Cited by 739SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approachesAnimal Virus Infections Studies

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Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization

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Liu, Zhuoming, VanBlargan, Laura A., Bloyet, Louis-Marie, Rothlauf, Paul W., Chen, Rita E., Stumpf, Spencer, Zhao, Haiyan, Errico, John M., Theel, Elitza S., Liebeskind, Mariel J., Alford, Brynn, Buchser, William J., Ellebedy, Ali H., Fremont, Daved H., Diamond, Michael S., Whelan, Sean P.J.·2021·Cell Host & Microbe

DOI 10.1016/j.chom.2021.01.014PMC PMC7839837

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Abstract

Neutralizing antibodies against the SARS-CoV-2 spike (S) protein are a goal of COVID-19 vaccines and have received emergency use authorization as therapeutics. However, viral escape mutants could compromise efficacy. To define immune-selected mutations in the S protein, we exposed a VSV-eGFP-SARS-CoV-2-S chimeric virus, in which the VSV glycoprotein is replaced with the S protein, to 19 neutralizing monoclonal antibodies (mAbs) against the receptor-binding domain (RBD) and generated 50 different escape mutants. Each mAb had a unique resistance profile, although many shared residues within an epitope of the RBD. Some variants (e.g., S477N) were resistant to neutralization by multiple mAbs, whereas others (e.g., E484K) escaped neutralization by convalescent sera. Additionally, sequential selection identified mutants that escape neutralization by antibody cocktails. Comparing these antibody-mediated mutations with sequence variation in circulating SARS-CoV-2 revealed substitutions that may attenuate neutralizing immune responses in some humans and thus warrant further investigation.

