CDRH2, and CDRH3, and the VL comprises CDRL1, CDRL2, and CDRL3, which have amino acid sequences as described in SEQ ID NOs: 112 to 114, 116, 117, and 158, respectively; iv) the antibody or antigen-binding fragment comprises any one of i) to iv) and a polypeptide having a polypeptide as described in SEQ ID NO: 44 to 80 and a light chain constant region having a sequence such as SEQ ID NO: 292; v) the antibody or antigen-binding fragment comprises a heavy chain having a sequence such as SEQ ID NO: 293 and a light chain having a sequence such as SEQ ID NO: 294; or vi) the antibody or antigen-binding fragment comprises a heavy chain having a sequence such as SEQ ID NO: 295 and a light chain having a sequence such as SEQ ID NO: 296. Embodiment 12. The antibody or antigen-binding fragment of any one of Embodiments 1 to 11, wherein: (i) recognizes epitopes in the spike proteins of two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses; (ii) is capable of blocking the interaction between the spike proteins of two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses and one or more cell surface receptors corresponding thereto, wherein, as required, The cell surface receptor comprises human ACE2; (iii) recognizes an epitope retained in the spike protein of two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses; (iv) is cross-reactive against two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses, optionally including one or more clade 1b severe acute respiratory syndrome beta coronaviruses; or (v) any combination of (i) to (iv). Specific embodiment 13. The antibody or antigen-binding fragment of any one of embodiments 1 to 12, which is of IgG, IgA, IgM, IgE, or IgD isotype. Embodiment 14. The antibody or antigen-binding fragment of Embodiment 13, which is selected from the IgG isotype of IgG1, IgG2, IgG3, and IgG4, and preferably is the IgG1 isotype. Embodiment 15. The antibody or antigen-binding fragment of any one of Embodiments 1 to 14, which is human, humanized, or chimeric. Embodiment 16. The antibody or antigen-binding fragment of any one of Embodiments 1 to 15, wherein the antibody or the antigen-binding fragment comprises a human antibody, a monoclonal antibody, a purified antibody, a single-chain antibody, Fab, Fab', F(ab')2, Fv, scFv, or scFab. Embodiment 17. The antibody or antigen-binding fragment of Embodiment 16, wherein the scFv comprises more than one VH domain and more than one VL domain. Embodiment 18. The antibody or antigen-binding fragment of any one of Embodiments 1 to 17, wherein the antibody or antigen-binding fragment is a multispecific antibody or antigen-binding fragment. Embodiment 19. The antibody or antigen-binding fragment of Embodiment 18, wherein the antibody or antigen-binding fragment is a bispecific antibody or antigen-binding fragment. Embodiment 20. The antibody or antigen-binding fragment of embodiment 19, comprising: a first VH and a first VL; and a second VH and a second VL, wherein the first VH and VL comprise i) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with the amino acid sequence described in SEQ ID NO: 23 and 27, respectively; ii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with the amino acid sequence described in SEQ ID NO: The amino acid sequence of NO. has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 31, 35, 36, or 43 and 37, respectively; 14 and 15, respectively; 16 and 17, respectively; 18 and 19, respectively; 20 and 21, respectively; 20 and 22, respectively; iii) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 83, 179, 181, 183, 185, 188, or 190 and any one of 87 or 193; iv) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and any one of 97, 225, 228, or 231; v) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 102, 235, 238, 241, 243, 245, 247, 249, or 251 and any one of 105, 254, 257, or 260; or vi) with the following SEQ ID NO. The amino acid sequence described has at least 85% (i.e. 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with an amino acid sequence: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of 115, 121, 157, 272, 277, 279, 282, 286, or 290; and wherein the second VH and VL comprise i) respectively with SEQ ID NO: 23 and 27 have at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs.; ii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs.: 31, 35, 36, or 43, respectively, and 37; 14 and 15, respectively; 16 and 17, respectively; 18 and 19, respectively; 20 and 21, respectively; 20 and 22, respectively; iii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs. NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 83, 179, 181, 183, 185, 188, or 190 and any one of 87 or 193; iv) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and any one of 97, 225, 228, or 231; v) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 102, 235, 238, 241, 243, 245, 247, 249, or 251 and any one of 105, 254, 257, or 260; or vi) with the following SEQ ID NO. has an amino acid sequence with at least 85% (i.e. 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity: any one of 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of 115, 121, 157, 272, 277, 279, 282, 286, or 290, respectively; wherein the first VH and the second VL are different from the second VH and VL, and wherein the first VH and the first VL together form a first antigen-binding site, and wherein the second VH and the second VL together form a second antigen-binding site. Embodiment 21. The antibody or antigen-binding fragment of any one of Embodiments 1 to 20, wherein the antibody or antigen-binding fragment comprises an Fc polypeptide or a fragment thereof. Embodiment 22. The antibody or antigen-binding fragment of embodiment 21, wherein the Fc polypeptide or fragment thereof comprises: (i) a mutation that enhances binding to FcRn, as compared to a reference Fc polypeptide not comprising the mutation; (ii) a mutation that enhances binding to FcγR, as compared to a reference Fc polypeptide not comprising the mutation; (iii) a mutation that enhances binding to human FcγRIIa and/or reduces binding to human FcγRIIb, as compared to a reference Fc polypeptide not comprising the mutation; and/or (iv) a mutation that enhances binding to human C1q, as compared to a reference Fc polypeptide not comprising the mutation. Embodiment 23. The antibody or antigen-binding fragment of embodiment 22, wherein the Fc polypeptide comprises the substitution mutations M428L/N434S, M428L/N434A, G236A/A330L/I332E/M428L/N434S, or G236A/A330L/I332E/M428L/N434A, wherein, optionally, the antibody or antigen-binding fragment is of IgG1 isotype and comprises or consists of an Fc polypeptide or a fragment thereof, the Fc polypeptide or a fragment thereof comprising or consisting of: 44 to 80 having at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity, optionally other than naturally occurring variants thereof; or the Fc polypeptide or fragment thereof comprises or consists of the amino acid sequence set forth in SEQ ID NOs: 52 to 80. Specific embodiment 24. An isolated polynucleotide encoding the antibody or antigen-binding fragment of any one of Specific embodiments 1 to 23. Specific embodiment 25. The polynucleotide of Specific embodiment 24, wherein the polynucleotide comprises or consists of: and SEQ ID NO: 81, 82, 91, 92, 100, 101, 109, 110, 119, 120, 123, 127, 130, 133, 136, 140, 144, 148, 152, 156, 159, 180, 182, 184, 187, 189, 191, 192, 195, 196, 200, 203, 206, 209, 211, 213, 215, 217, 219, 221, 223, 224, 227, 230, 233 , 234, 237, 240, 242, 244, 246, 248, 250, 252, 253, 256, 259, 261, 262, 263, 265, 268, 271, 276, 278, 281, 285, or 289. A nucleic acid sequence having at least 85% (i.e., 85%, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100%) identity to the nucleic acid sequence of one or more of Specific Embodiment 24 or Specific Embodiment 25. Specific Embodiment 26. A polynucleotide as in Specific Embodiment 24 or Specific Embodiment 25, wherein the polynucleotide comprises deoxyribonucleic acid (DNA) or ribonucleic acid (RNA), wherein the RNA optionally comprises a messaging RNA (mRNA). Embodiment 27. The polynucleotide of any one of Embodiments 24 to 26, which is codon-optimized for expression in a host cell. Embodiment 28. A recombinant vector comprising the polynucleotide of any one of Embodiments 24 to 27. Embodiment 29. A host cell comprising the polynucleotide of any one of Embodiments 24 to 27 and/or the vector of Embodiment 28, wherein the polynucleotide is heterologous to the host cell. Embodiment 30. A human B cell comprising the polynucleotide of any one of Embodiments 24 to 27 and/or the vector of Embodiment 28, wherein the polynucleotide is heterologous to the human B cell and/or wherein the human B cell is immortalized. Embodiment 31. A composition comprising: (i) an antibody or antigen-binding fragment as described in any one of Embodiments 1 to 23; (ii) a polynucleotide as described in any one of Embodiments 24 to 27; (iii) a recombinant vector as described in Embodiment 28; (iv) a host cell as described in Embodiment 29; and/or (v) a human B cell as described in Embodiment 30, and a pharmaceutically acceptable excipient, carrier, or diluent. Embodiment 32. The composition of embodiment 31, comprising two or more antibodies or antigen-binding fragments, wherein the first antibody or antigen-binding fragment and the second antibody or antigen-binding fragment respectively comprise, or the multispecific antibody or antigen-binding fragment comprises CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3, and optionally VH and VL, which are according to: (i) any S3A (ii) any S3A3 antibody and sotorovimab; (iii) any S3A3 antibody and S2K146; (iv) any S3A3 antibody and S2X259; (v) any S3A3 antibody and any S2X324 antibody; (vi) any S3A3 antibody and S309; (vii) any S3A19 antibody and sotorovimab; vii) any S3A19 antibody and S2K146; (viii) any S3A19 antibody and S2X259; (ix) any S3A19 antibody and any S2X324 antibody; (x) any S3A19 antibody and S309; (xi) any S3I2 antibody and any S3A3 antibody; (xii) any S3I2 antibody and any S3A19 antibody; (xiii) any S3I2 antibody and Sotovemab; (xiv) any S3I2 antibody and S2K146; (xv) any S3I2 antibody and S2X259; (xvi) any S3I2 antibody and any S2X324 antibody; (xvii) any S3I2 antibody and S309; (xviii) any S3I2 antibody and any S3O13 antibody; (xix) any S3I2 antibody and any S3L17 antibody; (xx) any S (xxi) any S3O13 antibody and any S3A3 antibody; (xxii) any S3O13 antibody and sotoviromab; (xxiii) any S3O13 antibody and S2K146; (xxiv) any S3O13 antibody and S2X259; (xxv) any S3O13 antibody and any S2X324 antibody; (xxvi) any S3O1 3 antibody and S309; (xxvii) any S3O13 antibody and any S3L17 antibody; (xxviii) any S3L17 antibody and any S3A3 antibody; (xxix) any S3L17 antibody and any S3A19 antibody; (xxx) any S3L17 antibody and sotoviromab; (xxxi) any S3L17 antibody and S2K146; (xxxii) any S3L17 antibody and S2X259; (xxxiii) any S3L17 antibody and any S2X324 antibody; (xxxiv) any S3L17 antibody and S309; (xxxv) any S2V29 antibody and any S3A3 antibody; (xxxvi) any S2V29 antibody and any S3A19 antibody; (xxxvii) any S2V29 antibody and sotoviromab; (xxxviii) any S 2V29 antibody and S2K146; (xxxix) any S2V29 antibody and S2X259; (xl) any S2V29 antibody and any S2X324 antibody; (xli) any S2V29 antibody and S309; (lxlii) any S2V29 antibody and any S3L17 antibody; and (xliii) any S2V29 antibody and any S3O13 antibody, or any antigen-binding fragment thereof. Specific embodiment 33. The composition of specific embodiment 31, wherein the first antibody or antigen-binding fragment comprises S3L17 antibody or antigen-binding fragment and the second antibody or antigen-binding fragment comprises S2V29 antibody. Embodiment 34. A composition as in embodiment 33, wherein the first antibody or antigen-binding fragment comprises the following CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences: such as SEQ ID NO: 103, 85, and, 104; 103, 85, and 236; or 103, 85, and 239, and 106 to 108; 106, 107, and 258; 255, 107, and 108; or 255, 107, or 258, and the second antibody or antigen-binding fragment comprises the following CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 amino acid sequences: such as SEQ ID NO: 112 to 114; 112, 126, and 114; 112, 129 and 114; 112, 132, and 114; 112, 135, and 114; 112, 138, and 114; 112, 142, and 114; 112, 146, and 114; 112, 150, and 114; 112, 154, and 114; 112, 267, and 114; 112, 270, and 114; 112, 113, and 139; 112, 126, and 139; 112, 129 and 139; 112, 132, and 139; 112, 135, and 139; 112, 138, and 139; 112, 142, and 139; 112, 146, and 139; 112, 150, and 139; 112, 154, and 139; 112, 267, and 139; 112, 270, and 139; 112, 113, and 143; 112, 126, and 143; 112, 129, and 143; 112, 132, and 143; 112, 135, and 143; 112, 138, and 143; 112, 142, and 143; 112, 146, and 143; 112, 150, and 143; 112, 154, and 143; 112, 267, and 143; 112, 270, and 143; 112, 113, and 147; 112, 126, and 147; 112, 129, and 147; 112, 132, and 147; 112, 135, and 147; 112, 138, and 147; 112, 142, and 147; 112, 146, and 147; 112, 150, and 1 47; 112, 154, and 147; 112, 267, and 147; 112, 270, and 147; 112, 113, and 151; 112, 126, and 151; 112, 129, and 151; 112, 132, and 151; 112, 135, and 151; 112, 138, and 151; 112, 142, and 151; 112, 146, and 151; 112, 150, and 151; 112, 154, and 151; 112, 267, and 151; 112, 270, and 15 1; 112, 113, and 155; 112, 126, and 155; 112, 129, and 155; 112, 132, and 155; 112, 135, and 155; 112, 138, and 155; 112, 142, and 155; 112, 146, and 1551; 112, 150, and 155; 112, 154, and 155; 112, 267, and 155; or 112, 270, and 155; and 116 to 118; 116, 274, and 118; 116, 287, and 118; 1 16, 117, and 122; 116, 274, and 122; 116, 287, and 122; 116, 117, and 158; 116, 274, and 275; 116, 287, and 275; 116, 117, and 280; 116, 274, and 280; 116, 287, and 280; 116, 117, and 284; 116, 274, and 