A broad-spectrum neutralizing antibody P5-2H11 against SARS-CoV-2 and its application

By screening and preparing P5-2H11 antibodies, the problem of poor neutralizing antibody efficacy against novel coronavirus mutant strains in existing technologies has been solved, achieving effective neutralization against multiple novel coronavirus mutant strains and providing a broad-spectrum means of virus prevention and control.

CN115960221BActive Publication Date: 2026-03-06TSINGHUA UNIVERSITY +1
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2023-01-30
Publication Date
2026-03-06

AI Technical Summary

Technical Problem

In existing technologies, neutralizing antibodies against novel coronavirus mutant strains are not very effective, especially the neutralizing activity of inactivated vaccine immune serum and mRNA vaccine immune serum against South African mutant strains has decreased. Many monoclonal antibodies have weakened or lost their neutralizing activity against mutant strains. There is an urgent need to develop broad-spectrum neutralizing antibodies against SARS-CoV-2 to address the challenge of naturally mutated strains of the virus.

Method used

P5-2H11 antibodies were screened and prepared. Memory B cells were screened from peripheral blood mononuclear cells of infected individuals to obtain monoclonal antibodies that specifically bind to the SARS-CoV-2 spike protein. P5-2H11 antibodies have broad-spectrum neutralizing ability and can effectively neutralize wild-type novel coronavirus and various natural variants.

Benefits of technology

The P5-2H11 antibody exhibits strong neutralizing ability against various novel coronavirus mutant strains, providing a broad-spectrum means of virus prevention and control, and has important application value.

✦ Generated by Eureka AI based on patent content.

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Abstract

This invention discloses a broad-spectrum neutralizing antibody P5-2H11 against SARS-CoV-2 and its applications. The invention provides an IgG antibody, named P5-2H11 antibody, composed of a light chain and a heavy chain; the CDR1, CDR2, and CDR3 in the variable region of the heavy chain are as shown in positions 26-33, 51-57, and 96-108 of SEQ ID NO: 1, respectively; the CDR1, CDR2, and CDR3 in the variable region of the light chain are as shown in positions 26-34, 52-54, and 91-100 of SEQ ID NO: 4, respectively. The P5-2H11 antibody provided by this invention has a broad-spectrum neutralizing effect against SARS-CoV-2, exhibiting strong neutralizing ability against both wild-type novel coronavirus and naturally occurring variants. This invention has significant application value for the prevention and control of the novel coronavirus and will have profound social implications.
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Description

Technical Field

[0001] This invention belongs to the field of biotechnology and relates to a broad-spectrum neutralizing antibody P5-2H11 that neutralizes SARS-CoV-2 and its applications. Background Technology

[0002] The main symptoms of novel coronavirus infection are low-grade fever, fatigue, and dry cough. A few patients may also experience upper respiratory and digestive symptoms such as nasal congestion, runny nose, and diarrhea. Severe cases can develop into acute respiratory distress syndrome, septic shock, metabolic acidosis, coagulation dysfunction, and multiple organ failure. The novel coronavirus (SARS-CoV-2) belongs to the β-coronavirus genus.

[0003] During its transmission, SARS-CoV-2 has undergone numerous mutations, enhancing its transmissibility and immune evasion. Currently, the main circulating naturally occurring mutant strains include the Alpha strain discovered in the UK, the Beta strain in South Africa, and the Gamma strain in Brazil. Vaccination against the novel coronavirus has also been affected. The neutralizing activity of inactivated vaccine serum against the South African mutant strain has decreased by half, and the neutralizing activity of mRNA vaccine serum against the South African mutant strain has decreased by approximately tenfold. Many monoclonal antibodies have also shown weakened or lost neutralizing activity against the mutant strain.