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Intra-Host Evolution Analyses in an Immunosuppressed Patient Supports SARS-CoV-2 Viral Reservoir Hypothesis
Fournelle, D., Mostefai, F., Brunet‐Ratnasingham, E., Poujol, R., Grenier, J., Gálvez, J. H., Pagliuzza, A., Levade, I., Moreira, S., Benlarbi, M., et al. (2024) · Viruses · doi:10.3390/v16030342 · Cited by 13
New Approaches and Repurposed Antiviral Drugs for the Treatment of the SARS-CoV-2 Infection
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Inferring selection effects in SARS-CoV-2 with Bayesian Viral Allele Selection
Jankowiak, M., Obermeyer, F. H., & Lemieux, J. E. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010540 · Cited by 12
Rapid surveillance platforms for key SARS-CoV-2 mutations in DenmarkPreprint
Spieß, K., Gunalan, V., Marving, E. L., Nielsen, S. H., Jørgensen, M. G. P., Fomsgaard, A. S., Nielsen, L., Alfaro‐Núñez, A., Karst, S. M., Mortensen, S., et al. (2021) · medRxiv · doi:10.1101/2021.10.25.21265484 · Cited by 12
A high-throughput, automated, cell-free expression and screening platform for antibody discoveryPreprint
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“…discovery platforms and (ii) the importance of identifying high-affinity antibodies targeting conserved epitopes 9,10 or non-overlapping epitopes 11,12 to resist viral escape and increase the ability to neutralize viral variants 13,14 ; both of which have required intensive screening campaigns.”
Background
Rapid detection of SARS-CoV-2 variants of concern by single nucleotide polymorphism genotyping using TaqMan assays
Velu, P., Cong, L., Rand, S., Qiu, Y., Zhang, Z., Zhang, J., Guo, J., Ruggiero, P., Sukhu, A. C., Fauntleroy, K. A., et al. (2022) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/j.diagmicrobio.2022.115789 · Cited by 11
“Variants which contain the E484K mutations have been shown to be partially or completely resistant to certain therapeutic monoclonal antibodies, and less susceptible to neutralization by convalescent plasma shown to help fight SARSCoV-2 infection [7,20], supporting the importance of accurate lineage determination.”
Background
Integrating artificial intelligence-based epitope prediction in a SARS-CoV-2 antibody discovery pipeline: caution is warranted
Acar, D. D., Witkowski, W., Wejda, M., Wei, R., Desmet, T., Schepens, B., Cae, S. D., Sedeyn, K., Eeckhaut, H., Fijałkowska, D., et al. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2023.104960 · Cited by 12
Evidence of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Reinfection Without Mutations in the Spike Protein
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Molecular epidemiology of SARS-CoV-2 in Cyprus
Richter, J., Fanis, P., Tryfonos, C., Koptides, D., Krashias, G., Bashiardes, S., Hadjisavvas, A., Loizidou, M. A., Oulas, A., Alexandrou, D., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248792 · Cited by 11
Generation and Effect Testing of a SARS-CoV-2 RBD-Targeted Polyclonal Therapeutic Antibody Based on a 2-D Airway Organoid Screening System
He, Y., Qu, J. T., Wei, L., Liao, S., Zheng, N., Liu, Y., Wang, X., Jing, Y., Shen, C. K.-F., Ji, C., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.689065 · Cited by 11
Outbreak of P.3 (Theta) SARS-CoV-2 emerging variant of concern among service workers in Louisiana
Rose, R., Nolan, D. J., LaFleur, T. M., & Lamers, S. L. (2021) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2021.11.011 · Cited by 11
Differentiation of SARS-CoV-2 Variants Using RT-qPCRs by Targeting Recurrent Mutation Sites: A Diagnostic Laboratory Experience from Multi-Center Regional Study, August 2020–December 2021, Poland
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ACE2 receptor polymorphism in humans and animals increases the risk of the emergence of SARS-CoV-2 variants during repeated intra- and inter-species host-switching of the virus
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“427 (Epsilon) variants was associated with a modest increase in infectivity as measured after incubation with soluble murine ACE2 (Liu et al., 2021).”
Background
Functional mutations of SARS-CoV-2: implications to viral transmission, pathogenicity and immune escape
Dang, S., Ren, L., & Wang, J. (2022) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002158 · Cited by 10
“1216 increasing S protein expression on the cellular membrane and enhancing the binding affinity with the ACE2 receptor.([79-84]) Compared with Wuhan-Hu-1 strain (with D614G mutation), the Delta strain is 6-fold less sensitive to host NAbs retrieved from recovered COVID-19 patients infected by Wuhan-Hu-1 strain, and 8…”
BackgroundInfluential
A SARS-CoV-2: Companion Animal Transmission and Variants Classification
Pandit, R., & Matthews, Q. L. (2023) · Pathogens · doi:10.3390/pathogens12060775 · Cited by 11
Comparative Study of the Mutations Observed in the SARS-CoV-2 RBD Variants of Concern and Their Impact on the Interaction with the ACE2 Protein
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Collaboration between the Fab and Fc contribute to maximal protection against SARS-CoV-2 following NVX-CoV2373 subunit vaccine with Matrix-M™ vaccinationPreprint
Alter, G., Gorman, M. J., Patel, N., Guebre‐Xabier, M., Zhu, A. L., Atyeo, C. G., Pullen, K. M., Loos, C., Goez-Gazi, Y., Carrion, R., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-200342/v1 · Cited by 9
SARS-CoV-2 3CLpro mutations confer resistance to Paxlovid (nirmatrelvir/ritonavir) in a VSV-based, non-gain-of-function systemPreprint
Heilmann, E., Costacurta, F., Volland, A., & von Laer, D. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.02.495455 · Cited by 11
“1 wt L32I, H80P, D216G allosteric, allosteric, allosteric L32F (78), H80Y (43) L32I (201), H80P (3), D216G (11)”
MethodInfluential
ACE2-Fc and DPP4-Fc decoy receptors against SARS-CoV-2 and MERS-CoV variants: a quick therapeutic option for current and future coronaviruses outbreaks
