CN116854803B - IFN-a2 site mutant fusion protein and application thereof in preparation of anti-respiratory virus immune preparation - Google Patents
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Abstract
The invention discloses IFN-a2 locus mutation fusion protein and application thereof in preparation of an anti-respiratory virus immune preparation, belonging to the technical fields of bioengineering and medicine. The 82 nd position of the amino acid sequence of the IFN-a2 site mutant fusion protein is mutated into E. The IFN-a2 site mutant fusion protein provided by the invention has the advantages that through the sequence modification of an IFN-alpha 2 receptor binding site, a specific amino acid site on IFN-alpha 2 is mutated into a corresponding IFN-alpha 4 amino acid site, and the IFN-alpha 2 mutant is subjected to antiviral capacity measurement and signal transduction pathway detection, so that the mutant has better antiviral capacity compared with non-mutated IFN-alpha 2, and can reduce viral protein replication in a limited way.
Description
Technical Field
The invention relates to the technical field of bioengineering and medicine, in particular to IFN-a2 site mutation fusion protein and application thereof in preparation of anti-respiratory virus immune preparations.
Background
Type I IFN is the primary response cytokine of virus-infected cells and has typical antiviral effects. IFN-alpha is the largest class of interferon systems and comprises multiple subtypes by itself, with the human genome known to contain 13 IFN-alpha subtypes, however, only a limited interferon class is currently used clinically. IFN-alpha 2 is taken as a subtype with the largest research, is approved to enter the diagnosis and treatment scheme of China from the eighties of the last century, and is mainly used for treating diseases caused by virus infection such as chronic hepatitis B virus infection and the like. In the HIV anti-infection research, IFN-alpha 2 is the most effective anti-HIV IFN so far, and the combination of anti-HIV medicaments can effectively reduce the RNA level of HIV latent viruses, and the research proves that the combination of IL-21 and IFN-alpha 2 can effectively reduce the inflammation level and virus replication in rhesus monkeys infected by SIV, and still obviously inhibit SIV virus rebound after the antiviral medicaments stop. In the past study of the infection of the pediatric syncytial virus, the supplement of exogenous interferon is necessary in the early stage of the disease course, thus effectively enhancing the clear ability of immune cells and achieving the purpose of controlling the progress of the disease course. At present, IFN-alpha 2 has little research in anti-respiratory virus immune application and has potential for further development.
More similar structures exist between IFN-alpha of different subtypes, and at the same time, about one third of specific non-conserved sequences are also possessed, and the IFN-alpha of different subtypes regulate downstream reaction and bypass signal paths through interaction with two different subunits IFNAR1 and IFNAR2 of the type I IFN receptor. However, the difference in binding force and binding site between IFN- α of different subtypes and IFNAR1 and IFNAR2 are different, and thus, the downstream pathway activation mode and activity degree are different among the subtypes. The existing research has basically analyzed the amino acid site related to the binding of interferon receptor in the interferon amino acid sequence, and provides a foundation for interferon engineering research. Through mutation of IFN-alpha local site, the binding capacity between the IFN-alpha and IFN receptor subunit can be changed, so that the effect of strengthening or weakening the response of downstream channels is achieved.
Disclosure of Invention
The invention aims to provide IFN-a2 site mutant fusion protein and application thereof in preparation of anti-respiratory virus immune preparations, so as to solve the problem of how to mutate IFN-alpha local sites, and change the binding capacity between the IFN-alpha local site and IFN receptor subunits, thereby achieving the effect of strengthening or weakening downstream pathway response.
The technical scheme for solving the technical problems is as follows:
the invention provides an IFN-a2 site mutant fusion protein, wherein the 82 nd site of the amino acid sequence of the IFN-a2 site mutant fusion protein is mutated into E.
Further, in the IFN-a2 site mutant fusion protein, the amino acid sequence of the IFN-a2 site mutant fusion protein is SEQ ID NO: 1.
The invention also provides a preparation method of the IFN-a2 site mutant fusion protein, which comprises the following steps:
designing a primer pair containing mutant bases, and carrying out PCR amplification on IFN-a2 to obtain IFN-a2-82E gene fragments;
performing enzyme digestion treatment on the IFN-a2-82E gene fragment, converting enzyme digestion products into escherichia coli competent DH5 alpha cells for amplification, and extracting to obtain recombinant expression plasmids;
transfecting the recombinant expression plasmid into 293t cells, centrifuging the culture solution after 48 hours of culture, removing precipitates, separating and purifying the binding protein, eluting the binding protein under acidic conditions, and neutralizing with alkaline solution to obtain the purified IIFN-a2 site mutant fusion protein.