[0004] Monoclonal antibodies can be mass-produced industrially. Their high affinity and specificity for antigen binding significantly reduce adverse reactions in clinical applications. Furthermore, antibody molecules can be modified to increase their antiviral efficacy. Antibodies, with their specificity and flexibility of use, are a very promising tool in the treatment of infectious diseases. Currently, there is an urgent need to address the challenges posed by naturally occurring mutant strains of the novel coronavirus. Developing broad-spectrum human monoclonal antibodies against the novel coronavirus will provide more effective prevention and treatment for infections caused by these naturally occurring mutant strains. Summary of the Invention

[0005] The purpose of this invention is to provide a broad-spectrum neutralizing antibody P5-2H11 that neutralizes SARS-CoV-2 and its applications.

[0006] This invention provides an IgG antibody, named P5-2H11 antibody, composed of a light chain and a heavy chain; the CDR1, CDR2, and CDR3 in the variable region of the heavy chain are as shown in positions 26-33, 51-57, and 96-108 of SEQ ID NO: 1, respectively; the CDR1, CDR2, and CDR3 in the variable region of the light chain are as shown in positions 26-34, 52-54, and 91-100 of SEQ ID NO: 4, respectively.

[0007] Specifically, the heavy chain variable region is shown in SEQ ID NO: 1.

[0008] Specifically, the light chain variable region is shown in SEQ ID NO: 4.

[0009] Specifically, the heavy chain is either (a) or (b) as follows: (a) the protein represented by positions 20-468 of SEQ ID NO: 2; (b) the protein represented by SEQ ID NO: 2.

[0010] Specifically, the light chain is either (c) or (d) as follows: (c) the protein shown in positions 20-236 of SEQ ID NO: 5; (d) the protein shown in SEQ ID NO: 5.

[0011] The gene encoding the IgG antibody is also within the scope of protection of this invention.

[0012] Specifically, the gene encoding the heavy chain is as follows (1) or (2):

[0013] (1) The DNA molecule represented by nucleotides 949-2298 in SEQ ID NO: 3;

[0014] (2) The DNA molecule represented by nucleotides 892-2298 in SEQ ID NO: 3.

[0015] Specifically, the gene encoding the light chain is as follows (3) or (4):

[0016] (3) The DNA molecule represented by nucleotides 1095-1748 in SEQ ID NO: 6;

[0017] (4) The DNA molecule represented by nucleotides 1038-1748 in SEQ ID NO: 6.

[0018] This invention also protects the use of any of the above-described IgG antibodies in the preparation of medicaments for inhibiting the novel coronavirus.

[0019] The present invention also protects a drug for inhibiting the novel coronavirus, the active ingredient of which is any of the IgG antibodies described above.

[0020] This invention also protects the use of any of the above-described IgG antibodies in the preparation of medicaments for neutralizing the novel coronavirus.

[0021] The present invention also protects a drug for neutralizing the novel coronavirus, the active ingredient of which is any of the IgG antibodies described above.

[0022] The present invention also protects the use of any of the above-described IgG antibodies in the preparation of medicaments for the prevention and / or treatment of COVID-19 infection.

[0023] The present invention also protects a medicament for the prevention and / or treatment of COVID-19 infection, wherein the active ingredient is any of the IgG antibodies described above.

[0024] The COVID-19 infection mentioned above refers to infection with the novel coronavirus.

[0025] The novel coronavirus mentioned above is either a wild-type novel coronavirus or a naturally occurring variant of the wild-type novel coronavirus.

[0026] The novel coronavirus mentioned above is a D614G mutant strain of the novel coronavirus.

[0027] The novel coronavirus mentioned above is a wild-type novel coronavirus, a novel coronavirus Alpha strain, a novel coronavirus Beta strain, a novel coronavirus Gamma strain, a novel coronavirus Delta strain, a novel coronavirus Delta plus strain, a novel coronavirus Mu strain, or a novel coronavirus Omeprone strain.

