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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A phylogeny-based metric for estimating changes in transmissibility from recurrent mutations in SARS-CoV-2Preprint
Richard, D., Shaw, L. P., Lanfear, R., Corbett-Detig, R. B., Hinrichs, A. S., McBroome, J., Turakhia, Y., Acman, M., Owen, C. J., Tan, C. C. S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.06.442903 · Cited by 20
Increased lung cell entry of B.1.617.2 and evasion of antibodies induced by infection and BNT162b2 vaccinationPreprint
Arora, P., Kempf, A. M., Nehlmeier, I., Sidarovich, A., Krüger, N., Graichen, L., Moldenhauer, A.-S., Winkler, M. S., Schulz, S. R., Jäck, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.23.449568 · Cited by 20
Follow-up investigation and detailed mutational characterization of the SARS-CoV-2 Omicron variant lineages (BA.1, BA.2, BA.3 and BA.1.1)Preprint
Abbas, Q., Викторович, К. А., Sharrouf, K. A., Jyakhwo, S., & Komissarov, A. S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.25.481941 · Cited by 19
“3] This mutation shows resistance to neutralising monoclonal antibodies and increased ACE2 binding [8, 61].”
Background
Neutralisation of the SARS-CoV-2 Delta variant sub-lineages AY.4.2 and B.1.617.2 with the mutation E484K by Comirnaty (BNT162b2 mRNA) vaccine-elicited sera, Denmark, 1 to 26 November 2021
Lassaunière, R., Polacek, C., Fonager, J., Bennedbæk, M., Boding, L., Rasmussen, M., & Fomsgaard, A. (2021) · Eurosurveillance · doi:10.2807/1560-7917.es.2021.26.49.2101059 · Cited by 19
Elucidating Design Principles for Engineering Cell‐Derived Vesicles to Inhibit SARS‐CoV‐2 Infection
Gunnels, T. F., Stranford, D. M., Mitrut, R. E., Kamat, N. P., & Leonard, J. N. (2022) · Small · doi:10.1002/smll.202200125 · Cited by 18
A broadly reactive antibody targeting the N-terminal domain of SARS-CoV-2 spike confers Fc-mediated protection
Adams, L. J., VanBlargan, L. A., Liu, Z., Gilchuk, P., Zhao, H., Chen, R. E., Raju, S., Chong, Z., Whitener, B. M., Shrihari, S., et al. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101305 · Cited by 18
Self-citation
Adjuvanted SARS-CoV-2 spike protein vaccination elicits long-lived plasma cells in nonhuman primates
Prabhakaran, M. S., Matassoli, F. L., Leggat, D. J., Hoover, A., Srikanth, A., Wu, W., Henry, A. R., Wang, J. P., Lin, B. C., Teng, I., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.add5960 · Cited by 19
High avidity of vaccine-induced immunoglobulin G against SARS-CoV-2: potential relevance for protective humoral immunity
Bauer, G. (2022) · Exploration of Immunology · doi:10.37349/ei.2022.00040 · Cited by 19
Epidemiological characteristics of the B.1.526 SARS-CoV-2 variant
Yang, W., Greene, S. K., Peterson, E. R., Li, W., Mathes, R. W., Graf, L. E., Lall, R., Hughes, S., Wang, J., & Fine, A. D. (2022) · Science Advances · doi:10.1126/sciadv.abm0300 · Cited by 18
SARS-CoV-2: The Interplay Between Evolution and Host Immunity
Case, J. B., Jain, S., Suthar, M. S., & Diamond, M. (2024) · Annual Review of Immunology · doi:10.1146/annurev-immunol-083122-043054 · Cited by 26
Self-citation
Clinical, virologic and immunologic features of a mild case of SARS-CoV-2 reinfection
Vetter, P., Cordey, S., Schibler, M., Vieux, L., Després, L., Laubscher, F., Andrey, D. O., Martischang, R., Harbarth, S., Cuvelier, C., et al. (2021) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2021.02.010 · Cited by 18
Identification and Development of Therapeutics for COVID-19
Rando, H. M., Wellhausen, N., Ghosh, S., Lee, A. J., Dattoli, A. A., Hu, F., Byrd, J. B., Rafizadeh, D. N., Lordan, R., Qi, Y., et al. (2021) · mSystems · doi:10.1128/msystems.00233-21 · Cited by 25
“A comprehensive mutagenesis screen recently identified several amino acid substitutions in the SARSCoV-2 spike protein that can prevent antibody neutralization (222).”