284; 116, 287, and 284; 116, 117, and 288; 116, 274, and 288; 116, 287, and 288; 16, 117, and 291; 116, 274, and 291; 116, 287, and 291; 273, 117, and 118; 273, 274, and 118; 273, 287, and 118; 273, 117, and 122; 273, 274, and 122; 273, 287, and 122; 273, 117, and 158; 273, 274, and 275; 273, 287, and 275; 273, 117, and 280; 273, 274, and 280; 1273, 287, and 280; 273, 117, and 284; 273, 274, and 284; 273, 287, and 284; 273, 117, and 288; 273, 274, and 288; 273, 287, and 288; 273, 117, and 291; 273, 274, and 291; 273, 287, and 291; 283, 117, 118; 283, 274, and 118; 283, 287, and 118; 283, 117, and 122; 283, 274, and 122; 283, 287, and 122; 2 83, 117, and 158; 283, 274, and 275; 283, 287, and 275; 283, 117, and 280; 283, 274, and 280; 283, 287, and 280; 283, 117, and 284; 283, 274, and 284; 283, 287, and 284; 283, 117, and 288; 283, 274, and 288; 283, 287, and 288; 283, 117, and 291; 283, 274, and 291; or 283, 287, and 291. Specific Example 35. The composition of embodiment 33, wherein the first antibody or antigen-binding fragment comprises a heavy chain variable domain (VH) and a light chain variable domain (VL), the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 103 or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of the substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 85, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence as any one of SEQ ID NO: 104, 236, or 239, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence as any one of SEQ ID NO: 106 or 255, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence such as SEQ ID NO: 107, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of an amino acid sequence such as SEQ ID NO: 108 or 258, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of the substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids, and wherein the second antibody or antigen-binding fragment comprises a heavy chain variable domain (VH) and a light chain variable domain (VL), the heavy chain variable domain comprising CDRH1, CDRH2, and CDRH3, the light chain variable domain comprising CDRL1, CDRL2, and CDRL3, wherein: (i) the CDRH1 comprises or consists of: as shown in SEQ ID NO: 112, or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) said CDRH2 comprising or consisting of an amino acid sequence as in any one of SEQ ID NOs: 113, 126, 129, 132, 135, 138, 142, 146, 150, 154, 267, or 270, or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) said CDRH3 comprising or consisting of an amino acid sequence as in any one of SEQ ID NOs: 114, 139, 143, 147, 151, or 155, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 116, 273, or 283, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence as any one of SEQ ID NO: or (vi) the CDRL3 comprises or consists of an amino acid sequence of any one of SEQ ID NOs: 118, 122, 158, 275, 280, 284, 288, or 291, or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retaining substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) said CDRL3 comprises or consists of an amino acid sequence of any one of SEQ ID NOs: 118, 122, 158, 275, 280, 284, 288, or 291, or a sequence variant thereof, said sequence variant comprising one, two, or three amino acid substitutions, one or more of said substitutions being optionally retaining substitutions and/or substitutions of germline-encoded amino acids. Embodiment 36. The composition of embodiment 33, wherein the first antibody or antigen-binding fragment comprises a VH sequence as described in any one of SEQ ID NOs: 102, 235, 238, 241, 243, 245, 247, 249, or 251 and a VL sequence as described in any one of SEQ ID NOs: 105, 254, 257, or 260, and wherein the second antibody or antigen-binding fragment comprises a VH sequence as described in any one of SEQ ID NOs: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and a VL sequence as described in any one of SEQ ID NOs: 115, 121, 157, 272, 277, 279, 282, 286, or 290. Embodiment 37. A composition comprising a polynucleotide as in any one of embodiments 24 to 27 encapsulated in a carrier molecule, wherein the carrier molecule optionally comprises a lipid, a lipid-derived delivery vehicle, such as a liposome, a solid lipid nanoparticle, an oily suspension, a submicron lipid emulsion, a lipid microbubble, a reverse lipid micelle, an otic liposome, a lipid microtubule, a lipid microcolumn, a lipid nanoparticle (LNP), or a nanoscale platform. Embodiment 38. A method for treating severe acute respiratory syndrome beta coronavirus infection (e.g., infection caused by SARS-CoV-2) in a subject, the method comprising administering to the subject an effective amount of (i) an antibody or antigen-binding fragment as described in any one of Embodiments 1 to 23; (ii) a polynucleotide as described in any one of Embodiments 24 to 27; (iii) a recombinant vector as described in Embodiment 28; (iv) a host cell as described in Embodiment 29; and/or (v) a human B cell as described in Embodiment 30, and/or (vi) a composition as described in any one of Embodiments 31 to 37. Embodiment 39. An antibody or antigen-binding fragment of any one of Embodiments 1 to 23, a polynucleotide of any one of Embodiments 24 to 27, a recombinant vector of Embodiment 28, a host cell of Embodiment 29, a human B cell of Embodiment 30, and/or a composition of any one of Embodiments 31 to 37, for use in a method of treating severe acute respiratory syndrome beta coronavirus infection (e.g., infection caused by SARS-CoV-2) in an individual. Embodiment 40. An antibody or antigen-binding fragment of any one of Embodiments 1 to 23, a polynucleotide of any one of Embodiments 24 to 27, a recombinant vector of Embodiment 28, a host cell of Embodiment 29, a human B cell of Embodiment 30, and/or a composition of any one of Embodiments 31 to 37 for the preparation of a medicament for treating a severe acute respiratory syndrome beta coronavirus infection (e.g., an infection caused by SARS-CoV-2) in a subject. Embodiment 41. An antibody or antigen-binding fragment of any one of Embodiments 1 to 23 or 39 to 40, wherein the antibody or antigen-binding fragment binds to two or more severe acute respiratory syndrome beta coronavirus S proteins as measured using bio-thin layer interferometry. Embodiment 42. A kit comprising a liquid composition and instructions for use thereof in treating SARS-CoV-2 infection in an individual, wherein the liquid composition comprises the antibody or antigen-binding fragment of any one of Embodiments 1 to 23 or 39 to 40. Embodiment 43. The kit of Embodiment 42, wherein the instructions for use are for the method of Embodiment 38 or the use of any one of Embodiments 39 to 40. Embodiment 44. A method for in vitro diagnosis of severe acute respiratory syndrome beta coronavirus infection (e.g., infection caused by SARS-CoV-2), the method comprising: (i) contacting a sample from an individual with an antibody or antigen-binding fragment as described in any one of Embodiments 1 to 23; and (ii) detecting a complex comprising an antigen and the antibody, or comprising an antigen and the antigen-binding fragment. Embodiment 45. A method for producing an antibody or antigen-binding fragment as described in any one of Embodiments 1 to 23 or Embodiments 39 to 40, wherein the method comprises culturing a host cell expressing the antibody or antigen-binding fragment under conditions and for a time sufficient to produce the antibody or antigen-binding fragment. Embodiment 46. The method for producing an antibody or an antigen-binding fragment of Embodiment 45, wherein the host cell comprises the recombinant vector of Embodiment 28. Embodiment 47. The method for producing an antibody or an antigen-binding fragment of Embodiment 46, wherein the host cell is a mammalian cell. *Table 2 indicates CDRH1, CDRH2 and CDRH3d (IMGT definition) in bold in order in each corresponding VH sequence; and indicates CDRL1, CDRL2, CDRL3 in order in bold in each corresponding VL sequence.

Example 1 Antibody Production and Materials The following materials and methods were used in Example 1 and, unless otherwise stated, were also used in Examples 2 and 3. Cell lines Cell lines used in Example 1 were obtained from ATCC (HEK293T, Vero, and Vero-E6), ThermoFisher Scientific (Expi293F™ cells). Recombinant protein production Wild-type SARS-CoV-2 RBD (with N-terminal signal peptide and "ETGT", and C-terminal 8xHis tag) was expressed in Expi293F cells in the presence of 10 µM kifunensine at 37°C and 8% CO2. Transfections were performed using the ExpiFectamine 293 Transfection Kit (Thermo Fisher Scientific). Cell culture supernatants were collected four days after transfection and supplemented with 10x PBS to a final concentration of 2.5x PBS (342.5 mM NaCl, 6.75 mM KCl, and 29.75 mM phosphate). SARS-CoV-2 S hexapro protein containing six proline substitutions for cryo-EM single particle studies was expressed and purified using known methods. Antibody Isolation and Recombinant Production Antigen-specific IgG ⁺ memory B cells were isolated and selected from PBMCs of convalescent individuals previously vaccinated or infected with SARS-CoV-2 and then later infected with the SARS-CoV-2 Omicron variant. Briefly, CD19 ⁺ B cells were enriched by staining with CD19 PE-Cy7 and anti-PE microbeads (Milteniy) followed by positive selection using LS columns. Enriched B cells were stained with anti-IgD, anti-IgM, anti-IgA, anti-CD14, all PE markers, and pre-fusion SARS-CoV-2 S-Avi tag conjugated to streptavidin Alexa-Fluor 647 (Life Technologies). SARS-CoV-2-specific IgG ⁺ memory B cells were sorted and seeded on MSCs (mesenchymal stromal cells) at 0.5 cells/well in the presence of CpG2006, IL-2, IL6, IL-10, and IL-21 using known methods. After 7 days, B cell supernatants were screened by ELISA binding to a panel of RBDs representing different SARS-beta coronavirus clades and neutralized using high-throughput VSV SARS-CoV-2 S-based microneutralization. Ab VH and VL sequences were obtained by reverse transcription PCR (RT-PCR) and mAbs were expressed as recombinant human IgG1 carrying the half-life-extending M428L/N434S ("LS", or "MLNS") mutations in the Fc region fragment. ExpiCHO cells were transiently transfected with heavy and light chain expression vectors using known methods. The VH and VL gene families and the number of somatic mutations were determined by analyzing the homology of the VH and VL sequences to known human V, D, and J genes using the database IMGT. UCA sequences of the heavy and light chain variable regions were constructed using IMGT/V-QUEST. MAb affinity purification was performed on an ÄKTA Xpress FPLC (Cytiva) operated by UNICORN software version 5.11 (Build 407) using HiTrap Protein A columns (Cytiva) for full-length human and hamster mAbs and CaptureSelect CH1-XL MiniChrom columns (ThermoFisher Scientific) for Fab fragments using PBS as the mobile phase. Buffer exchange to the appropriate formulation buffer was performed using a HiTrap Fast Desalting column (Cytiva). The final product was sterilized by filtering through a 0.22 µm filter and stored at 4°C. Various comparative anti-SARS-CoV-2 antibodies were used in these Examples. S2X259 is described in Tortorici, MA, et al . Broad sarbecovirus neutralization by a human monoclonal antibody. Nature 59 7 , 103-108 (2021). https://doi.org/10.1038/s41586-021-03817-4. S2K146 is described in Park, YJ., et al . Science https://doi.org/10.1126/science.abm8143 (2022). S2X324 is described in WO2021/226560. S309 is described in Pinto, D., et al . Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature 583 , 290-295 (2020). https://doi.org/10.1038/ s41586-020-2349-y. Sotoviromab (VIR-7831) was developed from S309 and is described in Cathcart, A., et al .The dual function monoclonal antibodies VIR-7831 and VIR-7832 demonstrate potent in vitro and in vivo activity against SARS-CoV-2; bioRxiv 2021.03.09.434607; doi: https://doi.org/10.1101/2021.03.09.434607. Sotoviromab is an IgG1 antibody with an MLNS F mutation in addition to the VH and VL sequences shown in Table 4. The antigen binding sites of certain antibodies used in the Examples are provided in Figure 3 and Table 4 . Antibodies or DNA sequences encoding antibodies used in the embodiments Example 2 Testing of S3A3 and S3A19 Monoclonal Antibodies Unless otherwise indicated in this Example 2, all tests were performed as described in Example 1. Spike Protein Binding ELISA Binding of various monoclonal antibodies to the spike protein RBD of different SARS beta-coronaviruses was measured by enzyme-linked immunosorbent assay (ELISA). 