[0028] Specifically, the novel coronavirus Omeprung strains are novel coronavirus Omeprung BA.1 strain, novel coronavirus Omeprung BA.2.12.1 strain, novel coronavirus Omeprung BA.2.75 strain, novel coronavirus Omeprung BA.3 strain, or novel coronavirus Omeprung BA.4 / 5 strain.

[0029] This invention utilizes the spike protein of the novel coronavirus as bait, screening antibody-generating memory B cells from peripheral blood mononuclear cells of infected individuals to obtain a monoclonal antibody that specifically binds to the spike protein, named P5-2H11 antibody. The P5-2H11 antibody provided by this invention has a broad-spectrum neutralizing effect against SARS-CoV-2, exhibiting strong neutralizing ability against both wild-type novel coronavirus and naturally occurring variants. This invention has significant application value for the prevention and control of the novel coronavirus and will have profound social implications. Attached Figure Description

[0030] Figure 1 The neutralizing activity of the P5-2H11 antibody against the novel coronavirus pseudovirus was measured. Detailed Implementation

[0031] The present invention will now be described in further detail with reference to specific embodiments. The given embodiments are merely illustrative of the invention and not intended to limit its scope. The embodiments provided below can serve as a guide for further improvements by those skilled in the art and do not constitute a limitation on the invention in any way.

[0032] Unless otherwise specified, the experimental methods used in the following examples are conventional methods, performed according to the techniques or conditions described in the literature in this field or according to the product instructions. Unless otherwise specified, the materials and reagents used in the following examples are commercially available. Unless otherwise specified, all quantitative experiments in the following examples were performed in triplicate, and the results were averaged. 293F cells and 293T cells were commercially available human embryonic kidney epithelial cells. The pMD18-T vector was a commercially available plasmid vector. The pcDNA3.1(+) vector was from Invitrogen, catalog number V790-20.

[0033] hACE2-hela cells (ie "HeLa cell lines stably expressing theACE2molecules"), recorded in the following literature: Wang, R., Zhang, Q., Ge, J., Ren, W., Zhang, R., Lan, J., Ju, B., Su, B., Yu, F., Ch. en,P.,Liao,H.,Feng,Y.,Li,X.,Shi,X.,Zhang,Z.,Zhang,F.,Ding,Q.,Zhang,T.,Wang,X.&Zhang,L.Analysis of SARS-CoV-2 variant mutations reveal neutralization escape mechanisms and the ability to use ACE2receptors from additional species. Immunity 54, 1611-1621.e1615, doi:10.1016 / j.immuni.2021.06.003(2021).

[0034] Example 1: Discovery and preparation of P5-2H11 antibody

[0035] I. Discovery of P5-2H11 Antibody

[0036] Memory B cells were isolated from peripheral blood mononuclear cells of patients recovering from SARS-CoV-2, and the antibody gene of the memory B cells was amplified to obtain the antibody sequence. Through extensive comparison, analysis, preparation, and efficacy verification, the inventors of this invention discovered a new SARS-CoV-2 IgG antibody with excellent activity, which was named P5-2H11 antibody.

[0037] The amino acid sequence of the variable region of the heavy chain of the P5-2H11 antibody is shown in SEQ ID NO: 1 (CDR1, CDR2, and CDR3 are located at positions 26-33, 51-57, and 96-108, respectively; CDR1, CDR2, and CDR3 are EFTVSSNY, IYSGGST, and ARTLPLYGDYFDY, respectively). The amino acid sequence of the full-length heavy chain of the P5-2H11 antibody is shown in SEQ ID NO: 2; in SEQ ID NO: 2, amino acid residues 1-19 form the signal peptide (guides the protein to be secreted extracellularly), amino acid residues 20-138 form the variable region of the heavy chain, and amino acid residues 139-468 form the constant region of the heavy chain.