Elucidating important structural features for the binding affinity of spike ‐ SARS‐CoV ‐2 neutralizing antibody complexes
Sharma, D., Rawat, P., Vani, J., & Gromiha, M. M. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26277 · Cited by 17
“Another study detected variants that escaped either neutralizing SARS-CoV-2 mAbs or convalescent plasma and observed that mutations S477N and E484K rank prominently among mAb escape mutations.(10) Although these mutational studies have significantly improved our knowledge on immune escape variants, they lack a large-s…”
Background
Monoclonal antibodies targeting two immunodominant epitopes on the Spike protein neutralize emerging SARS-CoV-2 variants of concern
Kováčech, B., Fialová, Ľ., Filipčík, P., Škrabana, R., Žilková, M., Ivanovova, N. P., Kováč, A., Palova, D., Rolkova, G., Tomkova, K., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.103818 · Cited by 19
Omicron-included mutation-induced changes in epitopes of SARS-CoV-2 spike protein and effectiveness assessments of current antibodies
Guo, D., Duan, H., Cheng, Y., Wang, Y., Hu, J., & Shi, H. (2022) · Molecular Biomedicine · doi:10.1186/s43556-022-00074-3 · Cited by 17
Decoding the effects of spike receptor binding domain mutations on antibody escape abilities of omicron variants
Chakraborty, S., Saha, A., Saha, C., Ghosh, S., & Mondal, T. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.08.050 · Cited by 18
Correlation between anti-S IgG and neutralizing antibody titers against three live SARS-CoV-2 variants in BNT162b2 vaccine recipients
Higashimoto, Y., Kozawa, K., Miura, H., Kawamura, Y., Ihira, M., Hiramatsu, H., Suzuki, R., Haga, K., Takai‐Todaka, R., Sawada, A., et al. (2022) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2022.2105611 · Cited by 18
“These new variants are highly infectious and can escape vaccine-induced host immunity.(27,28) In fact, neutralizing antibody titers induced by the BNT162b2 vaccine have been demonstrated to be significantly lower against the latest SARSCoV-2 Omicron variant.”
Background
Whole genome sequencing analysis of SARS-CoV-2 from Malaysia: From alpha to Omicron
Yu, C. Y., Wong, S. Y., Liew, N. W. C., Joseph, N. M. S., Zakaria, Z., Isa, N. M., Soe, H. J., Kairon, R., Nordin, S. A., & Chee, H. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.1001022 · Cited by 19
“Specifically, the RBD mutation L452R in Delta variant has been shown to reduce neutralizing activity by several monoclonal antibodies (46), convalescent plasma (62) and vaccine sera (63).”
Background
Identification of a broad sarbecovirus neutralizing antibody targeting a conserved epitope on the receptor-binding domain
Wang, Y., Zhang, Z., Yang, M., Xiong, X., Yan, Q., Cao, L., Wei, P., Zhang, Y., Zhang, L., Lv, K., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2023.113653 · Cited by 16
COVID-19 Variants and Vaccine Development
Zhao, Z., Bashiri, S., Ziora, Z. M., Tóth, I., & Skwarczyński, M. (2024) · Viruses · doi:10.3390/v16050757 · Cited by 20
Persistence of SARS‐CoV‐2 infection and viral intra ‐ and inter ‐host evolution in COVID‐19 hospitalized patients
Pavia, G., Quirino, A., Marascio, N., Veneziano, C., Longhini, F., Bruni, A., Garofalo, E., Pantanella, M., Manno, M., Gigliotti, S., et al. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29708 · Cited by 18
Mechanisms of Hepatitis C Virus Escape from Vaccine-Relevant Neutralizing Antibodies
Velázquez‐Moctezuma, R., Augestad, E. H., Castelli, M., Olesen, C. H., Clementi, N., Clementi, M., Mancini, N., & Prentoe, J. C. (2021) · Vaccines · doi:10.3390/vaccines9030291 · Cited by 18
“Further, many of the escape mutations identified in vitro have already been observed in circulating human isolates [126,127].”