96 half-area well plates (Corning, 3690) were coated with 25 µl of SARS beta-coronavirus RBD protein at 5 µg/ml prepared in PBS (pH 7.2) at 4°C overnight. After a 60-minute blocking step with PBS 1% BSA (Sigma-Aldrich, A3059) at room temperature, the plates were incubated with serial dilutions of mAb for 60 minutes at room temperature. After 4 washing steps with PBS 0.05% Tween 20 (PBS-T) (Sigma-Aldrich, 93773), goat anti-human IgG secondary antibody (Southern Biotech, 2040-04) was added and incubated for 45 minutes at room temperature. The plates were then washed 4 times with PBS-T and 4-nitrophenyl phosphate (pNPP, Sigma-Aldrich, 71768) substrate was added. After 45 minutes of incubation, the absorbance at 405 nm was measured by a plate reader (Biotek) and the data were plotted using Prism GraphPad. The IC50 of each antibody/virus combination was determined. ELISA assays were performed to test the ability of S3A3 and S3A19, along with other antibodies (including comparator antibodies S2X259 and S2K146), to bind to various SARS-CoV-2 betacoronaviruses representing clades 1a, 1b, 2, and 3, as well as several SARS-CoV-2 variants ( Figure 4 ). The results are summarized in Figure 5 (right panel). Neutralization assays To evaluate the neutralizing potency of S3A3 and S3A19, dose response inhibition assays were performed using a vesicular stomatitis virus (VSV) pseudotyping platform. Pseudotyped viruses were prepared using Lenti-X 293 cells seeded in 15-cm culture dishes. Briefly, cells in culture medium (DMEM supplemented with 10% heat-activated FBS, 1% PenStrep) were transfected with 25 µg of plasmid encoding the corresponding S glycoprotein using TransIT-Lenti (Mirus) as transfection reagent. One day after transfection, cells were infected with vesicular stomatitis virus (VSV) (G*ΔG-luciferase) for 1 hour, washed three times in PBS with Ca ²⁺ /Mg ²⁺ (Thermo Fisher), and then 25 ml of culture medium/dish were added. Particles were harvested after 18 to 24 hours, clarified from cell debris by centrifugation at 2,000 x g for 20 minutes at 4°C, aliquoted and stored at -80°C until used in neutralization experiments. For neutralization experiments, Vero E6 cells were plated at 20,000 cells/well in medium into white 96-well plates (PerkinElmer, 6005688) and incubated overnight at 37°C 5% CO2. Ten 3-fold serial dilutions of mAb were prepared in medium and mixed 1:1 with pseudotyped VSV prepared in medium to infect cells at the desired MOI. After 60 minutes of incubation at 37°C, the cell medium was aspirated and 50 µl of the PV/mAb mixture was added to the cells and incubated for 60 minutes at 37°C 5% _CO2 . After 60 minutes, 100 μl of medium was added to the cells and incubated for the next 16 to 24 hours at 37°C 5% CO _2. At the end of the incubation time, the medium was removed from the cells and 50 μl/well of Steadylite (PerkinElmer) diluted 1:2 with PBS with Ca ²⁺ Mg ²⁺ was added to the cells and incubated for 10 minutes in the dark. The luminescence signal was read using a Synergy H1 Hybrid Multi-Mode plate reader (Biotek). The measurements were performed in duplicate, and at least six wells per plate contained untreated infected cells (defining 0% neutralization, "MAX RLU" value) and infected cells in the presence of the control, defining 100% neutralization, "MIN RLU" value. The mean relative light units (RLU) of untreated infected cells were subtracted from the mean MIN RLU (MIN RLUave) and used to normalize the percentage of neutralization of individual RLU values of the experimental data according to the following formula: (1-(RLUx-MIN RLUave)/(MAX RLUave-MIN RLUave)) x 100. Data were analyzed and visualized using Prism (version 9.1.1). IC50 values were calculated by interpolation of log(inhibitor) versus response using a variable slope (four-parameter) nonlinear regression with an upper constraint of ≤100 and a lower constraint equal to 0. Results for variants of SARS-CoV-2 are presented in Figure 5 (left panel) and Table 5 along with results for other SARS-betacoronaviruses. S3A3 and S3A19 neutralized the Omicron variant of SARS-CoV-2 with low IC50. The fold changes compared to neutralization by comparator antibody S2X324 are presented in Table 6 . Additional neutralization testing was performed against SARS-CoV-2 variants of interest, and the results are presented in Figure 6. Results of additional neutralization testing of antibodies including S3A3 and S3A19 are presented in Figure 7. A summary of the results is presented in Table 7 . Thin-layer interferometry and KD Thin-layer interferometry (BLI) experiments were performed using Octet Red96 (ForteBio), and all reagents were prepared in Kinetics buffer (KB) (PBS 0.01% BSA). To assess competition with S2X259, S309, S2K146, and S2X324, His-tagged SARS-CoV-2 RBD was prepared at 8 µg/ml in kinetics buffer (PBS 0.01% BSA) and loaded onto prehydrated anti-penta-HIS biosensors (Sartorius) for 2.5 min. The biosensors were then moved to a solution containing 20 µg/ml S3A3 or S3A19 mAb and the association was recorded for 5 min. The second binding step was then performed in a 20 µg/ml solution of S2X259, S309, S2K146, or S2X324 mAb and recorded for 5 minutes. Response values were exported and plotted using GraphPad Prism (version 9.1.1). The results of the binding competition assay using antibodies including AS3A3 and S3A19 are presented in Table 8 . The antibodies listed in the top row were tested for competitive ("C") or non-competitive ("NC") binding against the antibodies listed in the leftmost row. S3A3 competes with S2X324 and S309, but not with S2K146 or S2X259, indicating that its binding site is similar to (e.g., overlapping) the binding sites of S2X324 and S309 ( Figure 8 ). S3A19 competes unidirectionally with S2K146 and S2X259, but not with S2X324 and S309, indicating that its binding site is similar to (e.g., overlapping) the binding sites of S2K146 and S2X259 ( Figure 9 ). To test binding affinity, 3 ug/ml of S3A3 and comparator antibody S2X324 were prepared and immobilized on prehydrated protein A biosensors (Sartorius) for 75 seconds. After a 30-second stabilization step in KB, the biosensor was transferred to SARS-CoV-2:2 serial dilutions (starting concentration: 18.5 nM) for a 600-second association step and then transferred back to KB to record the dissociation signal for 540 seconds. The data were baseline subtracted, and the results were fitted using Pall ForteBio/Sartorius analysis software (version 12.0) and plotted using GraphPad Prism (version 9.1.1). Bio-thin layer interferometry showed that S3A3 bound to the SARS-CoV-2 RBD with nanomolar affinity similar to that observed with S2X324-v3.1 ( Figure 10 ). Similar assays were performed with S3A19 and the results are presented in Figure 11. A summary of the KD values for S3A3, S3A19, and the comparator antibody S2X324-v3.1 determined in these assays is presented in Table 9 . ACE2 Binding and FcR Activation The ability of S3A3 to bind to the RBD of various SARS-CoV-2 betacoronaviruses was assessed by competition ELISA and the results are presented in Figure 12. The results for S3A19 are presented in Figure 13. The ability of S3A3 and S3A19 to block ACE2 receptor binding to SARS-CoV-2 RBD (Wuhan-Hu-1) was assessed by competition ELISA and compared to S2X324. SARS-CoV-2 mouse/rabbit Fc-tagged RBD (final concentration 20 ng/ml) was incubated with serial dilutions of recombinant mAb (starting from 25 µg/ml) and incubated at 37°C for 1 hour. The complex RBD:mAb was then added to a 96-well MaxiSorp (Nunc) pre-coated with hACE2 (2 µg/ml in PBS) and incubated for 1 hour at room temperature. Subsequently, the plates were washed and goat anti-mouse/rabbit IgG (Southern Biotech) coupled to alkaline phosphatase (Jackson Immunoresearch) was added to detect mouse Fc-tagged RBD binding. After further washing, the substrate (p-NPP, Sigma) was added and the plates were read at 405 nm using a microplate reader (Biotek). The inhibition percentage was calculated as follows: (1-((OD sample-OD negative control (neg ctr))/(OD positive control (pos. ctr)-OD negative control))*100. S3A3 and S3A19 inhibited the binding of SARS-CoV-2 RBD to human ACE2 in a dose-dependent manner ( Figure 14 ). Neutralization of SARS-CoV-2 variants of interest and S2X324 escape mutants The ability of S3A3 and S3A19 to neutralize SARS-CoV-2 WT and variants was tested compared with antibody S2X324 v.3.1, and the results are presented in Figures 15 and 16. S3A3 and S2X324 were also tested. The ability of v.3.1 to neutralize SARS-CoV-2 variants generated using the BA.2 backbone that escapes S2X324 is presented in Figure 17 and summarized in Table 10. The results indicate that S3A3 may be effective against S2X324 escape mutants. Antibody Combinations Antibody combinations were also evaluated for their ability to neutralize SARS-CoV-2 BA.5 in VSV-PV and potential synergy at different concentrations was assessed. Results for S3A3 and S3A19 in combination at the indicated concentrations are presented in Figure 18. In Figure 18 , synergy/antagonism volume <25 µM ² % was defined as additive, between 25 and 50 µM ² % as mild, between 50 and 100 µM ² % as moderate, and >100 µM ² % as strong. The confidence level of the results was 95% and the synergy score was 101.9. Results for S3A3 and sotovir in combination at the indicated concentrations are presented in Figure 19 . In Figure 19 , synergy/antagonism <25 µM ² % was defined as additive, between 25 and 50 µM ² % as mild, between 50 and 100 µM ² % as moderate, and >100 µM ² % as strong. The confidence level of the results was 95% and the synergy score was 2.6. The results for S3A3 and S2K146 combined at the indicated concentrations are presented in Figure 20. In Figure 20 , synergy/antagonism <25 µM ² % was defined as additive, between 25 and 50 µM ² % as mild, between 50 and 100 µM ² % as moderate, and >100 µM ² % as strong. The confidence level of the results was 95% and the synergy score was 104. The results for S3A19 and sotoviromab in combination at the indicated concentrations are presented in FIG21 . In FIG21 , synergy / antagonism <25 µM ² % was defined as additive, between 25 and 50 µM ² % as mild, between 50 and 100 µM ² % as moderate, and >100 µM ² % as strong. The confidence level of the results was 95% and the synergy score was 125.5. The results for S3A19 and S2K146 in combination at the indicated concentrations are presented in FIG22 . In Figure 22 , synergistic/antagonistic amounts <25 μM ² % were defined as additive, between 25 and 50 μM ² % were defined as mild, between 50 and 100 μM ² % were defined as moderate, and >100 μM ² % were defined as strong. The confidence level of the results was 95% and the synergy score was 11.1. Example 3 Testing of S2V29 , S3O13 , S3L17 , S3I2 , S2X259 , S2X324 and Certain Other Monoclonal Antibodies Table 11 is a table summarizing the properties of variant antibodies S2V29v1.2, S3O13, S3L17, S3I2v2.1, S2X259v50 AM, S309 AM, SVB, and S2X324. The antibodies were isolated from memory B cells. The V gene usage and somatic mutation load of the selected variant antibodies are shown below: 1. S3I2 (IGHV3-53*02; VH identity = 92.1%; CDR3 length = 21 aa) 2. S3L17 (IGHV3-66*02; VH identity = 93.1%; CDR3 length = 11 aa) 3. S2V29 (IGHV3-30*18; VH identity = 94%; CDR3 length = 16 aa) 4. S3O13 (IGHV1-3*02; VH identity = 95.5%; CDR3 length = 13 aa) Some variant antibodies were tested. The following results were obtained. Binding and Neutralization Assays Figure 23 shows binding of S2V29 to various SARS-CoV-2 betacoronaviruses and neutralization of S2V29 against SARS-CoV-2 variants. Monoclonal antibodies isolated from previously vaccinated (3 doses) Omicron infected donor (BA.5) show unprecedented breadth and potency. Covers escape of S2K146, S2X259, Sotoviromab and S2X324 (on BA.2 and BA.5). Sequence liability (unpaired cysteine in VL) is repaired. S2V29-v1.2 retains the neutralization properties of the parental antibody (S2V29-v1.1) against a panel of VSV SARS-CoV-2 viruses, as shown in Figure 24 . The S2V29-v1.2 variant resolves the high-impact sequence liability in VL-CDR3 (Cys105 à Ser). Figure 25 shows the in vitro neutralization of S2V29-v1.2 against infection with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1 VSV-pp. VSV -pp carries 38 mutations. The curves shown on the left are data based on RLU counts using a selected 1:10 Omicron virus stock dilution. The fold changes are shown in Tables 12 and 13. The average fold change vs. D614G is 0.9-fold (1:10 virus stock). S2V29 and S2V29-v1.2 were tested at various concentrations on ExpiCHO-S cells transiently transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1, or BA.2). Binding to the S protein was detected using a secondary antibody labeled with Alexa Fluor 647. S2V29 and S2V29-v1.2 retained binding activity against SARS-CoV-2 BQ.1.1 ( Figure 26 ). S2X324 was also tested for binding and neutralization. Figure 25 shows in vitro neutralization of S2X324 against VSV-pp infected with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1. VSV-pp carries 38 mutations. The curves shown on the left are data based on RLU counts using a selected 1:10 Omicron virus stock dilution. The fold changes are shown in Tables 12 and 13. The average fold change vs. D614G was 0.9-fold (1:10 virus stock). S2X324 did not neutralize BQ.1.1 (1:10 virus stock). S2X324 was also tested at various concentrations on ExpiCHO-S cells transiently transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1, or BA.2). Binding to the S protein was detected using a secondary antibody labeled with Alexa Fluor 647. S2X324 exhibited weak binding to the SARS-CoV-2 BQ1.1 spike ( Figure 27 ). Figure 25 shows the in vitro neutralization of S2X259v50 against VSV-pp infected with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1. VSV-pp carries 38 mutations. The curve shown on the left is data based on RLU counts using a selected 1:10 Omicron virus stock dilution. The fold changes are shown in Tables 12 and 13. The average fold changes vs. D614G were 28.7-fold ( 1:10 virus stock) and 2.3-fold (vs. BA.2). S3O13 and S3L17 were also tested for binding and neutralization. Figure 25 shows the in vitro neutralization of S3O13 against VSV-pp infected with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1. VSV-pp carries 38 mutations. The curves shown on the left are data based on RLU counts using a selected 1:10 Omicron virus stock dilution. The fold changes are shown in Tables 12 and 13. Unexpectedly, S3O13 did not neutralize BQ.1.1 (1:10 virus stock). Figure 25 also shows the in vitro neutralization of S3L17 against VSV-pp infected with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1. VSV-pp carries 38 mutations. The curves shown on the left are data based on RLU counts using a selected 1:10 Omicron virus stock dilution. The fold changes are shown in Tables 12 and 13 . S3L17 effectively neutralized BQ.1.1 (1:10 virus stock). S2X324-v3.1, S3L17 and S3O13 were tested in hamsters infected with BA.5. All variant antibodies tested were human monoclonal antibodies with LS modification. Table 14 shows the experimental details