Alfaleh, M. A., Alsulaiman, R. M., Almahboub, S. A., Nezamuldeen, L., Zawawi, A., Aljehani, N. D., Yasir, M., Abdulal, R. H., Alkhaldi, R. K., Helal, A., et al. (2023) · Antibody Therapeutics · doi:10.1093/abt/tbad030 · Cited by 9
“The efficiency of most of the available anti-SARS-CoV-2 monoclonal antibodies (mAbs) and vaccines is challenged by several aspects including the continuous variations in the viral genome and emergence of new variants including the “variants of concern” (VoCs) and “variants of interest” (VoIs) [2–5].”
Background
Synthetic coevolution reveals adaptive mutational trajectories of neutralizing antibodies and SARS-CoV-2
Ehling, R. A., Minot, M., Overath, M. D., Sheward, D. J., Han, J., Gao, B., Taft, J. M., Pertseva, M., Weber, C. R., Frei, L., et al. (2025) · Cell Systems · doi:10.1016/j.cels.2025.101391 · Cited by 8
On the association between SARS-COV-2 variants and COVID-19 mortality during the second wave of the pandemic in Europe
Jabłońska, K., Aballéa, S., Auquier, P., & Toumi, M. (2021) · Journal of Market Access & Health Policy · doi:10.1080/20016689.2021.2002008 · Cited by 10
Allosteric Determinants of the SARS-CoV-2 Spike Protein Binding with Nanobodies: Examining Mechanisms of Mutational Escape and Sensitivity of the Omicron Variant
Verkhivker, G. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042172 · Cited by 9
“Moreover, mutations at the E484 position (E484A, E484G, E484D, and E484K) confer partial resistance to the convalescent plasma, showing that E484 is also one of the dominant epitopes of spike protein [123,124].”
Background
Plasma and memory antibody responses to Gamma SARS-CoV-2 provide limited cross-protection to other variants
Agudelo, M., Muecksch, F., Schaefer-Babajew, D. J., Cho, A., DaSilva, J., Bednarski, E., Ramos, V., Oliveira, T. Y., Cipolla, M., Gazumyan, A., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220367 · Cited by 9
Immunogenicity and risk of disease flare after a three-dose regimen with SARS-CoV-2 vaccination in patients with systemic lupus erythematosus: results from the prospective cohort study COVAC-SLE
Larsen, E. S., Nilsson, A. C., Möller, S., Voss, A., & Johansen, I. S. (2022) · Clinical and Experimental Rheumatology · doi:10.55563/clinexprheumatol/b8a6zb · Cited by 10
Transchromosomic bovine-derived anti-SARS-CoV-2 polyclonal human antibodies protects hACE2 transgenic hamsters against multiple variants
Gilliland, T. H., Dunn, M., Liu, Y., Alcorn, M. D. H., Terada, Y., Vasilatos, S. N., Lundy, J. D., Li, R., Nambulli, S., Larson, D. P., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107764 · Cited by 10
A comprehensive overview of identified mutations in SARS CoV-2 spike glycoprotein among Iranian patients
Eslami, S., Glassy, M. C., & Ghafouri‐Fard, S. (2021) · Gene · doi:10.1016/j.gene.2021.146113 · Cited by 12
Immunogenicity of the Xcl1-SARS-CoV-2 Spike Fusion DNA Vaccine for COVID-19
Qi, H., Sun, Z., Yao, Y., Chen, L., & Su, X. (2022) · Vaccines · doi:10.3390/vaccines10030407 · Cited by 10
Computational modeling of the effect of five mutations on the structure of the ACE2 receptor and their correlation with infectivity and virulence of some emerged variants of SARS-CoV-2 suggests mechanisms of binding affinity dysregulation
Rodriguez, J. A., Gonzalez, J., Arboleda-Bustos, C. E., Mendoza, N., Martinez, C., & Pinzón, A. M. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110244 · Cited by 10
“vaccine-induced T cells, leading to enhanced T cell recognition towards emerging variants and the mutation S477N appears to promote resistance to neutralization by multiple mAbs [59].”
REGEN-COV protects against viral escape in preclinical and human studiesPreprint
Copin, R., Baum, A., Wloga, E. H., Pascal, K. E., Giordano, S., Fulton, B. O., Zhou, A., Negron, N., Lanza, K., Chan, N., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.10.434834 · Cited by 10
Impact of temperature on the affinity of SARS-CoV-2 Spike for ACE2Preprint
Prévost, J., Richard, J., Gasser, R., Ding, S., Fage, C., Anand, S. P., Adam, D., Vergara, N. G., Tauzin, A., Benlarbi, M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.09.451812 · Cited by 10
SARS-CoV-2 Omicron: evasion of potent humoral responses and resistance to clinical immunotherapeutics relative to viral variants of concernPreprint
Aggarwal, A., Stella, A. O., Walker, G. J., Akerman, A., Milogiannakis, V., Brilot, F., Amatayakul‐Chantler, S., Roth, N., Coppola, G., Schofield, P., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1207364/v1 · Cited by 10
The comparison of pathogenicity among SARS-CoV-2 variants in domestic cats
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A global collaboration for systematic analysis of broad-ranging antibodies against the SARS-CoV-2 spike protein
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Different configurations of SARS-CoV-2 spike protein delivered by integrase-defective lentiviral vectors induce persistent functional immune responses, characterized by distinct immunogenicity profiles
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Are the new SARS-CoV-2 variants resistant against the vaccine?
Abdalla, M., El‐Arabey, A. A., & Jiang, X. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1925503 · Cited by 9
“Moreover, the difference in producing antibody neutralization depends on which cell line reacts to which SARS-CoV-2 variants.(3,4) All the discussions above provide insights into why re-infection occurs and highlight the problem in vaccine design.”
Background
Large Scale SARS-CoV-2 Molecular Testing and Genomic Surveillance Reveal Prolonged Infections, Protracted RNA shedding, and Viral Reinfections
Morris, C. P., Luo, C. H., Sachithanandham, J., Li, M., Schwartz, M. C., Gaston, D. C., Gniazdowski, V., Giraldo, N. A., Amadi, A., Norton, J. M., et al. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.809407 · Cited by 10
