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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One year into the pandemic: Short-term evolution of SARS-CoV-2 and emergence of new lineages
Gónzález‐Candelas, F., Shaw, M., Phan, T. G., Kulkarni‐Kale, U., Paraskevis, D. N., Luciani, F., Kimura, H., & Sironi, M. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.104869 · Cited by 65
A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
Ghosh, N., Nandi, S., & Saha, I. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108565 · Cited by 64
A combination of cross-neutralizing antibodies synergizes to prevent SARS-CoV-2 and SARS-CoV pseudovirus infection
Liu, H., Yuan, M., Huang, D., Bangaru, S., Zhao, F., Lee, C.-C. D., Peng, L., Barman, S., Zhu, X., Nemazee, D. A., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.005 · Cited by 58
“The RBD is also prone to naturally occurring mutations, along with the N-terminal domain (NTD) and other non-RBD and non-NTD regions, where insertions and deletions have also been found (Greaney et al., 2021b; Kemp et al., 2021; Liu et al., 2021; McCarthy et al., 2021; Starr et al., 2020; Tegally et al., 2021; Van Ege…”
Integrated Biophysical Modeling of the SARS-CoV-2 Spike Protein Binding and Allosteric Interactions with Antibodies
Verkhivker, G. M., & Paola, L. D. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00395 · Cited by 55
Evidence for retained spike-binding and neutralizing activity against emerging SARS-CoV-2 variants in serum of COVID-19 mRNA vaccine recipients
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“However, S477N has also been described as escape mutation [32].”
A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy
Greaney, A. J., Starr, T. N., Eguia, R. T., Loes, A. N., Khan, K., Karim, F., Cele, S., Bowen, J. E., Logue, J. K., Corti, D., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010248 · Cited by 58
The spike glycoprotein of SARS-CoV-2: A review of how mutations of spike glycoproteins have driven the emergence of variants with high transmissibility and immune escape
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SARS-CoV-2’s Variants of Concern: A Brief Characterization
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“These mutations in the VOCs, without changing the viral fitness, can be selected during the course of the infection, by the host’s immune system, by therapy with convalescent plasma, by vaccines and also by treatment with antibodies (64).”
Background
An atlas of continuous adaptive evolution in endemic human viruses
Kistler, K. E., & Bedford, T. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.09.012 · Cited by 65
“…viruses as those with high rates of adaptation in the protein that mediates receptor-binding, as this is a primary location of antibody neutralization and the locus of antigenic escape mutations in seasonal influenza viruses 19,20,9,21 , coronavirus 229E 7 and SARS-CoV-2 22,23,24,25 .”
SARS-CoV-2 Subgenomic RNAs: Characterization, Utility, and Perspectives
Long, S. (2021) · Viruses · doi:10.3390/v13101923 · Cited by 67
SARS-CoV-2 variants – Evolution, spike protein, and vaccines
Chen, K.-W. K., Huang, D. T., & Huang, L. (2022) · Biomedical Journal · doi:10.1016/j.bj.2022.04.006 · Cited by 63
“There is no clear evidence suggesting an association of this variant with increased mortality, but some reports have shown that E484K mutation may affect neutralization by several mAbs, including casirivimab, bamlanivimab, and etesevimab [28,32,48].”
Influential
SARS-CoV-2 Variants and Their Relevant Mutational Profiles: Update Summer 2021
Alkhatib, M., Svicher, V., Salpini, R., Ambrosio, F. A., Bellocchi, M. C., Carioti, L., Piermatteo, L., Scutari, R., Costa, G., Artese, A., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.01096-21 · Cited by 62
“can favor viral escape from a large variety of monoclonal antibodies and from convalescent-phase sera of recovered individuals (40, 47, 48).”
BackgroundMethod
Discovery of ultrapotent broadly neutralizing antibodies from SARS-CoV-2 elite neutralizers
Vanshylla, K., Fan, C., Wunsch, M., Poopalasingam, N., Meijers, M., Kreer, C., Kleipass, F., Ruchnewitz, D., Ercanoglu, M. S., Gruell, H., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.12.010 · Cited by 58
“R346 and N440 mutants were previously only reported in cell culture-based escape assays (Liu et al., 2021;Weisblumet al., 2020).”