[0038] The amino acid sequence of the variable region of the light chain of the P5-2H11 antibody is shown in SEQ ID NO: 4 (CDR1, CDR2, and CDR3 are located at positions 26-34, 52-54, and 91-100, respectively; CDR1, CDR2, and CDR3 are SSNIGAGYD, GNN, and QSYDSSLSVV, respectively). The amino acid sequence of the full-length light chain of the P5-2H11 antibody is shown in SEQ ID NO: 5; in SEQ ID NO: 5, amino acid residues 1-19 form the signal peptide (guiding the protein to be secreted extracellularly), amino acid residues 20-129 form the variable region of the light chain, and amino acid residues 130-236 form the constant region of the light chain.

[0039] II. Preparation of P5-2H11 antibody

[0040] (I) Construction of recombinant plasmids

[0041] The heavy chain DNA molecule is a double-stranded DNA molecule, as shown in SEQ ID NO: 3. In SEQ ID NO: 3, nucleotides 1-891 form the promoter, nucleotides 892-2298 encode the full-length heavy chain, and nucleotides 2299-2444 form the terminator. Inserting the heavy chain DNA molecule into the pMD18-T vector yields the heavy chain expression vector.

[0042] The light chain DNA molecule is a double-stranded DNA molecule, as shown in SEQ ID NO: 6. In SEQ ID NO: 6, nucleotides 1-1037 form the promoter, nucleotides 1038-1748 encode the full-length light chain, and nucleotides 1749-1896 form the terminator. Inserting the light chain DNA molecule into the pMD18-T vector yields the light chain expression vector.

[0043] (II) Construction of Recombinant Cells

[0044] The heavy chain expression vector and the light chain expression vector were co-transfected into 293F cells to obtain recombinant cells.

[0045] (III) Antibody Preparation

[0046] 1. Take the recombinant cells obtained in step (II), culture them in DMEM medium containing 2% fetal bovine serum for 72 h, then centrifuge at 4℃ and 4000 rpm for 30 min, and collect the supernatant.

[0047] 2. Affinity chromatography

[0048] Affinity chromatography column specifications: length 3cm, inner diameter 1cm;

[0049] Affinity chromatography column packing material: protein A beads (Thermo, catalog number 10006D);

[0050] Procedure: ① Load 300 mL of the supernatant obtained in step 1 onto an affinity chromatography column and incubate at 4 °C for 16 hours; ② Wash the column with 60 mL of binding buffer; ③ Elute the target protein with 30 mL of elution buffer and collect the post-column solution.

[0051] Binding buffer: Dissolve 112.6g of glycine and 175.2g of sodium chloride in water and bring the volume to 1L. Adjust the pH to 8.0 with sodium hydroxide.

[0052] Elution buffer: Dissolve 7.5g of glycine in water and bring the volume to 500ml. Adjust the pH to 3.0 with hydrochloric acid.

[0053] 3. Take the post-column solution obtained in step 2, concentrate it with an ultrafiltration concentrator, and replace the system with PBS buffer (pH 7.2, 10mM) to obtain P5-2H11 antibody solution (antibody concentration is approximately 1 mg / ml).

[0054] Example 2, Neutralization Test

[0055] I. Preparation of Novel Coronavirus Pseudovirus

[0056] Co-transfection of 293T cells with a plasmid expressing the SARS-CoV-2 membrane protein and a backbone plasmid pNL4-3R-E-luciferase yielded an infectious but non-replicating pseudovirus of SARS-CoV-2, with infectivity similar to that of live SARS-CoV-2. The backbone plasmid pNL4-3R-E-luciferase, i.e., the backbone plasmid pNL4-3R-E containing Luciferase (i.e., vector with the luciferase gene containing backbone pNL4-3R-E in the literature), is described in the following literature: Wang Q, Liu L, Ren W, Gettie A, Wang H, Liang Q, Shi X, Montefiori DC, Zhou T, Zhang L. Cell Rep. 2019.