Mathematical artificial intelligence design of mutation-proof COVID-19 monoclonal antibodies
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Chronic shedding of a SARS-CoV-2 Alpha variant in wastewater
Conway, M. J., Yang, H., Revord, L. A., Novay, M. P., Lee, R. J., Ward, A. S., Abel, J. D., Williams, M. R., Uzarski, R. L., & Alm, E. W. (2024) · BMC Genomics · doi:10.1186/s12864-024-09977-7 · Cited by 9
An in vitro experimental pipeline to characterize the epitope of a SARS-CoV-2 neutralizing antibody
Atanasoff, K. E., Brambilla, L., Adelsberg, D. C., Kowdle, S., Stevens, C. S., Slamanig, S., Hung, C.-T., Fu, Y., Lim, R. K. V., Tran, L. M., et al. (2023) · mBio · doi:10.1128/mbio.02477-23 · Cited by 8
“Indeed, non-hydropho bic residues serine and proline at position 486 limit neutralizing capability of mAbs against circulating SARS-CoV-2 variants (38) and laboratory-generated mutants (39).”
Background
Neutralizing Antibody Responses to SARS-CoV-2 in Korean Patients Who Have Recovered from COVID-19
Kim, Y., Bae, J., Bae, S., Hwang, S., Kwon, K. T., Chang, H., Lee, W. K., Cui, C., Lee, G. E., Kim, S., et al. (2021) · Yonsei Medical Journal · doi:10.3349/ymj.2021.62.7.584 · Cited by 8
Standardized Two-Step Testing of Antibody Activity in COVID-19 Convalescent Plasma
Gilchuk, P., Thomsen, I. P., Yoder, S. M., Brady, E. J., Chappell, J. D., Stevens, L. J., Denison, M. R., Sutton, R. E., Chen, R. E., VanBlargan, L. A., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103602 · Cited by 7
“…pool of SARS2-2, SARS2-11, SARS2-16, SARS2-31, SARS2-38, SARS2-57 and SARS2-71 20 iScience 25, 103602, January 21, 2022 mouse anti-S antibodies (Liu et al., 2021; VanBlargan et al., 2021) and HRP-conjugated goat anti-mouse IgG (Sigma-Aldrich) in PBS supplemented with 0.1% saponin and 0.1%…”
MethodInfluentialSelf-citation
BSL2-compliant lethal mouse model of SARS-CoV-2 and variants of concern to evaluate therapeutics targeting the Spike protein
Manangeeswaran, M., Ireland, D. D. C., Thacker, S. G., Lee, H., Kelley-Baker, L., Lewkowicz, A. P., Rothlauf, P. W., Pontelli, M. C., Bloyet, L.-M., Eckhaus, M., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.919815 · Cited by 8
“SARS-CoV-2, like other RNA viruses, is prone to genetic evolution, and even single amino acid changes can drastically affect a virus’s ability to bind ACE2 or evade the immune system (5, 38).”
BackgroundSelf-citation
Long-term passaging of pseudo-typed SARS-CoV-2 reveals the breadth of monoclonal and bispecific antibody cocktails
Ma, H., Zong, H., Liu, J., Yue, Y., Ke, Y., Liao, Y., Tang, H., Wang, L., Wang, S., Yuan, Y., et al. (2023) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-01043-w · Cited by 7
“The L452R stabilized the conformation of the S protein [7] and led to an increased affinity between the virus and angiotensin converting enzyme 2 (ACE2) [8].”
Background
Spike Protein Genetic Evolution in Patients at High Risk of Severe Coronavirus Disease 2019 Treated by Monoclonal Antibodies
Leducq, V., Zafilaza, K., Fauchois, A., Ghidaoui, E., Sayon, S., Dorival, C., Meledje, M.-L., Lusivika‐Nzinga, C., Yordanov, Y., Martin‐Blondel, G., et al. (2023) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiad523 · Cited by 8
Global Discrepancies between Numbers of Available SARS-CoV-2 Genomes and Human Development Indexes at Country Scales
Colson, P., & Raoult, D. (2021) · Viruses · doi:10.3390/v13050775 · Cited by 8
Jumping a Moving Train: SARS-CoV-2 Evolution in Real Time
Moustafa, A. M., & Planet, P. J. (2021) · Journal of the Pediatric Infectious Diseases Society · doi:10.1093/jpids/piab051 · Cited by 8
“Most notable of these are mutations at the E484 position [130, 153, 154].”
Background
Genomic Sequencing of SARS-CoV-2 E484K Variant B.1.243.1, Arizona, USA
Skidmore, P. T., Kaelin, E. A., Holland, L. A., Maqsood, R., Wu, L. I., Mellor, N. J., Blain, J. M., Harris, V. K., LaBaer, J., Murugan, V., et al. (2021) · Emerging infectious diseases · doi:10.3201/eid2710.211189 · Cited by 8
“471 (5) and variant calling using Geneious Prime version 2021 (https://www.”
Background
Analysis of SARS-CoV-2 variants B.1.617: host tropism, proteolytic activation, cell–cell fusion, and neutralization sensitivity
Zhang, L., Li, Q., Wu, J., Yu, Y., Zhang, Y., Nie, J., Liang, Z., Cui, Z., Liu, S., Wang, H., et al. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2054369 · Cited by 10
“also been identified in the context of therapeutic mAb selective pressure and during persistent infection in immunocompromised hosts [37,38].”
Background
Neutralizing antibodies levels are increased in individuals with heterologous vaccination and hybrid immunity with Ad5-nCoV in the north of Mexico
Cervantes-Luévano, K., Espino‐Vázquez, A. N., Flores-Acosta, G. I., Bernáldez-Sarabia, J., Cabanillas-Bernal, O., Gasperin-Bulbarela, J., González-Sánchez, R., Comas‐García, A., & Licea-Navarro, A. F. (2022) · PLoS ONE · doi:10.1371/journal.pone.0269032 · Cited by 10
Characteristics and Functions of Infection-enhancing Antibodies to the N-terminal Domain of SARS-CoV-2
Connor, R. I., Sakharkar, M., Rappazzo, G., Kaku, C. I., Curtis, N. C., Shin, S., Wieland‐Alter, W., Wentworth, J., Mielcarz, D. W., Weiner, J. A., et al. (2024) · Pathogens and Immunity · doi:10.20411/pai.v9i2.679 · Cited by 8
“The RBD is subject to mutation contributing to the emergence of SARS-CoV-2 variants with increased transmissibility and significantly reduced susceptibility to neutralization [5–7].”
Background
Postinfectious Immunity After COVID-19 and Vaccination Against SARS-CoV-2
Kršák, M., Harry, B. L., Palmer, B. E., & Franco‐Paredes, C. (2021) · Viral Immunology · doi:10.1089/vim.2021.0054 · Cited by 8
“The speed of vaccination is all the more important now, after we have learned that the more time the virus has, the more escape mutations are likely to challenge effective immunity (33).”