Further, in the preparation method of the IFN-a2 site mutant fusion protein, the primer pair has the sequence as follows:
primer F GAAACCCTGCTGGAGAAGTTCTACACCGAGCTGTATC;
primer R GTAGAACTTCTCCAGCAGGGTTTCGTCCCAAGCGGCGC.
Further, in the preparation method of the IFN-a2 site mutant fusion protein, the DpnI enzyme is adopted to carry out enzyme digestion treatment on the IFN-a2-82E gene fragment.
Further, in the IFN-a2 site mutant fusion Protein preparation method, protein G purification column binding Protein is adopted.
Further, in the method for preparing the IFN-a2 site mutant fusion protein, the PCR amplification conditions are as follows: .
Further, in the preparation method of the IFN-a2 site mutant fusion protein, the acidic conditions are as follows: 0.1M glycine,pH 2.5.
Further, in the IFN-a2 site mutant fusion protein preparation method, the alkaline conditions are as follows: 1M Tris, pH 8.5.
The invention also provides the application of the IFN-a2 site mutant fusion protein or the IFN-a2 site mutant fusion protein prepared by the preparation method in preparation of anti-respiratory virus immune preparations.
The invention also provides an anti-respiratory virus immune preparation, which comprises the IFN-a2 site mutant fusion protein or the IFN-a2 site mutant fusion protein prepared by the preparation method.
The invention has the following beneficial effects:
the IFN-a2 site mutant fusion protein provided by the invention has the advantages that through the sequence modification of an IFN-alpha 2 receptor binding site, a specific amino acid site on IFN-alpha 2 is mutated into a corresponding IFN-alpha 4 amino acid site, and the IFN-alpha 2 mutant is subjected to antiviral capacity measurement and signal transduction pathway detection, so that the mutant has better antiviral capacity compared with non-mutated IFN-alpha 2, and can reduce viral protein replication in a limited way.
According to the invention, the 82 nd amino acid of IFN-a2 is mutated into E to obtain IFN-a2 site mutation fusion protein, so that the affinity between the IFN-a2 site mutation fusion protein and an interferon receptor is improved, the antiviral capability is enhanced, the problems of complicated preparation use, short timeliness and limited application scene can be effectively solved, and the broad-spectrum antiviral property is shown, so that the thought is provided for preparing a novel anti-respiratory tract virus immune preparation.
Drawings
In order to more clearly illustrate the technical solutions of the exemplary embodiments of the present invention, the drawings that are needed in the examples will be briefly described below, it being understood that the following drawings only illustrate some examples of the present invention and therefore should not be considered as limiting the scope, and that other related drawings may be obtained from these drawings without inventive effort for a person skilled in the art. In the drawings:
FIG. 1 shows the results of phosphorylation of STAT1 by IFN alpha 2-E fusion proteins in example 2 of the present invention;
FIG. 2 shows the result of inhibiting replication of influenza virus H1N1 by IFN alpha 2-E fusion protein of example 3 of the present invention;
FIG. 3 shows the second result of inhibiting replication of influenza virus H1N1 by IFN alpha 2-E fusion protein of example 3 of the present invention.
Detailed Description
For the purpose of making apparent the objects, technical solutions and advantages of the present invention, the present invention will be further described in detail with reference to the following examples and the accompanying drawings, wherein the exemplary embodiments of the present invention and the descriptions thereof are for illustrating the present invention only and are not to be construed as limiting the present invention. The specific conditions are not noted in the examples and are carried out according to conventional conditions or conditions recommended by the manufacturer. The reagents or apparatus used were conventional products commercially available without the manufacturer's attention.
The technical scheme of the invention is as follows:
an IFN-a2 site mutant fusion protein, wherein the amino acid sequence of said IFN-a2 site mutant fusion protein is E at position 82.
Further, the IFN-a2 site mutant fusion protein has an amino acid sequence shown in SEQ ID NO: 1.
The SEQ ID NO:1 is:
CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLEKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKEEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK。
in the early anti-respiratory virus immune application research, the inventor can effectively inhibit virus replication by using IFN-alpha 4, and the IFN-alpha 4 shows stronger anti-infection capability under the same using concentration. Accordingly, further by aligning the amino acid sequences of IFN-. Alpha.2 and IFN-. Alpha.4, the amino acid sites to which IFN-. Alpha.binds to IFNAR1 and IFNAR2 were analyzed, and a difference of 6 amino acid sites was found between the two. In combination with earlier-stage research, the IFN-alpha 2 is subjected to amino acid site modification, a specific amino acid site on the IFN-alpha 2 is mutated into a corresponding IFN-alpha 4 amino acid site, and the IFN-alpha 2 mutant is subjected to antiviral capacity measurement and signal transduction pathway detection, so that the mutant has better antiviral capacity and can reduce viral protein replication in a limited manner compared with the non-mutated IFN-alpha 2. The research result enriches the cognition of IFN-alpha antiviral, and provides a new research thought and evidence for developing new antiviral preparations.