Background
Neutralizing Antibody Response of Vaccinees to SARS-CoV-2 Variants
Anichini, G., Terrosi, C., Savellini, G. G., Gandolfo, C., Franchi, F., & Cusi, M. G. (2021) · Vaccines · doi:10.3390/vaccines9050517 · Cited by 18
The neutralization potency of anti-SARS-CoV-2 therapeutic human monoclonal antibodies is retained against viral variants
Makdasi, E., Zvi, A., Alcalay, R., Noy-Porat, T., Peretz, E., Mechaly, A., Levy, Y., Epstein, E., Chitlaru, T., Tennenhouse, A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109679 · Cited by 19
“Substitutions N501Y, E484K, K417N, Y453F, N439K, and S477N were among the most frequent mutations mediating immune escape and were shown to reduce and even completely abrogate the neutralizing activity of several highly potent mAbs, including those that are already in clinical use (Andreano et al., 2020; Chen et al.,…”
Computational profiling of natural compounds as promising inhibitors against the spike proteins of SARS‐CoV‐2 wild‐type and the variants of concern, viral cell‐entry process, and cytokine storm in COVID‐19
Kar, P., Saleh‐E‐In, M. M., Jaishee, N., Anandraj, A., Kormuth, E., Vellingiri, B., Angione, C., Rahman, P. K. S. M., Pillay, S., Sen, A., et al. (2022) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30243 · Cited by 23
“Though the exact role of the Thr478Lys mutation is not known, mutation at this position has been implicated in antibody escape.(41) Furthermore, abietatriene also interacted with the critical residues Asn501 and Tyr505 at the active binding pocket of the spike protein that interacts with the host ACE2 receptor.”
Background
Clinical Performance Characteristics of the Swift Normalase Amplicon Panel for Sensitive Recovery of Severe Acute Respiratory Syndrome Coronavirus 2 Genomes
Shrestha, L., Lin, M. J., Xie, H. J., Mills, M. G., Bakhash, S. A. M., Gaur, V. P., Livingston, R. J., Castor, J., Bruce, E. A., Botten, J., et al. (2022) · Journal of Molecular Diagnostics · doi:10.1016/j.jmoldx.2022.05.007 · Cited by 17
Design of Specific Primer Sets for the Detection of SARS-CoV-2 Variants of Concern B.1.1.7, B.1.351, P.1, B.1.617.2 using Artificial IntelligencePreprint
Perez-Romero, C. A., Tonda, A. P., Mendoza‐Maldonado, L., Coz, E., Tabeling, P., Vanhomwegen, J., Claassen, E., Garssen, J., Kraneveld, A. D., & Lopez‐Rincon, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.20.427043 · Cited by 18
Deep mutational engineering of broadly-neutralizing nanobodies accommodating SARS-CoV-1 and 2 antigenic drift
Laroche, A., Delgado, M. L. O., Chalopin, B., Cuniasse, P., DuBois, S. G., Sierocki, R., Gallais, F., Debroas, S., Bellanger, L., Simon, S., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2076775 · Cited by 21
Rapid and Accurate Identification of SARS-CoV-2 Omicron Variants Using Droplet Digital PCR (RT-ddPCR)
Mills, M. G., Hajian, P., Bakhash, S. M., Xie, H. J., Mantzke, D., Zhu, H., Perchetti, G. A., Huang, M.-L. W., Pepper, G., Jerome, K. R., et al. (2022) · Journal of Clinical Virology · doi:10.1016/j.jcv.2022.105218 · Cited by 17
Humoral and cellular immunity of two‐dose inactivated COVID‐19 vaccination in Chinese children: A prospective cohort study