Authors: Liu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., Alford, B., Buchser, W. J., Ellebedy, A. H., Fremont, D. H., Diamond, M. S., & Whelan, S. P. J.
Affiliations: Washington University in St. Louis (US)
Harvard University (US)
Mayo Clinic (US)
Corresponding author: Diamond, Michael S.
Whelan, Sean P.J.
ORCID: Liu, Zhuoming
VanBlargan, Laura A.
Bloyet, Louis-Marie
Rothlauf, Paul W.
Chen, Rita E.
Stumpf, Spencer
Zhao, Haiyan
Errico, John M.
Theel, Elitza S.
Liebeskind, Mariel J.
Buchser, William J.
Ellebedy, Ali H.
Fremont, Daved H.
Diamond, Michael S.
Whelan, Sean P.J.
Venue: Cell Host & Microbe
Publisher: Elsevier BV
Published: 2021-03
Volume: 29
Issue: 3
Pages: 477-488.e4
ISSN: 1931-3128 (ISSN-L)
DOI: 10.1016/j.chom.2021.01.014
PMC: PMC7839837
OpenAlex: W3121995178
Cited by: 725
References: 38
Citations by year: 2026: 11 · 2025: 22 · 2024: 57 · 2023: 77 · 2022: 255 · 2021: 302
FWCI: 55.27
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 374 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell Host & Microbe (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Funders: Washington University in St. Louis
University of Washington
Saint Louis University
National Institutes of Health (75N93019C00062, R01 AI127828, R01 AI157155, R37 AI059371)
AbbVie
Defense Advanced Research Projects Agency (HR001117S0019)
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Keywords: SARS-CoV-2 spike protein, antibody escape mutants, neutralizing monoclonal antibodies, receptor binding domain, E484K mutation
MeSH terms: Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, COVID-19 Vaccines, Animals, Antibodies, Monoclonal, Antibodies, Viral, Chlorocebus aethiops, Female, Humans, Mice, Inbred BALB C, Models, Molecular, Mutation, Neutralization Tests, Protein Binding, Receptors, Virus, Vero Cells, Amino Acid Substitution, Mice, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus

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Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization

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