of the test in hamsters. Figure 28 shows the log TCID values of S2X324-v3.1, S3L17 and S3O13, and isotype controls. S3L17 was found to effectively protect hamsters from BA.5 infection. S3I2v2.1 was further tested for binding and neutralization. Figure 25 shows the in vitro neutralization of S3I2v2.1 against VSV-pp infected with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1. VSV-pp carries 38 mutations. The curve shown on the left is data based on RLU counts using a selected 1:10 Omicron virus stock dilution. The fold changes are shown in Tables 12 and 13. S3I2v2.1 effectively neutralizes BQ.1.1 (1:10 virus stock). It was found that the EC50 was higher compared to previous results. Figure 29 summarizes the neutralizing activity of certain variant antibodies against SARS-CoV-2 Omicron variants. Table 15 Potential combinations of variant antibodies for treatment. Figure 30 shows neutralization of Wuhan-Hu-1 D614 and G614 mediated by sotoviromab and VIR-7832. Figure 31 illustrates the antigenic sites recognized by certain variant antibodies of the present disclosure on the SARS-CoV-2 RBD. Figure 32 shows the results of BLI studies testing S3I2, S3L17, S3O10, and S2V29 against S2K146, S2X259, S2X324, and S309. Figure 33 shows the results of a bio-thin layer interferometry (BLI) competition study testing the indicator antibodies. Table 16 shows a summary of the results from the binding competition assays. The antibodies listed in the top row are tested for competitive ("C"), partially competitive ("PC"), or non-competitive ("NC") binding to the antibodies listed in the leftmost row. Figure 34 shows the binding results of S3I1, S3L17, S2V29, and S3O13 to a set of RBDs from SARS beta coronaviruses (ELISA). Figure 35 shows the neutralization of VSV-PV by S3I2, S3L17, and S2V29 against BA.2 escape mutants. BA.2-G504D is an escape mutant of S2X259. Figure 36 shows the additional neutralization results of S3O13 against BA.2 escape mutants (including S2X324 escape mutants, S309 escape mutants, and S2K146 escape mutants). Fold changes are relative to BA.2 variants. Figure 37 shows the neutralization of VSV-PV against BA.5 escape mutants by S2V29, S3L17, S3I2, and S3O13. Table 17 summarizes the neutralization (IC50) against BA.5 escape mutants and the fold changes for BA.5 variants. Figure 38 summarizes the inhibition of ACE2 binding to the RBD of SARS-CoV-2 and SARS-CoV. Figure 39 shows S1 staining over time (positive cells are circled). S1 shedding shows that it is induced by the variant antibodies disclosed herein. Figure 40 shows the luminescence results of activated FcgRIIa and FcgRIIIa. Figure 41 summarizes the binding affinity (BLI) of S3L17 and S3O13 to a group of RBDs. Table 18 shows the KD, ka and kdis values of S3L17 and S3O13 for RBDs. Figure 42 shows the binding affinity (BLI) of S2V29 to the same set of RBDs. Table 18 shows the KD, ka and kdis values of S2V29 for RBDs. Figure 43 shows the binding affinity (BLI) to a group of RBDs representing different SARS-CoV-β coronavirus clades. Figure 44 illustrates antibody-dependent cytotoxicity (ADCC) and antibody-dependent cellular phagocytosis (ADCP). S3L17 was tested at different concentrations on ExpiCHO-S cells temporarily transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1 or BA.2). Binding to the S protein was detected using a secondary antibody labeled with Alexa Fluor 647 ( Figure 45 ). S3L17 retains binding activity against SARS-CoV-2 BQ.1.1. S3I2-v2.1 was tested at different concentrations on ExpiCHO-S cells transiently transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1, or BA.2). Binding to S protein was detected using a secondary antibody labeled with Alexa Fluor 647 ( Figure 46 ). S3I2-v2.1 retains binding activity against SARS-CoV-2 BQ.1.1. S3O13 was tested at different concentrations on ExpiCHO-S cells transiently transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1, or BA.2). Binding to the S protein was detected using a secondary antibody labeled with Alexa Fluor 647 ( Figure 47 ). S3O13 did not retain binding activity against SARS-CoV-2 BQ.1.1. S2V29 was tested at various concentrations on Expi-CHO-S cells transiently transfected with SARS-CoV-2 spike glycoproteins from variants Wuhan D614, BA.2, BQ.1.1, XBB.1, and E340A ( Figure 48 ). Specifically, Expi-CHO-S cells were harvested 24 to 48 hours after transfection, washed, and stained with the indicated antibody concentrations to assess binding to the cell surface. S2V29 exhibited potent and equal neutralizing activity against all pseudotyped viruses tested. Further testing of S3L17 and S2V29 S3L17, S2V29, REGEN-COV, and Evusheld were neutralized against pre-Omicron variants and Omicron SARS-CoV-2 variants and additional escape mutants, including sotoviromab escape mutants, begolomagumab escape mutants, S2K146 escape mutants, and S2X259 escape mutants ( Figure 49 ). IC50s for REGEN-COV and Evusheld are from the Stanford database as of January 22, 2023: https://covdb.stanford.edu/susceptibility-data/table-mab-susc/ and Park et al. Science 2022. S3L17 and S2V29 were further tested for additional neutralization against SARS-CoV-2 variants and escape mutants ( FIG. 50 and Table 19 ). Additional testing of S2V29-v1.2 against SARS-CoV and SARS-CoV-2 variants was also performed ( Figure 68 ). No rVSV escape mutants of S3L17 were identified, and all S2V29 escape mutants were only partial escapes. Full escape mutants for both antibodies were determined and marked as unsuitable ( Figure 50 ). In more than 14 million sequences from GISAID, all full escape mutants had less than 5 counts in total, indicating that such mutants are unlikely to occur. All full escape mutants require two or three nucleotide mutations. Results of similar testing with S2V29-v1.2 are provided in Figure 51 , which shows that neutralizing mutations have over 100 counts in the GISAID VS pseudotyped virus assay from 13.5 million total sequences. Further, in an assay using rVSV in two separate replicates, complete escape from S2V29-v1.2 was not observed until P5 or higher. Further testing of SARS-CoV (SARS1) and SARS-CoV-2 showed the breadth and barriers of escape in yet further strains ( Figure 51 ). Analysis of S3L17 and S2V29 data shows that escape mutants of these antibodies are unlikely to occur. Figure 52 summarizes the escape mutant neutralization and binding data and analysis of S2V29 and S3L17. GISAID counts are as of January 26, 2023, and are from over 14 million sequences, over 3 years of SARS-CoV-2 evolution (including antigenic shift). S2V29 total escape count is < 0.01%. S3L17 total escape count is < 0.00006% (below sequence error). For comparison, the escape frequency of stem helix mAb S2P6 is 0.1%. ACE2 binding and RBD performance in DMS data are obtained from <https://jbloomlab.github.io/SARS-CoV-2-RBD_DMS_Omicron/RBD-heatmaps/>. Diffusion probability is calculated using a machine learning model to predict the likelihood that a mutation will diffuse (> 0.03 to 0.05 indicates likely diffusion). ACE contact residues were identified using the published structure PDB ID 6MOJ. Putative single nucleotide mutation intermediates that lead to escape mutants were also determined ( Figure 52 ). A list of intermediate mutants required to generate the identified escape was determined in a stepwise process: that is, whether 2 or 3 mutated codons were required to change the amino acid from xx to yy. All possible intermediate AA changes (yet to be tested) were then listed. The only DMS data reported are from bloom on the effects of these mutations on ACE2 binding and RBD expression (both labeled with fitness). Further live virus testing of S2V29-v1.2 (S2V29) and S3L17 was performed ( Figure 53 and Table 20 ). The in vivo efficacy of S2V29-v1.2 (S2V29) and S3L17 was also determined. Antibodies were given 24 hours before SARS-CoV-2 BA.5 infection. The infectious viral load in the lungs was quantified on day 4. Both S2V29 and S3L17 reduced the infectious viral load in the lungs in a dose-dependent manner ( Figure 54 ). Binding affinity tests of S2V29-v1.2 (S2V29) and S3L17 to the Wuhan and BA.5 SARS-Co-V-2 RBD and a second test of S2V29-v1.2 to Wuhan and XBB1.5 ( Figure 55 ) showed picomolar binding activity to many variants and dissociation at the detection limit ( Table 21 ). A correlation between high affinity and high barrier to escape mutants was observed. SPR was also used to assess the binding affinity of S2V29-v1.2 Fab to the recombinant RBD carrying the escape mutation of BQ.1.1 ( FIG. 65 ), as well as to the recombinant RBD from other severe acute respiratory syndrome beta coronaviruses ( FIG. 66 ). Evolutionary breadth testing demonstrated that S3L17 binds to all clade 1b RBDs and S2V29-1.2 binds to all clade 1 to 3 RBDs ( Figure 56 ). This is an unexpectedly high breadth for an ACE2-competent antibody. Potential binding conformations of S2V29-v.2 and S3L17 to the RBD were determined ( Figure 57 ). The epitopes partially overlap, but the antibodies show different escape properties and no functional antagonism, making it possible to combine these two receptor-mimic antibodies. Serial passaging up to P7 with Wuhan rVSV showed no escape for either S3L17 or S2V29-v1.2 ( Table 22 ), whereas escape was observed for all other antibodies tested. S3L17 and S2V29 are ACE mimetics as demonstrated by testing for key RBD binding residues. Using deep mutation scanning (DMS), it was determined that those residues critical for S3L17 and S2V29 are also critical for ACE ( Figure 58 ). Most mutations that lost antibody binding (letters on Figure 58) also lost ACE2 binding (lighter colors). With the exception of L455W, all escape mutations required two or three nucleotide substitutions. Analysis of the binding contacts of S3L17 and S2V29 to the SARS-CoV-2 RBD showed that these contacts overlap with strong Omicron RBD-ACE2 contacts ( Figure 59 ). Figure 60 illustrates how S2V29 competes with ACE2 for binding to the RBD of SARS-CoV-2 BQ.1.1. The S2V29 epitope is outlined in black and the binding residues are shaded differently, as are the RBD contact residues. ADCP assays were performed using PBMC (monocytic sphere) effector cells and ExpiCHO target cells expressing SARS-CoV-2 to assess the effector function of S3L17 and S2V29-v1.2 ( Figure 61 ). Both S3L17 and S2V29-v.12 exhibited ADCP as measured by flow cytometry. The results for the BQ.1.1 variants were consistent with those for the Wuhan strain. ADCC assays were performed using purified NK cells to further investigate the effector function of S3L17 and S2V29-v1.2 ( Figure 62 ). Weak antibody-dependent phagocytosis was observed. FcgR activation assays in Jurkat reporter cells were also performed using S3L17-v1.2 and S2V29-v1 ( Figure 63 ). Figure 64 shows a comparison of the results obtained for S2V29-v1.2 using authentic virus vs. VSV pseudotype virus. The authentic virus data are consistent with the VSV pseudotype virus data. Figure 67 shows the results of pharmacokinetic studies in Tg32 SCID mice 3 weeks after injection. Based on this data, it is expected that S2V29-v1.2 will provide both a modest therapeutic effect and a six-month prophylactic effect after a single IM injection. Table 23 summarizes the selected properties of S2V29-v.12 and S3L17, which indicate the suitability of these antibodies or their variants for binding, treatment, prophylaxis, and testing against SARS-CoV-2. Table 23 : Properties of S2V29 and S3L17 S2V29 S2V29-v1.2 S3L17 Biophysics Tm CH2; Fab (NanoDSF) 68; 78 69; 72 71; 71 Charge and pI (icIEF) 7.62 7.17 8.32 Thermal stress (14 days, 25 mg/mL, 40C, aSEC) No gathering No gathering Chemistry Unstable residues (peptide maps at low and high pH after oxidation, simulated by computer) No obvious chemical degradation No obvious chemical degradation An oxidatively unstable Trp Virus neutralization after oxidative stress n/a No impairment Virus Neutralization at Low/High pH Pressure No impairment No impairment No impairment Q→pE (N-terminal LC) >95% Ignorable n/a O-linked glycans (peptide targeting) Very small amount Not observed without Charge profile (150 mg/ml, 40C, 1 month) Acid (5): 14.6 to 46.5% (Day 0 to Day 30) Chemically unstable residues in CDRs D54 (DG)-HC and N33 (NY)-LC (very small amount) Off-target Multi-reactivity without without without Non-GLP TCR Continuous without Continuous Hi-con Aggregation (150 mg/ml) (40°C, 4 days) Increase <2% Increase <5% HMWS: 0.50% to 4.72% (Day 0 to Day 90) Increase <2% HMWS (continuous) Viscosity (150 mg/ml) 6.67 mPa*S 6.67mPa.s 5.90 mPa*S PK Tg32 SCID mouse PK (1 month) 11±1.3 days Similar to S2V29 12±1.5 days Non-human primate (Cyno) PK (2 months) Continuous Half-life 20 +/- 3.0 days Continuous The various specific embodiments described above can be combined to provide additional specific embodiments. All U.S. patents, U.S. patent application publications, U.S. patent applications, foreign patents, foreign patent applications, and non-patent publications mentioned in this specification and/or listed in the application data sheet are incorporated herein by reference in their entirety. If it is necessary to adopt the concepts of various patents, applications, and publications, the aspects of the specific embodiments can be modified to provide further specific embodiments. According to the detailed description above, these and other changes can be made to the implementation aspects. Generally, in the following application scope, the terms used should not be interpreted as limiting the application scope to the specific embodiments disclosed in the specification and the application scope, but should be interpreted as including all possible embodiments and the full range of equivalents of the applicants of these application scopes. Therefore, the scope of the patent application is not limited by the present disclosure.