Wang, H., Gan, M., Wu, B., Zeng, R., Wang, Z., Xu, J., Li, J., Zhang, Y., Cao, J., Chen, L., et al. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28380 · Cited by 14
The role of S477N mutation in the molecular behavior of SARS‐CoV‐2 spike protein: An in‐silico perspective
Mondeali, M., Etemadi, A., Barkhordari, K., Kesheh, M. M., Shavandi, S., Bahavar, A., Hosseini, F., Gomari, M. M., & Modarressi, M. H. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30367 · Cited by 15
“Specific neutralizing antibodies against the S protein are produced by the human immune system after the virus enters the cell or after vaccination, and most of them seem to bind to RBD. 5 Since the outbreak of this virus, several mutations have negatively affected the efficiency of both vaccination and treatment meth…”
Background
Adaptive variations in SARS-CoV-2 spike proteins: effects on distinct virus-cell entry stages
Qing, E., & Gallagher, T. (2023) · mBio · doi:10.1128/mbio.00171-23 · Cited by 17
COVID-19 mutations: An overview
Sarkar, M. S., & Madabhavi, I. (2024) · World Journal of Methodology · doi:10.5662/wjm.v14.i3.89761 · Cited by 22
Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants
Yin, R. M., Guest, J. D., Taherzadeh, G., Gowthaman, R., Mittra, I., Quackenbush, J., & Pierce, B. G. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009380 · Cited by 18
Circulation and Evolution of SARS-CoV-2 in India: Let the Data Speak
Limaye, S., Kasibhatla, S. M., Ramtirthkar, M. R., Kinikar, M., Kale, M. M., & Kulkarni‐Kale, U. (2021) · Viruses · doi:10.3390/v13112238 · Cited by 18
Ensovibep, a novel trispecific DARPin candidate that protects against SARS-CoV-2 variantsPreprint
Rothenberger, S., Hurdiss, D. L., Walser, M., Malvezzi, F., Mayor, J., Ryter, S., Moreno, H., Liechti, N., Bosshart, A., Iss, C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.03.429164 · Cited by 17
Fast SARS-CoV-2 Variant Detection Using Snapback Primer High-Resolution Melting
Lownik, J. C., Farrar, J. S., Way, G. W., McKay, A., Roychoudhury, P., Greninger, A. L., & Martin, R. (2021) · Diagnostics · doi:10.3390/diagnostics11101788 · Cited by 16
There is nothing exempt from the peril of mutation – The Omicron spike
Behl, T., Kaur, I., Sehgal, A., Singh, S., Sharma, N., Anwer, M. K., Makeen, H. A., Albratty, M., Alhazmi, H. A., Bhatia, S., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112756 · Cited by 16
Evasion of Vaccine-Induced Humoral Immunity by Emerging Sub-Variants of SARS-CoV-2
Koyama, T., Miyakawa, K., Tokumasu, R., Jeremiah, S. S., Kudo, M., & Ryo, A. (2022) · Future Microbiology · doi:10.2217/fmb-2022-0025 · Cited by 15
SARS-CoV-2 Variants in Paraguay: Detection and Surveillance with an Economical and Scalable Molecular Protocol
Martinez, M., Nguyen, P.-V., Su, M., Cardozo, F., Valenzuela, A., Franco, L. X., Galeano, M. E., Rojas, L. E., Acosta, C. C. D., Fernández, J., et al. (2022) · Viruses · doi:10.3390/v14050873 · Cited by 16
“529 (omicron), mutations at position 478 have developed in vitro and confer decreased antibody neutralization, indicating that such mutations may benefit the virus through immunity escape [33,34].”