[0057] The gene encoding the novel coronavirus membrane protein was inserted between the BamHII and EcoRI restriction sites of the pcDNA3.1(+) vector to obtain a plasmid expressing the novel coronavirus membrane protein. The plasmid expressing the novel coronavirus membrane protein and the backbone plasmid pNL4-3R-E-luciferase were co-transfected into 293T cells and incubated at 37°C (using DMEM medium containing 10% fetal bovine serum). The cell culture supernatant was collected 60 hours after transfection; this was the viral solution containing the novel coronavirus pseudovirus. Viral solutions of pseudoviruses of 12 different novel coronavirus strains were prepared. The 12 novel coronavirus strains refer to the following: novel coronavirus D614G mutant strain, novel coronavirus Alpha strain, novel coronavirus Beta strain, novel coronavirus Gamma strain, novel coronavirus Delta strain, novel coronavirus Delta plus strain, novel coronavirus Mu strain, novel coronavirus Omeprone BA.1 strain, novel coronavirus Omeprone BA.2.12.1 strain, novel coronavirus Omeprone BA.2.75 strain, novel coronavirus Omeprone BA.3 strain, and novel coronavirus Omeprone BA.4 / 5 strain.

[0058] The membrane protein of the wild-type novel coronavirus (WT) is shown in SEQ ID NO: 7. The gene encoding the membrane protein of the wild-type novel coronavirus is located at positions 21563-25384 in the whole genome in GenBank: MN908947.3(18-MAR-2020).

[0059] The membrane protein of the novel coronavirus D614G mutant strain has undergone the following mutation compared to the wild-type strain: D614G. The gene encoding the membrane protein of the novel coronavirus D614G mutant strain is shown in SEQ ID NO: 8.

[0060] The membrane proteins of the novel coronavirus Alpha strain (Pango lineage B.1.1.7) exhibit the following mutations compared to the wild-type strain: 69-70del(HV), 144del(Y), N501Y, A570D, D614G, P681H, T716I, S982A, and D1118H. The coding genes for the membrane proteins of the novel coronavirus Alpha strain are described in GISAID:EPI_ISL_601443.

[0061] The membrane proteins of the novel coronavirus Beta strain (Pango lineage B.1.351) exhibit the following mutations compared to the wild-type strain: L18F, D80A, D215G, 242-244del (LLA), S305T, K417N, E484K, N501Y, D614G, and A701V. The coding genes for the membrane proteins of the novel coronavirus Beta strain are documented in GISAID: EPI_ISL_700450.

[0062] The membrane proteins of the novel coronavirus Gamma strain (Pango lineage P.1) have undergone the following mutations compared to the wild-type strain: L18F, T20N, P26S, D138Y, R190S, K417T, E484K, N501Y, D614G, H655Y, T1027I, and V1176F. The coding genes for the membrane proteins of the novel coronavirus Gamma strain are described in GISAID: EPI_ISL_792681.

[0063] The membrane proteins of the novel coronavirus Delta strain (Pango lineage B.1.617.2) exhibit the following mutations compared to the wild-type strain: T19R, G142D, 156-157del(EF), R158G, A222V, L452R, T478K, D614G, P681R, and D950N. The coding genes for the membrane proteins of the novel coronavirus Delta strain are documented in GISAID:EPI_ISL_1534938.

[0064] The membrane protein of the novel coronavirus Delta plus strain (Pango lineage AY.x) has the following mutation compared to the Delta strain: K417N. The coding gene for the membrane protein of the novel coronavirus Delta plus strain is described in GISAID:EPI_ISL_3019629.

[0065] The membrane proteins of the novel coronavirus Mu strain (Pango lineage B.1.621) exhibit the following mutations compared to the wild-type strain: T95I, Y144T, Y145S, ins146N, R346K, E484K, N501Y, D614G, P681H, and D950N. The coding genes for the membrane proteins of the novel coronavirus Mu strain are described in GISAID: EPI_ISL_3987640.