This patent or application file contains at least one color drawing. Copies of patents or patent application publications with one or more color drawings will be provided by the Patent Office upon request and payment of the necessary fee. [ Figure 1 ] shows a phylogenetic tree of SARS-CoV-2 betacoronaviruses divided into clade 1a (also known as clade 1), clade 1b (also known as clade 1/2), clade 2, and clade 3. [ Figure 2 ] shows differences in receptor binding domain (RBD) amino acid sequences among various SARS-CoV-2 betacoronaviruses and amino acids that may be important for the interaction of wild-type S2K146 with viral antigens (boxes). [ Figure 3 ] illustrates certain antibodies that bind to the SARS-CoV-2 RBD and their respective binding sites. [ Figure 4 ] shows the binding of antibodies including S3A3 and S3A19, and comparator antibodies S2X259 and S2K146 to various SARS-CoV-2 beta coronaviruses representing claims 1a, 1b, 2, and 3. [ Figure 5 ] Summarizes (on the right side of the table) the binding results from clades 1a, 1b, 2, and 3 of Figure 4. Figure 5 also shows (on the left side of the table) the neutralization IC50 values obtained in the neutralization assay of SARS-CoV-2 and its Omicron variants, and SARS-Co-V VSV. [ Figure 6 ] Shows the neutralization of certain antibodies including S3A3 and S3A19 against SARS-CoV-2 variants. [ Figure 7 ] Shows the results of repeated neutralization tests of antibodies including S3A3 and S3A19. [ Figure 8 ] Shows the results of a competitive biothin layer interferometry (BLI) study testing S3A3 against an indicator antibody. [ Figure 9 ] Shows the results of a BLI study testing S3A19 and an indicator antibody. [ Figure 10 ] Shows the binding of S3A3 and the comparator antibody S2X324-v3.1 to SARS-CoV-2 Wuhan-Hu-1 and the indicator variant (BLI). [ Figure 11 ] Shows the binding of S3A19 to SARS-CoV-2 Wuhan-Hu-1 and the indicator variant (BLI). [ Figure 12 ] Shows the binding of S3A3 to various SARS beta coronaviruses (ELISA). [ Figure 13 ] Shows the binding of S3A19 to various SARS beta coronaviruses (ELISA). [ Figure 14 ] shows inhibition of ACE-2 binding to SARS-CoV-2 Wuhan-Hu-1 RBD by the indicated antibodies. [ Figure 15 ] provides neutralization data for S3A3 and comparator antibody S2X324-v3.1 against SARS-CoV-2 Wuhan-Hu-1 ("WT") and variants of interest. [ Figure 16 ] provides neutralization data for S3A19 against SARS-CoV-2 Wuhan-Hu-1 ("WT") and variants. [ Figure 17 ] provides neutralization data for S3A3 and S2X234-v3.1 against SARS-CoV-2 variants that escape S2X324. The indicated variants were generated using the BA.2 backbone. [ Figure 18 ] provides synergy and neutralization data for S3A3 and S3A19 (combined at indicated concentrations). [ Figure 19 ] Provides synergy and neutralization data for S3A3 and sotoviromab (in the indicated concentration combinations). [ Figure 20 ] Provides synergy and neutralization data for S3A3 and S2K146 (in the indicated concentration combinations). [ Figure 21 ] Provides synergy and neutralization data for S3A19 and sotoviromab (in the indicated concentration combinations). [ Figure 22 ] Provides synergy and neutralization data for S3A19 and S2K146 (in the indicated concentration combinations). [ Figure 23 ] Shows binding of S2V29 to various SARS-CoV-2 beta coronaviruses and neutralization of S2V29 against SARS-CoV-2 variants. [ Figure 24 ] shows that S2V29-v1.2 retains the neutralizing properties of the parental antibody (S2V29-v1.1) against a panel of VSV SARS-CoV-2 viruses. [ Figure 25 ] shows the in vitro neutralization of S2V29-v1.2 against VSV-pp infected with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1. The curves shown on the left are data based on RLU counts using a selected 1:10 dilution of the Omicron virus stock. Figure 25 also shows the in vitro neutralization of S2X324 against VSV-pp infected with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1. VSV-pp carries 38 mutations. The curves shown on the left are data based on RLU counts using a selected 1:10 Omicron virus stock dilution. Figure 25 also shows the in vitro neutralization of S2X259v50 against infection with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1 VSV-pp. VSV-pp carries 38 mutations. The curves shown on the left are data based on RLU counts using a selected 1:10 Omicron virus stock dilution. Figure 25 also shows the in vitro neutralization of S3O13 against infection with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1 VSV-pp. The curves shown on the left are data based on RLU counts using a selected 1:10 Omicron virus stock dilution. Figure 25 also shows the in vitro neutralization of S3L17 against infection with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1 VSV-pp. The curves shown on the left are data based on RLU counts using a selected 1:10 dilution of Omicron virus stock. Figure 25 also shows the in vitro neutralization of S3I2v2.1 against infection with WT (Wuhan-1 D614G) and Omicron BA.2 and BQ.1.1 VSV-pp. The curves shown on the left are data based on RLU counts using a selected 1:10 dilution of Omicron virus stock. [ Figure 26 ] shows the binding activity of S2V29 and S2V29-v1.2 tested at different concentrations on ExpiCHO-S cells transiently transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1 or BA.2). Binding to S protein was detected using a secondary antibody labeled with Alexa Fluor 647. [ Figure 27 ] shows the binding activity of S2X324 tested at different concentrations on ExpiCHO-S cells transiently transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1 or BA.2). Binding to S protein was detected using a secondary antibody labeled with Alexa Fluor 647. [ Figure 28 ] shows the log TCID values of S2X324-v3.1, S3L17 and S3O13, and isotype controls. [ Figure 29 ] Summarizes the neutralization activity of certain variant antibodies against SARS-CoV-2 Omicron variants. [ Figure 30 ] Shows the neutralization of Wuhan-Hu-1 D614 and G614 mediated by sotoviromab and VIR-7832. [ Figure 31 ] Illustrate the antigenic sites recognized by certain variant antibodies of the present disclosure on the SARS-CoV-2 RBD. [ Figure 32 ] Shows the results of biological thin layer interferometry (BLI) studies testing S3I2, S3L17, S3O10, and S2V29 against S2K146, S2X259, S2X324, and S309. [ Figure 33 ] Shows the results of a biothin layer interferometry (BLI) competition study testing the indicator antibodies. [ Figure 34 ] Shows the binding results of S3I1, S3L17, S2V29, and S3O13 to a set of RBDs from SARS-CoV-2 (ELISA). [ Figure 35 ] Shows the neutralization of VSV-PV by S3I2, S3L17, and S2V29 against BA.2 escape mutants. BA.2-G504D is an escape mutant of S2X259. [ Figure 36 ] Shows the additional neutralization results of S3O13 against BA.2 escape mutants (including S2X324 escape mutant, S309 escape mutant, and S2K146 escape mutant). Fold changes are relative to BA.2 variants. [ FIG. 37 ] Shows neutralization of VSV-PV against BA.5 escape mutants by S2V29, S3L17, S3I2, and S3O13. [ FIG. 38 ] Summary of ACE2 binding inhibition of RBDs of SARS-CoV-2 and SARS-CoV. [ FIG. 39 ] Shows S1 staining over time (positive cells are circled). S1 shedding is shown to be induced by the variant antibodies of the present disclosure. [ FIG. 40 ] Shows luminescence results for activation of FcgRIIa and FcgRIIIa. [ FIG. 41 ] Summary of binding affinity (BLI) of S3L17 and S3O13 to a panel of RBDs. [ FIG. 42 ] Shows binding affinity (BLI) of S2V29 to the same panel of RBDs. [ Figure 43 ] shows the binding affinity (BLI) to a group of RBDs representing different SARS-CoV-2 beta coronavirus clades. [ Figure 44 ] illustrates antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cellular phagocytosis (ADCP). [ Figure 45 ] shows the binding activity of S3L17 tested at different concentrations on ExpiCHO-S cells transiently transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1 or BA.2). Binding to the S protein was detected using a secondary antibody labeled with Alexa Fluor 647. [ Figure 46 ] shows the binding activity of S3I2-v2.1 tested at different concentrations on ExpiCHO-S cells temporarily transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1 or BA.2). Binding to S protein was detected using a secondary antibody labeled with Alexa Fluor 647. [ Figure 47 ] shows the binding activity of S3O13 tested at different concentrations on ExpiCHO-S cells temporarily transfected with SARS-CoV-2 spike glycoprotein (Wuhan D614, BQ.1.1 or BA.2). Binding to S protein was detected using a secondary antibody labeled with Alexa Fluor 647. [ Figure 48 ] shows the binding activity of S2V29 tested at different concentrations on ExpiCHO-S cells temporarily transfected with SARS-CoV-2 spike glycoprotein (Wuhan-D614 ("Wu-D614"), BA.2, BQ 1.1, XBB.1, and E340A). [ Figure 49 ] shows the additional neutralization results of S3L17-v1.2 (S3L17), S2V29-v1.2 (S2V29), REGEN-COV and Evusheld against pre-Omicron variants and Omicron SARS-CoV-2 variants and additional escape mutants, including sotrovimab escape mutants, bebtelovimab escape mutants, S2K146 escape mutants, and S2X259 escape mutants. [ Figure 50 ] shows the additional neutralization results of S3L17 and S2V29 against SARS-CoV-2 variants and escape mutants. [ Figure 51 ] Shows additional neutralization results of S2V29-v1.2 against SARS-CoV and SARS-CoV-2 variants and escape mutants. Mutations associated with low pseudotype virus infectivity in the BQ.1.1 or XBB1.5 background are underlined in the variant box. [ Figure 52 ] Summarizes the neutralization and binding data of escape mutants of S2V29 and S3L17. Nt changes: number of nucleotide changes required for the mutation to occur. Retained: position identity between SARS-CoV betacoronaviruses. *, NT with VSV-pp, IC50 (in ng/ml); †, virus with low fitness, IC50 to be confirmed; #, L455W was found to also have BA.2 DMS escape; †, FC calculated compared to Wu-D614G. Figure 52 also shows the putative single nucleotide mutation intermediates that lead to escape mutants. [ Figure 53 ] Shows the results of two replicates of live cell testing with S2V29-v1.2 (S2V29) and S3L17. [ Figure 54 ] Shows the in vivo viral protection data of S2V29-v1.2 (S2V29) and S3L17. [ Figure 55 ] Shows the binding affinity dates of S2V29-v1.2 and S3L17 to Wuhan, BA.5, and XBB1.5 SARS-Co-V-2 RBD. [ Figure 56 ] Shows the results of the evolutionary breadth test of S2V29-v1.2 (S2V29) and S3L17. [ Figure 57 ] shows possible epitopes of S3L17 and S2V29 and binding of these antibodies to SARS-CoV-2 RBD. [ Figure 58 ] shows deep mutational scanning (DMS) results of S3L17 and S2V29-v1.2 binding compared to ACE2 binding of Wuhan and BA.2 strains. [ Figure 59 ] shows the binding contacts of S3L17 and S2V29 to SARS-CoV-2 RBD and overlap with strong Omicron RBD-ACE2 contacts. [ Figure 60 ] shows how S2V29 binding competes with RBD-ACE2 binding. [ Figure 61 ] shows the results of ADCP test with S3L17 and S2V29-v1.2 (S2V29). [ Figure 62 ] shows the results of ADCC assays with S3L17-v1.2 and S2V29-v1.2. [ Figure 63 ] shows the results of FcgR activation assays with S3L17-v1.2 and S2V29-v1.2. [ Figure 64 ] shows a comparison of the results obtained with authentic virus and VSV pseudotyped virus for S2V29-v1.2. [ Figure 65 ] shows the binding affinity of S2V29-v1.2 to various BQ1.1 escape mutants as measured by surface plasmon resonance (SPR). [ Figure 66 ] shows the binding affinity of S2V29-v1.2 to various SARS-CoV-2 beta coronaviruses as measured by surface plasmon resonance (SPR). [ Figure 67 ] shows the pharmacokinetic test data of S2V29-v1.2. [ Figure 68 ] shows the additional neutralization data of S2V29-v1.2 against SARS-CoV and SARS-CoV-2 variants.

