PreprintCited by 1,178SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approachesSARS-CoV-2 detection and testing

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Comprehensive mapping of mutations to the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human serum antibodies

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Greaney, Allison J., Loes, Andrea N., Crawford, Katharine H.D., Starr, Tyler N., Malone, Keara D., Chu, Helen Y., Bloom, Jesse D.·2021·Cell Host & Microbe

DOI 10.1101/2020.12.31.425021PMC PMC7869748

Preprint — published as 10.1016/j.chom.2021.02.003 · Paper page

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Abstract

The evolution of SARS-CoV-2 could impair recognition of the virus by human antibody-mediated immunity. To facilitate prospective surveillance for such evolution, we map how convalescent serum antibodies are impacted by all mutations to the spike’s receptor-binding domain (RBD), the main target of serum neutralizing activity. Binding by polyclonal serum antibodies is affected by mutations in three main epitopes in the RBD, but there is substantial variation in the impact of mutations both among individuals and within the same individual over time. Despite this inter- and intra-person heterogeneity, the mutations that most reduce antibody binding usually occur at just a few sites in the RBD’s receptor binding motif. The most important site is E484, where neutralization by some sera is reduced >10-fold by several mutations, including one in emerging viral lineages in South Africa and Brazil. Going forward, these serum escape maps can inform surveillance of SARS-CoV-2 evolution.