[0066] The novel coronavirus Omeprone BA.1 strain (Pango lineage) The membrane proteins of BA.1) underwent the following mutations relative to the wild-type membrane proteins: A67V, Δ69-70(HV), T95I, G142D, Δ143-145(VYY), Δ211(N), L212I, ins214EPE, G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, Y505H, T547K, D614G, H655Y, N679K, P681H, N764K, D796Y, N856K, Q954H, N969K, L981F. The gene encoding the membrane protein of the novel coronavirus Omeprón BA.1 strain is documented in GISAID:EPI_ISL_6752027.

[0067] The membrane proteins of the novel coronavirus Pango lineage BA.2.12.1 strain have undergone the following mutations compared to the wild-type strain: T19I, 24-26del(LPP), A27S, G142D, V213G, G339D, S371F, S373P, S375F, T376A, D405N, R408S, K417N, N440K, L452Q, S477N, T478K, E484A, Q493R, Q498R, N501Y, Y505H, D614G, H655Y, N679K, P681H, N764K, D796Y, Q954H, and N969K. The gene encoding the membrane protein of the novel coronavirus strain Omeprón BA.2.12.1 is documented in GISAID:EPI_ISL_12560123.

[0068] The membrane proteins of the novel coronavirus Omeprone BA.2.75 strain have undergone the following mutations compared to the wild-type strain: T19I, del24-26(LPP), A27S, G142D, K147E, W152R, F157L, I210V, V213G, G257S, G339H, S371F, S373P, S375F, T376A, D405N, R408S, K417N, N440K, G446S, N460K, S477N, T478K, E484A, Q498R, N501Y, Y505H, D614G, H655Y, N679K, P681H, N764K, D796Y, Q954H, N969K. The gene encoding the membrane protein of the novel coronavirus strain Omeprón BA.2.75 is documented in GISAID:EPI_ISL_14393635.

[0069] The membrane proteins of the novel coronavirus Pango lineage BA.3 strain have undergone the following mutations compared to the wild-type strain: A67V, del69-70(HV), T95I, G142D, del143-145(VYY), 211del(N), L212I, G339D, S371F, S373P, S375F, D405N, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, Q498R, N501Y, Y505H, D614G, H655Y, N679K, P681H, N764K, D796Y, Q954H, N969K. The gene encoding the membrane protein of the novel coronavirus Omeprón BA.3 strain is documented in GISAID:EPI_ISL_7740765.

[0070] The membrane proteins of the novel coronavirus Pango lineage BA.4 / 5 strain have undergone the following mutations compared to the wild-type strain: T19I, 24-26del (LPP), A27S, del69-70 (HV), G142D, V213G, G339D, S371F, S373P, S375F, T376A, D405N, R408S, K417N, N440K, G446S, L452R, S477N, T478K, E484A, F486V, Q498R, N501Y, Y505H, D614G, H655Y, N679K, P681H, N764K, D796Y, Q954H, N969K. The gene encoding the membrane protein of the novel coronavirus Omeprón BA.4 / 5 strain is documented in EPI_ISL_12559461.

[0071] II. Detection of antibody neutralizing activity

[0072] Test virus solutions: virus solutions of the 12 novel coronavirus strains prepared in step one.

[0073] 1. Take the P5-2H11 antibody solution prepared in Example 1 and dilute it with PBS buffer (pH 7.2, 10mM) to obtain antibody dilution solutions of various concentrations.

[0074] 2. Take a 96-well cell culture plate and add 100 μL of antibody diluent and 50 μL of test virus solution to each well (the virus concentration in the 50 μL test virus solution is 1 × 10⁻⁶). 4 Incubate at 37°C for 1 hour with TCID50 / ml. Use an equal volume of PBS buffer (pH 7.2, 10mM) instead of antibody dilution as a virus control. Use an equal volume of DMEM medium containing 10% fetal bovine serum instead of the test virus solution as a cell control.