TW202417477A_112124637_SEQL.xml

Claims (33)

An antibody, or an antigen-binding fragment thereof, comprising a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein: (A) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 24, or a functional variant thereof, wherein the functional variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 25, or a functional variant thereof, the functional variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 26, or a functional variant thereof, the functional variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 28, or a functional variant thereof, the functional variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (v) the CDRL2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 29, or a functional variant thereof, the functional variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 30, or a functional variant thereof, the functional variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (B) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 32 or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 33, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 34, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: ID NO: 38, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (v) the CDRL2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 39, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 40, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (C) (i) The CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 84 or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, wherein one or more of the substitutions are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (ii) The CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 85 or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, wherein one or more of the substitutions are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iii) The CDRH3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 86 or 186, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 88 or 194, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (v) the CDRL2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 89, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 90, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (D) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as any one of SEQ ID NO: 94, 198, or 208, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 95, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 96, 199, 202, or 205, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 98, 226, 229, 232, or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, wherein one or more of the substitutions are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (v) the CDRL2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 39, or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, wherein one or more of the substitutions are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; and/or (vi) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 99 amino acid sequence, or a sequence variant thereof, the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (E) (i) the CDRH1 comprises or consists of the following: such as the amino acid sequence of SEQ ID NO: 103 or a sequence variant thereof, the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (ii) the CDRH2 comprises or consists of the following: such as the amino acid sequence of SEQ ID NO: 85 or a sequence variant thereof, the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iii) the CDRH3 comprises or consists of the following: an amino acid sequence of any one of SEQ ID NO: 104, 236, or 239, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (iv) the CDRL1 comprises or consists of the following: an amino acid sequence of any one of SEQ ID NO: 106 or 255, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (v) the CDRL2 comprises or consists of the following: an amino acid sequence of any one of SEQ ID NO: 107, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; and/or (iv) the CDRL3 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 108 or 258, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; and/or; (E) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 103 or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (ii) the CDRH2 comprises or consists of the following: such as the amino acid sequence of SEQ ID NO: 85, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iii) the CDRH3 comprises or consists of the following: such as the amino acid sequence of any one of SEQ ID NO: 104, 236, or 239, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (iv) the CDRL1 comprises or consists of: an amino acid sequence such as any one of SEQ ID NO: 106 or 255, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; (v) the CDRL2 comprises or consists of: an amino acid sequence such as SEQ ID NO: 107, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of amino acids encoded by the germline; and/or (iv) the CDRL3 comprises or consists of: an amino acid sequence such as SEQ ID NO: 108 or 258, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (F) (i) the CDRH1 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 112 or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retained substitutions and/or substitutions of amino acids encoded by the germline; (ii) the CDRH2 comprises or consists of the following: an amino acid sequence such as SEQ ID NO: 113, 126, 129, 132, 135, 138, 142, 146, 150, 154, 267, or 270, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iii) the CDRH3 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 114, 139, 143, 147, 151, or 155, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (iv) the CDRL1 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 116, 273, or 283, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; (v) the CDRL2 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 117, 274, or 287, or a sequence variant thereof, the sequence variant comprising one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids; and/or (vi) the CDRL3 comprises or consists of an amino acid sequence as any one of SEQ ID NO: 118, 122, 158, 275, 280, 284, 288, or 291, or a sequence variant thereof, wherein the sequence variant comprises one, two, or three amino acid substitutions, one or more of which are optionally retention substitutions and/or substitutions of germline-encoded amino acids, wherein the substitutions are optionally substitutions as shown in Table 2 or Table 2, and wherein the antibody or antigen-binding fragment is capable of binding to the surface glycoprotein of severe acute respiratory syndrome beta coronavirus. An antibody, or an antigen-binding fragment thereof, comprising a heavy chain variable domain (VH) and a light chain variable domain (VL), wherein the heavy chain variable domain comprises CDRH1, CDRH2, and CDRH3, and the light chain variable domain comprises CDRL1, CDRL2, and CDRL3, wherein the CDRH1, CDRH2, and CDRH3 and the CDRL1, CDRL2, and CDRL3 have the following amino acid sequences: (A) SEQ ID NOs: 24 to 26 and 28 to 30, respectively; (B) SEQ ID NOs: 32 to 34 and 38 to 40, respectively; (C) SEQ ID NOs: 84 to 86 or 84, 85 and 186 and 88 to 90 or 194, 89, and 90, respectively; (D) SEQ ID NOs: 94 to 96; 198, 95 and 96; 208, 95 and 96; 94, 95, and 199; 198, 95 and 199; 208, 95, and 199; 94, 95, and 202; 198, 95, and 205; 208, 95, and 199; 205, 95, and 202; or 208, 95, and 205, and 98, 39, and 99; 226, 39, and 99; or 229, 39, and 232; (E) are SEQ ID NOs: 103, 85, and 104; 103, 85, and 236; or 103, 85, and 239, and 106 to 108; 106, 107, and 258; 255, 107, and 108; or 255, 107, or 258; and (F) are SEQ ID NOs: 112 to 114; 112, 126, and 114; 112, 129, and 114; 112, 132, and 114; 112, 135, and 114; 112, 138, and 114; 112, 142, and 114; 112, 146, and 114; 112, 150, and 114; 112, 154, and 114; 112, 267, and 114; 112, 270, and 114; 112, 113, and 139; 112, 126, and 139; 112, 129, and 139; 112, 132, and 139; 112, 135, and 139; 112 , 138, and 139; 112, 142, and 139; 112, 146, and 139; 112, 150, and 139; 112, 154, and 139; 112, 267, and 139; 112, 270, and 139; 112, 113, and 143; 112, 126, and 143; 112, 129, and 143; 112, 132, and 143; 112, 135, and 143; 112, 138, and 143; 112, 142, and 143; 112, 146, and 143; 112, 150, and 143; 112, 154, and 143; 1 12, 267, and 143; 112, 270, and 143; 112, 113, and 147; 112, 126, and 147; 112, 129, and 147; 112, 132, and 147; 112, 135, and 147; 112, 138, and 147; 112, 142, and 147; 112, 146, and 147; 112, 150, and 147; 112, 154, and 147; 112, 267, and 147; 112, 270, and 147; 112, 113, and 151; 112, 126, and 151; 112, 129, and 151; 112, 132, and 151; 112, 135, and 151; 112, 138, and 151; 112, 142, and 151; 112, 146, and 151; 112, 150, and 151; 112, 154, and 151; 112, 267, and 151; 112, 270, and 151; 112, 113, and 155; 112, 126, and 155; 112, 129, and 155; 112, 132, and 155; 112, 135, and 155; 112, 138, and 155; 112, 142, and 155; 112, 146, and 15 51; 112, 150, and 155; 112, 154, and 155; 112, 267, and 155; or 112, 270, and 155; and 116 to 118; 116, 274, and 118; 116, 287, and 118; 116, 117, and 122; 116, 274, and 122; 116, 287, and 122; 116, 117, and 158; 116, 274, and 275; 116, 287, and 275; 116, 117, and 280; 116, 274, and 280; 116, 287, and 280; 116, 117, and 2 84; 116, 274, and 284; 116, 287, and 284; 116, 117, and 288; 116, 274, and 288; 116, 287, and 288; 116, 117, and 291; 116, 274, and 291; 116, 287, and 291; 273, 117, and 118; 273, 274, and 118; 273, 287, and 118; 273, 117, and 122; 273, 274, and 122; 273, 287, and 122; 273, 117, and 158; 273, 274, and 275; 273, 287 , and 275; 273, 117, and 280; 273, 274, and 280; 1273, 287, and 280; 273, 117, and 284; 273, 274, and 284; 273, 287, and 284; 273, 117, and 288; 273, 274, and 288; 273, 287, and 288; 273, 117, and 291; 273, 274, and 291; 273, 287, and 291; 283, 117, 118; 283, 274, and 118; 283, 287, and 118; 283, 117, and 122; 283, 274, and 122; 283, 287, and 122; 283, 117, and 158; 283, 274, and 275; 283, 287, and 275; 283, 117, and 280; 283, 274, and 280; 283, 287, and 280; 283, 117, and 284; 283, 274, and 284; 283, 287, and 284; 283, 117, and 288; 283, 274, and 288; 283, 287, and 288; 283, 117, and 291; 283, 274, and 291; or 283, 287, and 291. The antibody or antigen-binding fragment of claim 1 or claim 2, wherein the SARS-CoV-2 is a Clade 1b SARS-CoV-2. The antibody or antigen-binding fragment of claim 3, wherein the severe acute respiratory syndrome beta coronavirus is SARS-CoV-2 WT, SARS-CoV-2 BA.1, RATG13, PANG/GD, or PAND/GX. The antibody or antigen-binding fragment of any one of claims 1 to 4, wherein the antibody or antigen-binding fragment is capable of binding to the surface glycoprotein when the surface glycoprotein is expressed on the cell surface of a host cell and/or contained on a virus particle. An antibody or antigen-binding fragment of any one of claims 1 to 5, which is capable of binding to surface glycoproteins from two or more (e.g., two, three, four, five, or more) severe acute respiratory syndrome beta coronaviruses. An antibody or antigen-binding fragment of any one of claims 1 to 6, which is capable of neutralizing infection caused by one or more severe acute respiratory syndrome beta coronaviruses in an in vitro model of infection and/or in an in vivo animal model of infection and/or in humans. An antibody or antigen-binding fragment of any one of claims 1 to 7, which is capable of neutralizing infection caused by two or more severe acute respiratory syndrome beta coronaviruses in an in