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SARS-CoV-2 variants from COVID-19 positive cases in the Free State province, South Africa from July 2020 to December 2021
Mwangi, P. N., Okendo, J., Mogotsi, M. T., Ogunbayo, A. E., Adelabu, O. A., Sondlane, H., Maotoana, M. G., Mahomed, L., Morobadi, M. D., Vawda, S., et al. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.935131 · Cited by 6
SARS-CoV-2 RBD-Specific Antibodies Induced Early in the Pandemic by Natural Infection and Vaccination Display Cross-Variant Binding and Inhibition
Walker, M. R., Podlekareva, D. N., Johnsen, S., Leerhøy, B., Fougeroux, C. E., Søgaard, M., Salanti, A., Ditlev, S. B., & Barfod, L. K. (2022) · Viruses · doi:10.3390/v14091861 · Cited by 5
“We propose that this increase is due to re-infection and subsequent boosting with the WT, which amplifies existing antibodies that target conserved epitopes on the RBD [48,49].”
Background
Recombinant Decoy Exhibits Broad Protection against Omicron and Resistance Potential to Future Variants
Tang, H., Ke, Y., Wang, L., Wu, M., Sun, T., & Zhu, J. (2022) · Pharmaceuticals · doi:10.3390/ph15081002 · Cited by 4
The chimera of S1 and N proteins of SARS-CoV-2: can it be a potential vaccine candidate for COVID-19?
Kumar, A., Ladha, A., Choudhury, A., Ikbal, A. M. A., Bhattacharjee, B., Das, T., Gupta, G., Sharma, C., Sarbajna, A., Mandal, S. C., et al. (2022) · Expert Review of Vaccines · doi:10.1080/14760584.2022.2081156 · Cited by 5
“Mutation of the E484 site to K, Q, or P in the RBD significantly reduces virus-specific antibody neutralization [46].”
Background
Antibody escape and cryptic cross-domain stabilization in the SARS-CoV-2 Omicron spike protein
Javanmardi, K., Segall-Shapiro, T. H., Chou, C.-W., Boutz, D., Olsen, R. J., Xie, X.-P., Xia, H.-J., Shi, P.-Y., Johnson, C. D., Annapareddy, A., et al. (2022) · bioRxiv · doi:10.1101/2022.04.18.488614 · Cited by 4
Genome wide screen of RNAi molecules against SARS-CoV-2 creates a broadly potent prophylaxisPreprint
Yogev, O., Weissbrod, O., Battistoni, G., Bressan, D., Naamti, A., Falciatori, I., Berkyurek, A. C., Rasnic, R., Hosmillo, M. D. T., Ilan, S., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.12.488010 · Cited by 5
In-Flight Transmission of a SARS-CoV-2 Lineage B.1.617.2 Harbouring the Rare S:E484Q Immune Escape Mutation
Martinell, M., Andersson, T., Mannsverk, S., Bergholm, J., Ellström, P., Hill, A., Lindh, J. G., & Kaden, R. (2022) · Viruses · doi:10.3390/v14030504 · Cited by 5
Neutralization Of SARS-CoV-2 Variants By A Human Polyclonal Antibody Therapeutic (COVID-HIG, NP-028) With High Neutralizing Titers To SARS-CoV-2Preprint
Toth, D. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.27.478053 · Cited by 5
“…neutralizing antibodies from natural infection, vaccination, or antibody therapeutics like convalescent plasma, monoclonals, and monoclonal cocktails (Andreano et al., 2020; Greaney et al., 2021; Tada et al., 2021; Wang et al., 2021c; Weisblum et al., 2020; West et al., 2021; Wibmer et al., 2021).”
Background
SARS-CoV-2 Variants Associated with Vaccine Breakthrough in the Delaware Valley through Summer 2021
Marques, A. D., Sherrill-Mix, S. A., Everett, J. K., Reddy, S. G., Hokama, P., Roche, A. M., Hwang, Y., Glascock, A. L., Whiteside, S. A., Graham-Wooten, J., et al. (2022) · mBio · doi:10.1128/mbio.03788-21 · Cited by 15
RETRACTED ARTICLE: Genome sequence analysis of SARS-COV-2 isolated from a COVID-19 patient in Erbil, Iraq
Hussen, B. M., Sabir, D. K., Karim, Y., Karim, K. K., & Hidayat, H. J. (2022) · Applied Nanoscience · doi:10.1007/s13204-021-02300-w · Cited by 5
“The L452R mutation, which changes the amino acid Leucine (L) to Arginine (R) at position 22917, is the main change at receptor binding domain (RBD) that inhibit the Spike glycoprotein’s reactivity, so that it become resistant to neutralizing antibodies in the sera of patients (Li et al. 2020; Greaney et al. 2021).”
Background
Retracted
Mutations of SARS-CoV-2 variants of concern escaping Spike-specific T cellsPreprint
Bert, N. L., Tan, A. T., Kunasegaran, K., Chia, A., Tan, N., Chen, Q., Hang, S. K., Qui, M., Chan, B. S.-W., Low, J. G. H., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.20.477163 · Cited by 5
Genomic Characterization of SARS-CoV-2 Isolated from Patients with Distinct Disease Outcomes in Mexico
Boukadida, C., Taboada, B., Escalera‐Zamudio, M., Iša, P., Ramírez–González, J. E., Vázquez-Pérez, J. A., Muñoz‐Medina, J. E., Grajales-Muñíz, C., González-Torres, C., Gaytán-Cervantes, J., et al. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01249-21 · Cited by 4
“In addition, E484K confers resistance to several monoclonal antibodies and significantly reduces neutralization by convalescent plasma and sera obtained from vaccinated individuals, indicating that this substitution is located in an immunodominant epitope (11, 19, 24).”
Background
Spike Protein and the Various Cell-Surface Carbohydrates: An Interaction Study
Jayaprakash, N. G., & Surolia, A. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00691 · Cited by 4
A case series of SARS-CoV-2 reinfections caused by the variant of concern Gamma in BrazilPreprint
Naveca, F. G., do Nascimento, V. A., Nascimento, F., Ogrzewalska, M., Pauvolid‐Corrêa, A., de Araújo, M. F., Arantes, I., Batista, É. L. R., Magalhães, A. L. Á., Vinhal, F. A., et al. (2021) · medRxiv · doi:10.1101/2021.11.29.21266109 · Cited by 5