[0075] 3. After completing step 2, take the cell culture plate and inoculate each well with 100 μL of hACE2-hela cell suspension (the solvent used to prepare the cell suspension is DMEM medium containing 10% fetal bovine serum, and the concentration of hACE2-hela cells in the cell suspension is 2 × 10⁻⁶). 5 (cells / ml), incubated at 37°C for 64 hours.

[0076] 4. After completing step 3, take the cell culture plate, aspirate the supernatant, add 150 μL of lysis buffer (Microglass Biotechnology, catalog number T003, follow the instructions) to each well, and incubate at 37°C for 5 minutes.

[0077] 5. After completing step 4, take the cell culture plate and detect the luciferase activity.

[0078] Each process is configured with multiple duplicate holes.

[0079] Neutralization activity (%) = [1 - (fluorescence intensity of experimental group - fluorescence intensity of cell control) / (fluorescence intensity of virus control - fluorescence intensity of cell control)] × 100%.

[0080] Neutralization activity results are shown in Figure 1 . Figure 1 The vertical axis represents neutralizing activity (%); the horizontal axis represents the antibody concentration (μg / ml) logarithm to base 10. The antibody concentration refers to the antibody concentration in the mixed system consisting of 100 μL of antibody dilution and 50 μL of test virus solution in step 2.

[0081] The antibody concentration at which the neutralizing activity is 50% was calculated using Prism 5 software, i.e., the IC50 value of the antibody.

[0082] Table 1 shows the IC50 values ​​(in ng / ml) of the P5-2H11 antibody against pseudoviruses of 12 novel coronavirus strains.

[0083] Table 1

[0084]

[0085]

[0086] The present invention has been described in detail above. For those skilled in the art, the invention can be practiced in a wide range of ways with equivalent parameters, concentrations, and conditions without departing from its spirit and scope, and without requiring unnecessary experiments. Although specific embodiments have been given, it should be understood that further modifications can be made to the invention. In summary, according to the principles of the invention, this application is intended to include any changes, uses, or improvements to the invention, including changes made using conventional techniques known in the art that depart from the scope disclosed herein. Some of the essential features can be applied within the scope of the following appended claims.

Claims

1. An IgG antibody, which is composed of a light chain and a heavy chain; CDR1, CDR2 and CDR3 in the heavy chain variable region in the heavy chain are sequentially shown in SEQ ID NO: 1 at positions 26-33, 51-57, 96-108; CDR1, CDR2 and CDR3 in the light chain variable region in the light chain are sequentially shown in SEQ ID NO: 4 at positions 26-34, 52-54, 91-100. 2.The IgG antibody of claim 1, wherein: the heavy chain variable region is shown in SEQ ID NO: 1; and the light chain variable region is shown in SEQ ID NO:

4. 3.The IgG antibody of claim 2, wherein: the heavy chain is (a) a protein shown in SEQ ID NO: 2 at positions 20-468 or (b) a protein shown in SEQ ID NO: 2; and the light chain is (c) a protein shown in SEQ ID NO: 5 at positions 20-236 or (d) a protein shown in SEQ ID NO:

5. 4.A gene encoding the IgG antibody of any one of claims 1 to 3. 5.Use of the IgG antibody of claim 1 or 2 or 3 in the preparation of a medicament for inhibiting a novel coronavirus. 6.A medicament for inhibiting a novel coronavirus, wherein the active ingredient is the IgG antibody of claim 1 or 2 or 3. 7.Use of the IgG antibody of claim 1 or 2 or 3 in the preparation of a medicament for neutralizing a novel coronavirus. 8.A medicament for neutralizing a novel coronavirus, wherein the active ingredient is the IgG antibody of claim 1 or 2 or 3. 9.Use of the IgG antibody of claim 1 or 2 or 3 in the preparation of a medicament for preventing and / or treating a novel coronavirus infection. 10.A medicament for preventing and / or treating a novel coronavirus infection, wherein the active ingredient is the IgG antibody of claim 1 or 2 or 3. ​ ​ ​ ​

Citation Information

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