A method for preparing an IFN-a2 site mutant fusion protein comprising:
designing a primer pair containing mutant bases, and carrying out PCR amplification on IFN-a2 to obtain IFN-a2-82E gene fragments;
wherein, the primer pair has the sequence as follows:
primer F GAAACCCTGCTGGAGAAGTTCTACACCGAGCTGTATC;
primer R GTAGAACTTCTCCAGCAGGGTTTCGTCCCAAGCGGCGC.
The conditions for PCR amplification were: 98 ℃ for 3min, and 35 cycles are carried out: 98℃for 10s,55℃for 15s,72℃for 35s; after the cycle was completed, the temperature was 72℃for 5min.
Performing enzyme digestion treatment on the IFN-a2-82E gene fragment by adopting DpnI enzyme, converting enzyme digestion products into escherichia coli competent DH5 alpha cells for amplification, culturing at 37 ℃ for 14 hours, and extracting to obtain recombinant expression plasmids;
the recombinant expression plasmid is transfected into 293t cells, the culture medium is replaced by an Expi293 expression culture medium after transfection for 6 hours, and 5% CO is added at 37 DEG C 2 After culturing in an incubator for 48 hours, the culture broth was centrifuged to remove the precipitate, and the bound Protein was purified by Protein G purification column separation, and the bound Protein was eluted under acidic conditions (0.1M glycine,pH 2.5) and neutralized with alkaline solution (1M Tris, pH 8.5) to obtain the purified IFN-a2 fusion Protein.
The application of the respiratory tract virus infection related gene IFN-a2 fusion protein in preparing an anti-respiratory tract virus immune preparation.
For further explanation of the present invention, the following description will be given with reference to examples of IFN-a2 fusion proteins, which are genes related to infection by a respiratory virus, provided by the present invention, but it should be understood that these examples are carried out on the premise of the technical scheme of the present invention, and detailed embodiments and specific procedures are given, only for further explanation of the features and advantages of the present invention, not limitation of the claims of the present invention, and the scope of protection of the present invention is not limited to the following examples.
The IFN-a2 site mutant fusion protein of the gene related to respiratory tract virus infection is marked as IFN alpha 2-E fusion protein.
EXAMPLE 1 preparation of IFN alpha 2-E fusion proteins
Designing a primer pair IFN-a2 containing mutant bases, and carrying out PCR amplification to obtain an IFN-a2-82E gene fragment; wherein, the conditions of PCR amplification are: 98 ℃ for 3min; enter 35 cycles: 98℃for 10s,55℃for 15s,72℃for 35s; after the cycle was completed, the temperature was 72℃for 5min.
Wherein, the sequence of the primer is as follows:
primer F GAAACCCTGCTGGAGAAGTTCTACACCGAGCTGTATC;
primer R GTAGAACTTCTCCAGCAGGGTTTCGTCCCAAGCGGCGC.
Performing enzyme digestion treatment on the IFN-a2-82E gene fragment by adopting DpnI enzyme, converting enzyme digestion products into escherichia coli competent DH5 alpha cells for amplification, and culturing at 37 ℃ for 14 hours to extract recombinant expression plasmids;
the recombinant expression plasmid is transfected into 293t cells, the culture medium is replaced by an Expi293 expression culture medium after transfection for 6 hours, and 5% CO is added at 37 DEG C 2 After the culture is continued in the incubator for 48 hours, the culture solution is centrifuged to remove the precipitate, after the culture is completed for 48 hours, the culture solution is centrifuged to remove the precipitate, the Protein G purification column is used for separating and purifying the binding Protein, the binding Protein is eluted under the acidic condition (0.1M glycine,pH 2.5), and then the alkaline solution (1M Tris, pH 8.5) is used for neutralization to obtain the purified IFN alpha 2-E fusion Protein.
Example 2 ability of IFN alpha 2-E fusion protein to phosphorylate STAT1
The interferon is combined with an interferon receptor on the surface of a cell, so that the intracellular segment of the receptor is recruited to bind to TYK/JAK kinase and is phosphorylated, STAT1 is further phosphorylated, and the phosphorylated STAT1 dimer is translocated to the nucleus, so that the expression of a downstream interferon stimulation gene is initiated, and further the antiviral effect is exerted.