vitro model of infection and/or in an in vivo animal model of infection and/or in humans. The antibody or antigen-binding fragment of any one of claims 1 to 8, wherein the VH and VL respectively comprise or consist of an amino acid sequence that is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the amino acid sequences described below; or respectively comprise or consist of the amino acid sequences described below: (I) 1) SEQ ID NOs: 23 and 27; 2) SEQ ID NOs: 23 and 37; 3) SEQ ID NOs: 31 and 27; 4) SEQ ID NOs: 31 and 37; 5) SEQ ID NOs: 35 and 27; 6) SEQ ID NOs: 35 and 37; 7) SEQ ID NOs: 36 and 27; 8) SEQ ID NO: 36 and 37; 9) SEQ ID NO: 43 and 27; 10) SEQ ID NO: 43 and 37; 11) SEQ ID NO: 83 and 87; 12) SEQ ID NO: 83 and 193; 13) SEQ ID NO: 179 and 87; 14) SEQ ID NO: 179 and 193; 15) SEQ ID NO: 181 and 87; 16) SEQ ID NO: 181 and 193; 17) SEQ ID NO: 183 and 87; 18) SEQ ID NO: 183 and 193; 18) SEQ ID NO: 185 and 87; 19) SEQ ID NO: 185 and 193; 20) SEQ ID NO: 188 and 87; 21) SEQ ID NO: 188 and 193; 22) SEQ ID NO: 190 and 87; 23) SEQ ID NO: 190 and 193; 24) SEQ ID NO: 93 and 97; 25) SEQ ID NO: 93 and 225; 26) SEQ ID NO: 93 and 228; 27) SEQ ID NO: 93 and 231; 28) SEQ ID NO: 197 and 97; 29) SEQ ID NO: 197 and 225; 30) SEQ ID NO: 197 and 228; 31) SEQ ID NO: 197 and 231; 32) SEQ ID NO: 201 and 97; 33) SEQ ID NO: 201 and 225; 34) SEQ ID NO: 201 and 228; 35) SEQ ID NO: 201 and 231; 36) SEQ ID NO: 204 and 97; 37) SEQ ID NO: 49) SEQ ID NO: 212 and 225; 50) SEQ ID NO: 212 and 228; 51) SEQ ID NO: 212 and 231; 52) SEQ ID NO: 212 and 231; 64) SEQ ID NO: 220 and 97; 65) SEQ ID NO: 220 and 225; 66) SEQ ID NO: 220 and 228; 67) SEQ ID NO: 220 and 228; 7) SEQ ID NO: 235 and 105; 77) SEQ ID NO: 235 and 254; 78) SEQ ID NO: 235 and 257; 79) SEQ ID NO: 235 and 260; 80) SEQ ID NO: 238 and 105; 81) SEQ ID NO: 238 and 254; 82) SEQ ID NO: 238 and 257; 83) SEQ ID NO: 238 and 260; 84) SEQ ID NO: 241 and 105; 85) SEQ ID NO: 241 and 254; 86) SEQ ID NO: 241 and 257; 87) SEQ ID NO: 241 and 260; 88) SEQ ID NO: 243 and 105; 89) SEQ ID NO: 243 and 254; 90) SEQ ID NO: 243 and 257; 91) SEQ ID NO: 243 and 260; 92) SEQ ID NO: 245 and 105; 93) SEQ ID NO: 245 and 254; 94) SEQ ID NO: 245 and 257; 95) SEQ ID NO: 245 and 260; 96) SEQ ID NO: 106) SEQ ID NO: 251 and 257; 107) SEQ ID NO: 251 and 260; 108) SEQ ID NO: 111 and 115; 109) SEQ ID NO: 111 and 121; 110) SEQ ID NO: 19) SEQ ID NO: 125 and 157; 120) SEQ ID NO: 125 and 272; 121) SEQ ID NO: 125 and 277; 122) SEQ ID NO: 125 and 279; 123) SEQ ID NO: 125 and 282; 124) SEQ ID NO: 125 and 157; 125) SEQ ID NO: 125 and 272; 126) SEQ ID NO: 125 and 277; 127) SEQ ID NO: 125 and 279; 128) SEQ ID NO: 128 and 282; 129) SEQ ID NO: 129 and 290; 130) SEQ ID NO: 125 and 157; 131) SEQ ID NO: 125 and 272; 132) SEQ ID NO: 125 and 277; 133) SEQ ID NO: 125 and 279; 134) SEQ ID NO: 125 and 282; 135) SEQ ID NO: 125 and 282; 136) SEQ ID NO: 125 and 290 134) SEQ ID NO: 131 and 115; 135) SEQ ID NO: 131 and 121; 136) SEQ ID NO: 131 and 157; 137) SEQ ID NO: 131 and 272; 138) SEQ ID NO: 131 and 279; 139) SEQ ID NO: 128 and 282; 140) SEQ ID NO: 128 and 286; 141) SEQ ID NO: 128 and 290; 142) SEQ ID NO: 128 and 290; 143) SEQ ID NO: 131 and 115; 144) SEQ ID NO: 131 and 121; 145) SEQ ID NO: 131 and 157; 146) SEQ ID NO: 131 and 272; 147) SEQ ID NO: 131 and 279 147) SEQ ID NO: 134 and 279; 148) SEQ ID NO: 134 and 282; 149) SEQ ID NO: 134 and 286; 150) SEQ ID NO: 134 and 290; 151) SEQ ID NO: 134 and 115; 152) SEQ ID NO: 134 and 121; 153) SEQ ID NO: 134 and 157; 154) SEQ ID NO: 134 and 272; 155) SEQ ID NO: 134 and 277; 156) SEQ ID NO: 134 and 279; 157) SEQ ID NO: 134 and 279; 158) SEQ ID NO: 134 and 282; 159) SEQ ID NO: 134 and 286; 160) SEQ ID NO: 134 and 290; 161) SEQ ID NO: 137 and 115; 152) SEQ ID NO: 137 and 121; 153) SEQ ID NO: 137 and 157; 154) SEQ ID NO: 137 and 272; 155) SEQ ID NO: 137 and 277; 156) SEQ ID NO: 137 and 279; 157) SEQ ID NO: 137 and 282; 158) SEQ ID NO: 137 and 286; 159) SEQ ID NO: 137 and 290; 160) SEQ ID NO: 141 and 115; 161) SEQ ID NO: 141 and 121; 162) SEQ ID NO: 141 and 157; 162) SEQ ID NO: 141 and 272; 162) SEQ ID NO: 164) SEQ ID NO: 141 and 282; 165) SEQ ID NO: 141 and 286; 166) SEQ ID NO: 141 290; 167) SEQ ID NO: 145 and 115; 168) SEQ ID NO: 145 and 121; 169) SEQ ID NO: 145 and 157; 170) SEQ ID NO: 145 and 272; 171) SEQ ID NO: 145 and 277; 172) SEQ ID NO: 145 and 279; 173) SEQ ID NO: 145 and 282; 174) SEQ ID NO: 145 and 282; 175) SEQ ID NO: 145 and 286; 176) SEQ ID NO: 141 290; 167) SEQ ID NO: 145 and 115; 168) SEQ ID NO: 145 and 121; 169) SEQ ID NO: 145 and 157; 170) SEQ ID NO: 145 and 272; 171) SEQ ID NO: 145 and 277; 172) SEQ ID NO: 145 and 279; 173) SEQ ID NO: 145 and 282; 174) SEQ ID NO: 145 and 282; 175) SEQ ID NO: 145 and 286; 176) SEQ ID 184) SEQ ID NO: 149 and 286; 185) SEQ ID NO: 149 and 290; 186) SEQ ID NO: 153 and 115; 187) SEQ ID NO: 153 and 121; 188) SEQ ID NO: 153 and 157; 189) SEQ ID NO: 153 and 272; 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 264 and 115; 196) SEQ ID NO: 264 and 121; 197) SEQ ID NO: 264 and 157; 198) SEQ ID NO: 264 and 272; 199) SEQ ID NO: 264 and 277; 200) SEQ ID NO: 264 and 279; 201) SEQ ID NO: 264 and 282; 202) SEQ ID NO: 264 and 286; 203) SEQ ID NO: 212) SEQ ID NO: 266 and 290; 213) SEQ ID NO: 269 and 115; 214) SEQ ID NO: 269 and 121; 215) SEQ ID NO: 269 and 157; 216) SEQ ID NO: 269 and 157; 217) SEQ ID NO: 269 and 157; 218) SEQ ID NO: 269 and 157; 219) SEQ ID NO: 269 and 272; 220) SEQ ID NO: 221 and 277; 221) SEQ ID NO: 269 and 279; 222) SEQ ID NO: 269 and 282; 223) SEQ ID NO: 269 and 286; 224) SEQ ID NO: 269 and 290; 225) SEQ ID NO: 269 and 115; 226) SEQ ID NO: 269 and 121; 227) SEQ ID NO: 269 and 157; 228) SEQ ID NO: 269 and 157; 229) SEQ ID NO: 269 and 157 NO: 269 and 272; 218) SEQ ID NO: 269 and 277; 219) SEQ ID NO: 269 and 279; 219) SEQ ID NO: 269 and 282; 220) SEQ ID NO: 269 and 286; or 221) SEQ ID NO: 269 and 290, or (II) any other combination of the same antibody types as described in Tables 2 and 3. The antibody or antigen-binding fragment of any one of claims 1 to 9, wherein the VH and VL respectively comprise or consist of the amino acid sequences described below: 1) SEQ ID NOs: 23 and 27; 2) SEQ ID NOs: 23 and 37; 3) SEQ ID NOs: 31 and 27; 4) SEQ ID NOs: 31 and 37; 5) SEQ ID NOs: 35 and 27; 6) SEQ ID NOs: 35 and 37; 7) SEQ ID NOs: 36 and 27; 8) SEQ ID NOs: 36 and 37; 9) SEQ ID NOs: 43 and 27; 10) SEQ ID NOs: 43 and 37; 11) SEQ ID NOs: 83 and 87; 12) SEQ ID NOs: 83 and 193; 13) SEQ ID NOs: 179 and 87; 14) SEQ ID NOs: 17) SEQ ID NO: 181 and 87; 18) SEQ ID NO: 181 and 87; 19) SEQ ID NO: 183 and 193; 20) SEQ ID NO: 185 and 87; 21) SEQ ID NO: 185 and 87; 22) SEQ ID NO: 190 and 87; 23) SEQ ID NO: 190 and 193; 24) SEQ ID NO: 93 and 97; 25) SEQ ID NO: 93 and 225; 26) SEQ ID NO: 93 and 228; 27) SEQ ID NO: 93 and 231; 28) SEQ ID NO: 41) SEQ ID NO: 207 and 225; 42) SEQ ID NO: 207 and 228; 43) SEQ ID NO: 54) SEQ ID NO: 214 and 228; 55) SEQ ID NO: 214 and 231; 56) SEQ ID NO: 216 and 97; 57) SEQ ID NO: 216 and 225; 58) SEQ ID NO: 69) SEQ ID NO: 222 and 225; 70) SEQ ID NO: 222 and 228; 71) SEQ ID NO: 222 and 231; 72) SEQ ID NO: 102 and 105; 73) SEQ ID NO: 106 and 107; 74) SEQ ID NO: 108 and 109; 75) SEQ ID NO: 112 and 113; 76) SEQ ID NO: 114 and 115; 77) SEQ ID NO: 115 and 116; 78) SEQ ID NO: 116 and 228; 79) SEQ ID NO: 216 and 231; 80) SEQ ID NO: 218 and 97; 81) SEQ ID NO: 218 and 225; 82) SEQ ID NO: 218 and 228; 83) SEQ ID NO: 218 and 231; 84) SEQ ID NO: 220 and 97; 85) SEQ ID NO: 220 and 225; 86) SEQ ID NO: 220 and 228; 87) SEQ ID NO: 220 and 231; 88) SEQ ID NO: 222 and 97; 7) SEQ ID NO: 235 and 260; 80) SEQ ID NO: 238 and 105; 81) SEQ ID NO: 238 and 254; 82) SEQ ID NO: 238 and 257; 83) SEQ ID NO: 238 and 260; 84) SEQ ID NO: 241 and 105; 85) SEQ ID NO: 241 and 254; 86) SEQ ID NO: 241 and 257; 87) SEQ ID NO: 97) SEQ ID NO: 247 and 254; 98) SEQ ID NO: 247 and 257; 99) SEQ ID NO: 247 and 260; 100) SEQ ID NO: 249 and 105; 101) SEQ ID NO: 10) SEQ ID NO: 111 and 115; 109) SEQ ID NO: 111 and 121; 110) SEQ ID NO: 111 and 157; 111) SEQ ID NO: 111 and 272; 112) SEQ ID NO: 111 and 277; 113) SEQ ID NO: 111 and 279; 114) SEQ ID NO: 111 and 282; 115) SEQ ID NO: 111 and 286; 116) SEQ ID NOs: 111 and 290; 117) SEQ ID NOs: 125 and 115; 118) SEQ ID NOs: 125 and 121; 119) SEQ ID NOs: 125 and 157; 120) SEQ ID NOs: 125 and 272; 121) SEQ ID NOs: 125 and 277; 122) SEQ ID NOs: 125 and 279; 123) SEQ ID NOs: 125 and 282; 124) SEQ ID NOs: 125 and 286; 125) SEQ ID NOs: 125 and 290; 126) SEQ ID NOs: 128 and 115; 127) SEQ ID NOs: 128 and 121; 128) SEQ ID NOs: 128 and 157; 129) SEQ ID NOs: 129 and 286; 136) SEQ ID NO: 131 and 272; 137) SEQ ID NO: 131 and 277; 138) SEQ ID NO: 131 and 279; 139) SEQ ID NO: 131 and 282; 140) SEQ ID NO: 131 and 286; 141) SEQ ID NO: 131 and 290; 142) SEQ ID NO: 143) SEQ ID NO: 144) SEQ ID NO: 145) SEQ ID NO: 146) SEQ ID NO: 147; 148) SEQ ID NO: 149) SEQ ID NO: 150) SEQ ID NO: 151 and 157; 149) SEQ ID NO: 152 and 158; 153) SEQ ID NO: 154 and 159; 160) SEQ ID NO: 155 and 159; 161) SEQ ID NO: 156 and 157; 162) SEQ ID NO: 157 and 159; 163) SEQ ID NO: 156 and 159; 143) SEQ ID NO: 134 and 121; 144) SEQ ID NO: 134 and 157; 145) SEQ ID NO: 134 and 272; 146) SEQ ID NO: 134 and 277; 147) SEQ ID NO: 134 and 279; 148) SEQ ID NO: 134 and 282; 149) SEQ ID NO: 134 and 286; 150) SEQ ID NO: 134 and 290; 151) SEQ ID NO: 137 and 115; 152) SEQ ID NO: 137 and 121; 153) SEQ ID NO: 137 and 157; 154) SEQ ID NO: 137 and 272; 155) SEQ ID NO: 137 and 277; 156) SEQ ID NO: 137 and 279; 157) SEQ ID NO: 137 and 282; 158) SEQ ID NO: 137 and 286; 159) SEQ ID NO: 137 and 290; 160) SEQ ID NO: 141 and 115; 161) SEQ ID NO: 141 and 121; 162) SEQ ID NO: 141 and 157; 162) SEQ ID NO: 141 and 272; 162) SEQ ID NO: 141 and 277; 163) SEQ ID NO: 141 and 279; 164) SEQ ID NO: 141 and 282; 165) SEQ ID NO: 141 and 286; 166) SEQ ID NO: 141 290; 167) SEQ ID NO: 176) SEQ ID NO: 145 and 290; 177) SEQ ID NO: 149 and 115; 178) SEQ ID NO: 149 and 121; 179) SEQ ID NO: 149 and 157; 170) SEQ ID NO: 149 and 272; 171) SEQ ID NO: 149 and 277; 172) SEQ ID NO: 149 and 279; 173) SEQ ID NO: 149 and 282; 174) SEQ ID NO: 149 and 282; 175) SEQ ID NO: 149 and 286; 176) SEQ ID NO: 149 and 290; 177) SEQ ID NO: 149 and 115; 178) SEQ ID NO: 149 and 121; 179) SEQ ID NO: 149 and 157; 180) SEQ ID NO: 149 and 272; 181) SEQ ID NO: 149 and 277 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 153 and 115; 187) SEQ ID NO: 153 and 121; 188) SEQ ID NO: 153 and 157; 189) SEQ ID NO: 153 and 272; 190) SEQ ID NO: 153 and 277; 191) SEQ ID NO: 153 and 279; 192) SEQ ID NO: 153 and 282; 193) SEQ ID NO: 153 and 286; 194) SEQ ID NO: 153 and 290; 195) SEQ ID NO: 264 and 115; 196) SEQ ID NO: 264 and 121; 197) SEQ ID NO: 264 and 157; 198) SEQ ID NO: 264 and 272; 199) SEQ ID NO: 264 and 277; 200) SEQ ID NO: 264 and 279; 201) SEQ ID NO: 264 and 282; 202) SEQ ID NO: 264 and 286; 203) SEQ ID NO: 264 and 290; 204) SEQ ID NO: 266 and 115; 205) SEQ ID NO: 266 and 121; 206) SEQ ID NO: 266 and 157; 207) SEQ ID NO: 266 and 272; 208) SEQ ID NO: 269 and 272; 218) SEQ ID NO: 269 and 277; 219) SEQ ID NO: 269 and 279; 210) SEQ ID NO: 266 and 282; 211) SEQ ID NO: 266 and 286; 212) SEQ ID NO: 266 and 290; 213) SEQ ID NO: 269 and 115; 214) SEQ ID NO: 269 and 121; 215) SEQ ID NO: 269 and 157; 216) SEQ ID NO: 269 and 157; 217) SEQ ID NO: 269 and 272; 218) SEQ ID NO: 269 and 277; 219) SEQ ID NO: 269 and 279; 219) SEQ ID NO: 269 and 282; 220) SEQ ID NO: 269 and 286; or 221) SEQ ID NO: 269 and 290. An antibody or antigen-binding fragment of any of claims 1 to 10, which: (i)   