Molecular Aspects Concerning the Use of the SARS-CoV‑2 Receptor Binding Domain as a Target for Preventive Vaccines
Valdés-Balbín, Y., Santana-Mederos, D., Paquet, F., Fernández-Castillo, S., Climent, Y., Chiodo, F., Rodríguez, L., Ramírez, B. S., León, K., Hernández, T., et al. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00216 · Cited by 53
Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2
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The trispecific DARPin ensovibep inhibits diverse SARS-CoV-2 variants
Rothenberger, S., Hurdiss, D. L., Walser, M., Malvezzi, F., Mayor, J., Ryter, S., Moreno, H., Liechti, N., Bosshart, A., Iss, C., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01382-3 · Cited by 75
Ten emerging SARS-CoV-2 spike variants exhibit variable infectivity, animal tropism, and antibody neutralization
Zhang, L., Cui, Z., Li, Q., Wang, B., Yu, Y., Wu, J., Nie, J., Ding, R., Wang, H., Zhang, Y., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02728-4 · Cited by 58
Pre-existing immunity modulates responses to mRNA boosters
Dangi, T., Sanchez, S., Lew, M. H., Awakoaiye, B., Visvabharathy, L., Richner, J. M., Koralnik, I. J., & Penaloza‐MacMaster, P. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112167 · Cited by 55
Understanding Mutations in Human SARS-CoV-2 Spike Glycoprotein: A Systematic Review & Meta-Analysis
Kumar, R., Srivastava, Y., Muthuramalingam, P., Singh, S. K., Verma, G., Tiwari, S., Tandel, N., Beura, S. K., Panigrahi, A. R., Maji, S., et al. (2023) · Viruses · doi:10.3390/v15040856 · Cited by 57
“Thus, S477N mutation plays a significant role in the interaction with hACE2 and confers resistance to convalescent sera and antibodies, subsequently increasing infectivity [45,46].”
Background
Emergence and outcomes of the SARS-CoV-2 ‘Marseille-4’ variant
Fournier, P., Colson, P., Levasseur, A., Devaux, C. A., Gautret, P., Bedotto, M., Delerce, J., Bréchard, L., Pinault, L., Lagier, J., et al. (2021) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2021.03.068 · Cited by 57
Rapid Increase of SARS-CoV-2 Variant B.1.1.7 Detected in Sewage Samples from England between October 2020 and January 2021
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Predicting Mutational Effects on Receptor Binding of the Spike Protein of SARS-CoV-2 Variants
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Structural and functional insights into the spike protein mutations of emerging SARS-CoV-2 variants
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“This mutant serves as an escape mutant against SARS-CoV-2 infection as it interferes with the ability of the antibodies to bind with the RBD region [53, 82, 90, 100, 101].”
Background
Physicochemical effect of the N501Y, E484K/Q, K417N/T, L452R and T478K mutations on the SARS-CoV-2 spike protein RBD and its influence on agent fitness and on attributes developed by emerging variants of concern
Pondé, R. A. D. A. (2022) · Virology · doi:10.1016/j.virol.2022.05.003 · Cited by 54
“…since it favors the virus spread, compromises the neutralizing activity of therapeutic monoclonal antibodies (Weisblum et al., 2020) and also gives the virus a ability to evade immunity induced by natural infection and by vaccination (Wang et al., 2021b; Jangra et al., 2021; Liu et al., 2021a).”
Influential
Understanding the Secret of SARS-CoV-2 Variants of Concern/Interest and Immune Escape
Lou, F., Li, M., Pang, Z., Jiang, L., Guan, L., Tian, L., Hu, J., Fan, J., & Fan, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.744242 · Cited by 54
“L452 residue did not directly interact with ACE2, but the L452R mutation could affect the structural stability of the region where S protein interacts with ACE2 and facilitate SARS-CoV-2 to enter into human respiratory organs (37), which accounted for the prevalence of B.1.427/429 in North America and B.1.617 in India.”
BackgroundInfluential
SARS-CoV-2 prefusion spike protein stabilized by six rather than two prolines is more potent for inducing antibodies that neutralize viral variants of concern
Lu, M., Chamblee, M., Zhang, Y., Ye, C., Dravid, P., Park, J., Mahesh, K., Trivedi, S., Murthy, S. S., Sharma, H., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2110105119 · Cited by 55
Inhibitors of Protein Glycosylation Are Active against the Coronavirus Severe Acute Respiratory Syndrome Coronavirus SARS-CoV-2
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“A recent addition to the armamentarium of strategies to inhibit SARS-CoV-2 is represented by neutralizing monoclonal antibodies, although their narrow window of applicability and sensitivity to Spike immunological escape mutations makes them non-resolutive [8].”