Background
Dynamics of Viral Infection and Evolution of SARS-CoV-2 Variants in the Calabria Area of Southern Italy
Marco, C. D., Veneziano, C., Massacci, A., Pallocca, M., Marascio, N., Quirino, A., Barreca, G. S., Giancotti, A., Gallo, L., Lamberti, A. G., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.934993 · Cited by 16
Fc engineered ACE2-Fc is a potent multifunctional agent targeting SARS-CoV2
Wines, B. D., Kurtovic, L., Trist, H. M., Esparon, S. E., López, E., Chappin, K., Chan, L., Mordant, F. L., Lee, W. S., Gherardin, N. A., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.889372 · Cited by 15
“9 nM) simply replicated this hierarchy of increasing neutralization potency over trACE2-Fc-WT as variants with increased affinity for ACE2 have equivalent increased susceptibility to inhibition by ACE2, including the N439K, S477N and E484K RBDs and other variants associated with escape from neutralizing antibodies (11…”
Background
Host genetic diversity and genetic variations of SARS-CoV-2 in COVID-19 pathogenesis and the effectiveness of vaccination
Delshad, M., Sanaei, M., Pourbagheri‐Sigaroodi, A., & Bashash, D. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109128 · Cited by 18
Pathogen-host adhesion between SARS-CoV-2 spike proteins from different variants and human ACE2 studied at single-molecule and single-cell levels
Zhang, X., Hong, B., Wei, P., Pei, P., Xu, H. C., Chen, L., Tong, Y., Chen, J., Luo, S., Fan, H., et al. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2128887 · Cited by 16
“2) harbours L452R and T478K mutations in the RBD, which could enhance the stability of S protein and the affinity to ACE2 [1,11,12].”
Background
A potent, broadly protective vaccine against SARS-CoV-2 variants of concern
Wang, Z., An, J., Liu, K., Yü, P., Fang, X. D., Li, J., Zhu, H., Zhu, Q., Huang, C., Zhang, C., et al. (2022) · npj Vaccines · doi:10.1038/s41541-022-00571-0 · Cited by 15
Broad strategies for neutralizing SARS-CoV-2 and other human coronaviruses with monoclonal antibodies
Ling, Z., Yi, C., Sun, X., Yang, Z., & Sun, B. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2215-6 · Cited by 16
“…of SARS-CoV-2 escape variants under the pressure of NAbs and deep mutational scanning (DMS) experiments with yeast cells expressing all possible amino acid substitutions in the RBD have been performed to understand the escape mechanism of SARS-CoV-2 (Greaney et al., 2021; Liu et al., 2021).”
Method
Interspecies transmission of SARS CoV-2 with special emphasis on viral mutations and ACE-2 receptor homology roles
Hamdy, M. E., El‐Deeb, A. H., Hagag, N. M., Shahein, M. A., Alaidi, O., & Hussein, H. A. (2023) · International Journal of Veterinary Science and Medicine · doi:10.1080/23144599.2023.2222981 · Cited by 17
“● It causes immune evasion and a resistance to convalescent antibodies [105,106].”
Background
Specific epitopes form extensive hydrogen-bonding networks to ensure efficient antibody binding of SARS-CoV-2: Implications for advanced antibody design
Wang, D., Ge, Y., Zhong, B., & Liu, D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.03.021 · Cited by 15
Three epitope-distinct human antibodies from RenMab mice neutralize SARS-CoV-2 and cooperatively minimize the escape of mutants
Nie, J., Xie, J., Liu, S., Wu, J., Liu, C., Li, J., Liu, Y., Wang, M., Zhao, H., Zhang, Y., et al. (2021) · Cell Discovery · doi:10.1038/s41421-021-00292-z · Cited by 15
Self-citation
Mutational Hotspot in the SARS-CoV-2 Spike Protein N-Terminal Domain Conferring Immune Escape Potential
Kubik, S., Arrigo, N., Bonet, J., & Xu, Z. (2021) · Viruses · doi:10.3390/v13112114 · Cited by 16
“Since the last months of 2020, increase in frequency of other mutations was observed, with the N501Y and E484K being two prominent examples.”
BackgroundInfluential

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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