recognizes an epitope in the spike protein of two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses; (ii)  is capable of blocking the interaction between the spike protein of two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses and one or more cell surface receptors corresponding thereto, wherein, optionally, the cell surface receptor comprises human ACE2; (iii) recognizes an epitope retained in the spike protein of two or more, three or more, four or more, or five or more severe acute respiratory syndrome beta coronaviruses; (iv) Cross-reactive against two or more, three or more, four or more, or five or more SARS-betacoronaviruses, including, where appropriate, one or more clade 1b SARS-betacoronaviruses; or (v) any combination of (i) to (iv). The antibody or antigen-binding fragment of any one of claims 1 to 11, which is of IgG, IgA, IgM, IgE, or IgD isotype. The antibody or antigen-binding fragment of claim 12, which is of IgG isotype selected from IgG1, IgG2, IgG3, and IgG4, and is preferably of IgG1 isotype. The antibody or antigen-binding fragment of any one of claims 1 to 13, which is human, humanized, or chimeric. The antibody or antigen-binding fragment of any one of claims 1 to 14, wherein the antibody or the antigen-binding fragment comprises a human antibody, a monoclonal antibody, a purified antibody, a single-chain antibody, Fab, Fab', F(ab')2, Fv, scFv, or scFab. The antibody or antigen-binding fragment of claim 15, wherein the scFv comprises more than one VH domain and more than one VL domain. The antibody or antigen-binding fragment of any one of claims 1 to 16, wherein the antibody or antigen-binding fragment is a multispecific antibody or antigen-binding fragment. The antibody or antigen-binding fragment of claim 17, wherein the antibody or antigen-binding fragment is a bispecific antibody or antigen-binding fragment. The antibody or antigen-binding fragment of claim 18, comprising: a first VH and a first VL; and a second VH and a second VL, wherein the first VH and VL comprise i) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with the amino acid sequence described in SEQ ID NO: 23 and 27, respectively; ii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with the amino acid sequence described in SEQ ID NO: NO. having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with the amino acid sequence described in: 31, 35, 36, or 43 and 37, respectively; 14 and 15, respectively; 16 and 17, respectively; 18 and 19, respectively; 20 and 21, respectively; 20 and 22, respectively; iii) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 83, 179, 181, 183, 185, 188, or 190 and any one of 87 or 193; iv) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and any one of 97, 225, 228, or 231; v) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 102, 235, 238, 241, 243, 245, 247, 249, or 251 and any one of 105, 254, 257, or 260; or vi) with the following SEQ ID NO. The amino acid sequence described has at least 85% (i.e. 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with an amino acid sequence: 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of 115, 121, 157, 272, 277, 279, 282, 286, or 290; and wherein the second VH and VL comprise i) respectively with SEQ ID NO: 23 and 27 have at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs.; ii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs.: 31, 35, 36, or 43, respectively, and 37; 14 and 15, respectively; 16 and 17, respectively; 18 and 19, respectively; 20 and 21, respectively; 20 and 22, respectively; iii) an amino acid sequence having at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity to the amino acid sequences described in the following SEQ ID NOs. NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 83, 179, 181, 183, 185, 188, or 190 and any one of 87 or 193; iv) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 93, 197, 201, 204, 207, 210, 212, 214, 216, 218, 220, or 222 and any one of 97, 225, 228, or 231; v) with the following SEQ ID NO. The amino acid sequence has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with any one of 102, 235, 238, 241, 243, 245, 247, 249, or 251 and any one of 105, 254, 257, or 260; or vi) with the following SEQ ID The amino acid sequence described in NO. has at least 85% (i.e., 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%) identity with the amino acid sequence: any one of 111, 125, 128, 131, 134, 137, 141, 145, 149, 153, 264, 266, or 269 and any one of 115, 121, 157, 272, 277, 279, 282, 286, or 290; wherein the first VH and the second VL are different from the second VH and VL; wherein the first VH and the first VL together form a first antigen binding site; and wherein the second VH and the second VL together form a second antigen binding site. The antibody or antigen-binding fragment of any one of claims 1 to 19, wherein the antibody or antigen-binding fragment comprises an Fc polypeptide or fragment thereof, the Fc polypeptide or fragment thereof comprises the substitution mutations M428L/N434S, M428L/N434A, G236A/A330L/I332E/M428L/N434S, or G236A/A330L/I332E/M428L/N434A, wherein, optionally, the antibody or antigen-binding fragment is of IgG1 isotype and comprises or consists of an Fc polypeptide or fragment thereof, the Fc polypeptide or fragment thereof comprises or consists of: and SEQ ID NO: 80, optionally other than naturally occurring variants thereof; or the Fc polypeptide or fragment thereof comprises or consists of an amino acid sequence as set forth in SEQ ID NOs: 52 to 80. An isolated polynucleotide encoding the antibody or antigen-binding fragment of any one of claims 1 to 20. A recombinant vector comprising the polynucleotide of any claim 21. A host cell comprising the polynucleotide of claim 21 and/or the vector of claim 22, wherein the polynucleotide is heterologous to the host cell. A human B cell comprising the polynucleotide of claim 21 and/or the vector of claim 22, wherein the polynucleotide is heterologous to the human B cell and/or wherein the human B cell is immortalized. A composition comprising: (i)   the antibody or antigen-binding fragment of any one of claims 1 to 20; (ii)  the polynucleotide of claim 21; (iii) the recombinant vector of claim 22; (iv) the host cell of claim 23; and/or (v)  the human B cell of claim 24, and a pharmaceutically acceptable excipient, carrier, or diluent. The composition of claim 25, comprising two or more antibodies or antigen-binding fragments, wherein the first antibody or antigen-binding fragment and the second antibody or antigen-binding fragment respectively comprise, or the multispecific antibody or antigen-binding fragment comprises CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3, and optionally VH and VL, which are based on: (i) any S3A3 antibody and any S3A19 antibody; (ii) any S3A3 antibody and sotorovimab; (iii) any S3A3 antibody and S2K146; (iv) any S3A3 antibody and S2X259; (v) any S3A3 antibody and any S2X324 antibody; (vi) any S3A3 antibody and S309; (vi) any S3A19 antibody and sotorovimab; (vii) any S3 A19 antibody and S2K146; (viii) any S3A19 antibody and S2X259; (ix) any S3A19 antibody and any S2X324 antibody; (x) any S3A19 antibody and S309; (xi) any S3I2 antibody and any S3A3 antibody; (xii) any S3I2 antibody and any S3A19 antibody; (xiii) any S3I2 antibody and sotoviromab; ( (xiv) any S3I2 antibody and S2K146; (xv) any S3I2 antibody and S2X259; (xvi) any S3I2 antibody and any S2X324 antibody; (xvii) any S3I2 antibody and S309; (xviii) any S3I2 antibody and any S3O13 antibody; (xix) any S3I2 antibody and any S3L17 antibody; (xx) any S3O13 antibody (xxii) any S3O13 antibody and sotoviromab; (xxiii) any S3O13 antibody and S2K146; (xxiv) any S3O13 antibody and S2X259; (xxv) any S3O13 antibody and any S2X324 antibody; (xxvi) any S3O13 antibody and S309; (xxvii) any S3O13 antibody and any S3L17 antibody; (xxviii) any S3L17 antibody and any S3A3 antibody; (xxix) any S3L17 antibody and any S3A19 antibody; (xxx) any S3L17 antibody and sotoviromab; (xxxi) any S3L17 antibody and S2K146; (xxxii) any S3L17 antibody and S 2X259; (xxxiii) any S3L17 antibody and any S2X324 antibody; (xxxiv) any S3L17 antibody and S309; (xxxv) any S2V29 antibody and any S3A3 antibody; (xxxvi) any S2V29 antibody and any S3A19 antibody; (xxxvii) any S2V29 antibody and sotoviromab; (xxxviii) any S2V29 antibody and S2K146; (xxxix) any S2V29 antibody and S2X259; (xl) any S2V29 antibody and any S2X324 antibody; (xli) any S2V29 antibody and S309; (lxlii) any S2V29 antibody and any S3L17 antibody; and (xliii) any S2V29 antibody and any S3O13 antibody, or any antigen-binding fragment thereof. A composition comprising a polynucleotide as claimed in claim 25 or claim 26 encapsulated in a carrier molecule, wherein the carrier molecule optionally comprises a lipid, a lipid-derived delivery vehicle, such as a liposome, a solid lipid nanoparticle, an oily suspension, a submicron lipid emulsion, a lipid microbubble, an inverse lipid micelle, a cochlear liposome, a lipid microtubule, a lipid microcylinder, a lipid nanoparticle (LNP), or a nanoscale platform. A method for treating severe acute respiratory syndrome beta coronavirus infection in an individual, the method comprising administering to the individual an effective amount of (i)   an antibody or antigen-binding fragment as described in any one of claims 1 to 20; (ii)  a polynucleotide as described in claim 21; (iii) a recombinant vector as described in claim 22; (iv) a host cell as described in claim 23; and/or (v)  a human B cell as described in claim 24, and/or (vi) a composition as described in any one of claims 25 to 271. An antibody or antigen-binding fragment as described in any one of claims 1 to 20, a polynucleotide as described in claim 21, a recombinant vector as described in claim 22, a host cell as described in claim 23, a human B cell as described in claim 24, and/or a composition as described in any one of claims 25 to 27, for use in a method for treating severe acute respiratory syndrome beta-coronavirus infection in an individual. An antibody or antigen-binding fragment as described in any one of claims 1 to 20, a polynucleotide as described in claim 21, a recombinant vector as described in claim 22, a host cell as described in claim 23, a human B cell as described in claim 24, and/or a composition as described in any one of claims 25 to 27, which is used to prepare a medicament for treating severe acute respiratory syndrome beta-coronavirus infection in an individual. A kit comprising a liquid composition and instructions for use thereof in treating SARS-CoV-2 infection in an individual, wherein the liquid composition comprises the antibody or antigen-binding fragment of any one of claims 1 to 20 or 29 to 30. A method for in vitro diagnosis of severe acute respiratory syndrome beta coronavirus infection (e.g., infection caused by SARS-CoV-2), the method comprising: (i)   contacting a sample from an individual with an antibody or antigen-binding fragment as described in any one of claims 1 to 20; and (ii)  detecting a complex comprising an antigen and the antibody, or comprising an antigen and the antigen-binding fragment. A method for producing the antibody or antigen-binding fragment of any one of claims 1 to 20 or claims 29 to 30, wherein the method comprises culturing a host cell expressing the antibody or antigen-binding fragment under conditions and for a time sufficient to produce the antibody or antigen-binding fragment.