Background
Genomic analysis reveals a rapid spread and predominance of lambda (C.37) SARS‐COV‐2 lineage in Peru despite circulation of variants of concern
Padilla, C., Jimenez‐Vasquez, V., Hurtado, V., Mestanza, O., Molina, I. S., Barcena, L., Ruiz, S. M., Acedo-Lazo, S. V., Lizárraga, W. C., Bailón, H., et al. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27261 · Cited by 54
“Noteworthy, the L452Q mutation uniquely present in this variant is very similar to the L452R present in the delta variant and in the epsilon variants, which together with the D614G mutation, are considered to increase the transmissibility.(13,14)”
Background
The way of SARS-CoV-2 vaccine development: success and challenges
Dong, Y., Dai, T., Wang, B., Zhang, L., Zeng, L., Huang, J., Yan, H., Zhang, L., & Zhou, F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00796-w · Cited by 53
An ACE2-blocking antibody confers broad neutralization and protection against Omicron and other SARS-CoV-2 variants of concern
Du, W., Hurdiss, D. L., Drabek, D., Mykytyn, A. Z., Kaiser, F. K., González-Hernández, M., Muñoz‐Santos, D., Lamers, M. M., van Haperen, R., Li, W., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.abp9312 · Cited by 56
SARS-CoV-2 drug resistance and therapeutic approaches
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Dominance of Alpha and Iota variants in SARS-CoV-2 vaccine breakthrough infections in New York City
Duerr, R., Dimartino, D., Marier, C., Zappile, P., Wang, G., Lighter, J., Elbel, B. D., Troxel, A. B., & Heguy, A. (2021) · Journal of Clinical Investigation · doi:10.1172/jci152702 · Cited by 53
Immune Escape Associated with RBD Omicron Mutations and SARS-CoV-2 Evolution Dynamics
Kudriavtsev, A. V., Vakhrusheva, A., Novoseletsky, V. N., Bozdaganyan, M. E., Шайтан, К. В., Kirpichnikov, M. P., & Sokolova, O. S. (2022) · Viruses · doi:10.3390/v14081603 · Cited by 52
“The presence of this mutation led to an almost complete absence of neutralization by monoclonal antibodies C121 and C144 [43] and convalescent plasma [40,44].”
Background
One-shot identification of SARS-CoV-2 S RBD escape mutants using yeast screening
Francino-Urdaniz, I. M., Steiner, P. J., Kirby, M. B., Zhao, F., Haas, C. M., Barman, S., Rhodes, E. R., Leonard, A. C., Peng, L., Sprenger, K. G., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109627 · Cited by 47
“There have been a number of recent approaches to identify specific S escape mutants (summarized in Data S2; Baum et al., 2020; Greaney et al., 2021; Li et al., 2020; Liu et al., 2021; Weisblum et al., 2020).”
On the road to ending the COVID-19 pandemic: Are we there yet?
Case, J. B., Winkler, E. S., Errico, J. M., & Diamond, M. (2021) · Virology · doi:10.1016/j.virol.2021.02.003 · Cited by 47
Self-citation
SARS-CoV-2: phenotype, genotype, and characterization of different variants
Saberiyan, M., Karimi, E., Khademi, Z., Movahhed, P., Safi, A., & Ghahfarrokhi, A. M. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-022-00352-6 · Cited by 56
SARS-CoV-2 Entry Related Viral and Host Genetic Variations: Implications on COVID-19 Severity, Immune Escape, and Infectivity
Huang, S., & Wang, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063060 · Cited by 50
“• Enhance the infectivity and compensate the decrease of infectivity due to emerge of RBD immune escape mutations, such as D796H.”
BackgroundInfluential
Understanding mutation hotspots for the SARS-CoV-2 spike protein using Shannon Entropy and K-means clustering
Mullick, B., Magar, R., Jhunjhunwala, A., & Farimani, A. B. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104915 · Cited by 49
“This mutation lies in the region 473 – 487 which includes another mutation of significance S477 N [16,54].”
Molecular rationale for SARS-CoV-2 spike circulating mutations able to escape bamlanivimab and etesevimab monoclonal antibodies
Laurini, E., Marson, D., Aulić, S., Fermeglia, A., & Pricl, S. (2021) · Scientific Reports · doi:10.1038/s41598-021-99827-3 · Cited by 45
Dynamic Profiling of Binding and Allosteric Propensities of the SARS-CoV-2 Spike Protein with Different Classes of Antibodies: Mutational and Perturbation-Based Scanning Reveals the Allosteric Duality of Functionally Adaptable Hotspots
Verkhivker, G. M., Agajanian, S., Öztaş, D. Y., & Gupta, G. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.1c00372 · Cited by 40
Omicron variant of SARS-CoV-2 imposes a new challenge for the global public health
Xu, Z., Liu, K., & Gao, G. F. (2022) · Biosafety and Health · doi:10.1016/j.bsheal.2022.01.002 · Cited by 49
“K417N tends to affect the binding of Class 1 antibodies and is less important for polyclonal antibodies targeting RBD, which mainly relate to Class 2 antibodies [7].”