To verify if IFN alpha 2-E has better effect of phosphorylating STAT1, this embodiment adopts A549 cells plated on 12-well plates, 1mL of IFN alpha 2, IFN alpha 2-E and IFN alpha 4 fusion protein at a concentration of 5nM, respectively, was used in CO 2 After 1h of culture in a cell incubator, influenza virus nucleoprotein N was analyzed by western immunoblottingExpression of P. The primary antibodies used are anti-pSTAT1-mouse (Abcam, ab281999, 1:1000), anti-pSTAT1-mouse (CST, 14994, 1:1000), anti-ACTIN-mouse (CST, 3700, 1:1000), respectively; the secondary antibody is anti-rabit-HRP (CST, 7074, 1:4000), anti-mu-HRP (CST, 7076, 1:4000).
The results are shown in FIG. 1, all three can phosphorylate STAT1, the IFN alpha 2 has the weakest ability to phosphorylate STAT1, and the IFN alpha 2-E can obviously enhance the ability of IFNA alpha 2 to phosphorylate STAT1, so that the variant IFN alpha 2-E has better ability of stimulating the expression of interferon stimulation genes.
Example 3IFN alpha 2-E fusion protein inhibits replication of influenza virus H1N1
The lung epithelial cell line A549 is derived from human non-small cell lung cancer epithelial cells and is a main cell model for researching influenza virus infection.
To verify the effect of IFN alpha 2-E on infection with different subtypes of influenza virus, this example employs plating A549 on a 12-well plate using 1mL of IFN alpha 2, IFN alpha 2-E and IFN alpha 4 fusion protein at a concentration of 5nM in CO 2 The cells were cultured in a cell culture incubator for 24 hours, after the medium was aspirated, the cells were washed once with PBS, and treated with 400. Mu.L of DMEM containing H1N1 influenza virus for 2 hours, with an average number of virus-infected particles (MOI) per cell of 0.01. After 2h, the virus-containing medium was aspirated, and 1ml of DMEM containing 2% FBS was added to continue culturing the cells for 24h, followed by harvesting the cells, and the expression of influenza virus nucleoprotein NP was analyzed by western immunoblotting. The primary antibodies used were anti-NP-rabit (Yiqiaoshenzhou, 11675-T62, 1:5000), anti-GAPDH-rabit (CST, 2118, 1:1000); the secondary antibody is anti-rabit-HRP (CST, 7074, 1:4000).
The results are shown in fig. 2 and 3, compared with the virus control, the three can obviously inhibit the replication of influenza virus H1N1 sub-strain CA04 and PR8 nucleoprotein NP (fig. 2), the capacity of IFN alpha 2-E for resisting influenza virus nucleoprotein NP replication of IFN alpha 4 is equivalent, and the inhibition capacity of IFN alpha 2-E for CA04 sub-strain replication is obviously stronger than IFN alpha 2, so that the IFN alpha 2-E variant has better anti-influenza virus effect.
The foregoing description of the embodiments has been provided for the purpose of illustrating the general principles of the invention, and is not meant to limit the scope of the invention, but to limit the invention to the particular embodiments, and any modifications, equivalents, improvements, etc. that fall within the spirit and principles of the invention are intended to be included within the scope of the invention.
Claims (3)
1. An IFN-a2 site mutant fusion protein, which is characterized in that the amino acid sequence of the IFN-a2 site mutant fusion protein is shown as SEQ ID NO:1, and the 82 nd position of the amino acid sequence of the IFN-a2 site mutant fusion protein is mutated into E.
2. Use of the IFN-a2 site mutant fusion protein of claim 1 for the preparation of an anti-respiratory virus immunizing formulation.
3. An anti-respiratory virus immunizing formulation comprising the IFN-a2 site mutant fusion protein of claim 1.
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| CN1944463A (en) * | 2006-10-30 | 2007-04-11 | 中国科学技术大学 | Fusion protein with alpha-interferon activity and its coded gene and use |
| CN105384828A (en) * | 2015-12-18 | 2016-03-09 | 中国科学技术大学 | Long-acting interferon-alpha and transformation method thereof |
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| CN1944463A (en) * | 2006-10-30 | 2007-04-11 | 中国科学技术大学 | Fusion protein with alpha-interferon activity and its coded gene and use |
| CN105384828A (en) * | 2015-12-18 | 2016-03-09 | 中国科学技术大学 | Long-acting interferon-alpha and transformation method thereof |
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