CVnCoV protects human ACE2 transgenic mice from ancestral B BavPat1 and emerging B.1.351 SARS-CoV-2
Hoffmann, D., Corleis, B., Rauch, S., Roth, N., Mühe, J., Halwe, N. J., Ulrich, L., Fricke, C., Schön, J., Kraft, A., et al. (2021) · doi:10.1101/2021.03.22.435960 · Cited by 48
Common Variable Immunodeficiency Disorders, T-Cell Responses to SARS-CoV-2 Vaccines, and the Risk of Chronic COVID-19
Ameratunga, R., Longhurst, H. J., Steele, R. H., Lehnert, K., Leung, E. Y., Brooks, A. E. S., & Woon, S. (2021) · The Journal of Allergy and Clinical Immunology In Practice · doi:10.1016/j.jaip.2021.06.019 · Cited by 49
Interactions of the Receptor Binding Domain of SARS-CoV-2 Variants with hACE2: Insights from Molecular Docking Analysis and Molecular Dynamic Simulation
Çeli̇k, İ., Yadav, R., Düzgün, Z., Albogami, S. M., El‐Shehawi, A. M., Fatimawali, F., Idroes, R., Tallei, T. E., & Emran, T. B. (2021) · Biology · doi:10.3390/biology10090880 · Cited by 49
Implication of SARS-CoV-2 Immune Escape Spike Variants on Secondary and Vaccine Breakthrough Infections
Ahmad, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.742167 · Cited by 46
Delta variant (B.1.617.2) of SARS-CoV-2: current understanding of infection, transmission, immune escape, and mutational landscape
Bhattacharya, M., Chatterjee, S., Sharma, A. R., Lee, S., & Chakraborty, C. (2022) · Folia Microbiologica · doi:10.1007/s12223-022-01001-3 · Cited by 48
Impact of new variants on SARS-CoV-2 infectivity and neutralization: A molecular assessment of the alterations in the spike-host protein interactions
Cheng, M. H., Krieger, J., Banerjee, A., Xiang, Y., Kaynak, B., Shi, Y., Arditi, M., & Bahar, İ. (2022) · iScience · doi:10.1016/j.isci.2022.103939 · Cited by 50
“…been studied in deep scanning mutagenesis (Dong et al., 2021; Greaney et al., 2021a, 2021c; Starr et al., 2020, 2021a, 2021b), in vitro evolution (Liu et al., 2021d; Muecksch et al., 2021; Wang et al., 2021c; Weisblum et al., 2020; Zahradnik et al., 2021), cryo-EM (Cai et al., 2021;…”
Influential
Engineered ACE2-Fc counters murine lethal SARS-CoV-2 infection through direct neutralization and Fc-effector activities
Chen, Y., Sun, L., Ullah, I., Beaudoin-Bussières, G., Anand, S. P., Hederman, A. P., Tolbert, W. D., Sherburn, R. T., Nguyen, D. N. P., Marchitto, L., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn4188 · Cited by 49
“neutralizing antibodies (nAbs) elicited through natural infection and vaccination act by disrupting 64 this interaction; however, selection pressure results in viral escape mutations, in many cases 65 generating VOCs with an enhanced ability to bind host receptors (12-16).”
Sequence Analysis of 20,453 Severe Acute Respiratory Syndrome Coronavirus 2 Genomes from the Houston Metropolitan Area Identifies the Emergence and Widespread Distribution of Multiple Isolates of All Major Variants of Concern
Long, S. W., Olsen, R. J., Christensen, P. A., Subedi, S., Olson, R., Davis, J. J., Saavedra, M. O., Yerramilli, P., Pruitt, L., Reppond, K., et al. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.03.004 · Cited by 46
Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants
Upadhyay, V., Lucas, A., Panja, S., Miyauchi, R., & Mallela, K. M. G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101208 · Cited by 44
A review: Antibody-dependent enhancement in COVID-19: The not so friendly side of antibodies
Sánchez‐Zuno, G. A., Matuz-Flores, M. G., González-Estévez, G., Nicoletti, F., Turrubiates‐Hernández, F. J., Mangano, K., & Muñóz-Valle, J. F. (2021) · International Journal of Immunopathology and Pharmacology · doi:10.1177/20587384211050199 · Cited by 48
“To date, 4150 mutations have been identified in the S-gene of SARSCoV-2 isolated from humans, resulting in 1246 changes in amino acids, including 187 RBD substitutions compared to the reference genome.(72) The main variants identified that seem to have high relevance in the immunogenicity of the virus are D614G, N501Y…”

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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