Postvaccination SARS-COV-2 among Health Care Workers in New Jersey: A Genomic Epidemiological Study
Mathema, B., Chen, L., Chow, K. F., Zhao, Y., Zody, M. C., Mediavilla, J. R., Cunningham, M. H., Composto, K., Lee, A., Oschwald, D. M., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.01882-21 · Cited by 7
Neutralization of VOCs including Delta one year post COVID-19 or vaccinePreprint
Havervall, S., Marking, U. W., Gordon, M., Ng, H., Greilert‐Norin, N., Lindbo, S., Blom, K. G., Nilsson, P., Phillipson, M., Klingström, J., et al. (2021) · medRxiv · doi:10.1101/2021.08.12.21261951 · Cited by 4
“Both display three mutations in the RBD region and particularly related to the 78 E484K mutation, which has been shown to reduce antibody binding and neutralization (12).”
Background
Memory B cells control SARS-CoV-2 variants upon mRNA vaccination of naive and COVID-19 recovered individualsPreprint
Sokal, A., Spaeth, G. B., Fernández, I., Broketa, M., Azzaoui, I., Selle, A. D. L., Vandenberghe, A., Fourati, S., Roeser, A., Meola, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.17.448459 · Cited by 5
Ultrafast topological data analysis reveals pandemic-scale dynamics of convergent evolutionPreprint
Bleher, M., Hahn, L., Neumann, M., Ardern, Z., Patiño-Galindo, J. Á., Carrière, M., Bauer, U., Rabadán, R., & Ott, A. (2021) · medRxiv · doi:10.1101/2021.06.10.21258550 · Cited by 3
“[9].”
BackgroundInfluential
Host–pathogen dynamics in longitudinal clinical specimens from patients with COVID-19
Lin, M. J., Rachleff, V. M., Xie, H. J., Shrestha, L., Lieberman, N. A. P., Peddu, V., Addetia, A., Casto, A. M., Breit, N., Mathias, P. C., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-09752-2 · Cited by 6
Return to normal: COVID-19 vaccination under mitigation measures
Marziano, V., Guzzetta, G., Mammone, A., et al. (2021) · medRxiv · doi:10.1101/2021.03.19.21253893 · Cited by 5
An Updated Investigation Prior To COVID-19 Vaccination Program In Indonesia: Full-Length Genome Mutation Analysis Of SARS-CoV-2Preprint
Nidom, R. V., Indrasari, S., Normalina, I., Nidom, A. N., Afifah, B., Dewi, L., Putra, A. K., Ansori, A. N. M., Kusala, M. K. J., Alamudi, M. Y., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.26.426655 · Cited by 11
Omicron BA.2 specifically evades broad sarbecovirus neutralizing antibodiesPreprint
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Cholera toxin B scaffolded, focused SIV V2 epitope elicits antibodies that influence the risk of SIVmac251 acquisition in macaques
Rahman, M. A., Becerra‐Flores, M., Patskovsky, Y., de Castro, I. S., Bissa, M., Basu, S., Shen, X., Williams, L. D., Sarkis, S., N’Guessan, K. F., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1139402 · Cited by 5
Antibody isotype epitope mapping of SARS‐CoV‐2 Spike RBD protein: Targets for COVID‐19 symptomatology and disease control
Contreras, M., Vicente, J., Cerón, J. M. C., Martı́nez-Subiela, S., Urra, J. M., Rodríguez‐del‐Río, F. J., Ferreras‐Colino, E., Vaz‐Rodrigues, R., de Mera, I. G. F., Antunes, S., et al. (2023) · European Journal of Immunology · doi:10.1002/eji.202250206 · Cited by 5
Comparative study of clinical features and vaccination status in Omicron and non-Omicron infected patients during the third wave in Mumbai, India
Takke, A., Zarekar, M., Muthuraman, V., Ashar, A., Patil, K., Badhavkar, A., Trivedi, J., Khargekar, N. C., Madkaikar, M. R., & Banerjee, A. (2022) · Journal of Family Medicine and Primary Care · doi:10.4103/jfmpc.jfmpc_430_22 · Cited by 4
SARS-CoV-2 Omicron Variant Genomic Sequences and Their Epidemiological Correlates Regarding the End of the Pandemic: In Silico Analysis
Kumar, A., Asghar, A., Singh, H. N., Faiq, M. A., Kumar, S., Narayan, R. K., Kumar, G., Dwivedi, P., Sahni, C., Jha, R. K., et al. (2022) · JMIR Bioinformatics and Biotechnology · doi:10.2196/42700 · Cited by 5
SARS-CoV-2 Variants Screening in Burkina Faso
Soubeïga, S. T., Institut de Recherche en Sciences de la Santé (IRSS) /Laboratoire de Recherche Biomédicale (LaReBio), O., Charlotte, K., Zouré, A. A., Institut de Recherche en Sciences de la Santé (IRSS) /Laboratoire de Recherche Biomédicale (LaReBio), O., Compaore, T. R., Institut de Recherche en Sciences de la Santé (IRSS) /Laboratoire de Recherche Biomédicale (LaReBio), O., Zida, S., Institut de Recherche en Sciences de la Santé (IRSS) /Laboratoire de Recherche Biomédicale (LaReBio), O., Kagembega, A., et al. (2022) · Journal of Medical Microbiology and Infectious Diseases · doi:10.52547/jommid.10.3.135 · Cited by 3
Potential Coronaviral Inhibitors of the Nucleocapsid Protein Identified In Silico and In Vitro from a Large Natural Product Library
Pohler, A., Abdelfatah, S., Riedl, M., Meesters, C., Hildebrandt, A., & Efferth, T. (2022) · Pharmaceuticals · doi:10.3390/ph15091046 · Cited by 5
“This represents a considerable challenge for the prevention of COVID-19 by vaccination and treatment by chemical drugs [22,24,25].”
Background
SARS-CoV-2 Intermittent Virulence as a Result of Natural Selection
Rubio‐Casillas, A., Redwan, E. M. M. M., & Uversky, V. N. (2022) · COVID · doi:10.3390/covid2080080 · Cited by 5
A review of mass spectrometry‐based analyses to understand COVID‐19 convalescent plasma mechanisms of action
Baros‐Steyl, S. S., Heialy, S. A., Semreen, A. H., Semreen, M. H., Blackburn, J. M., & Soares, N. C. (2022) · PROTEOMICS · doi:10.1002/pmic.202200118 · Cited by 4
“Therefore, Beta and Gamma, but not Alpha, could potentially increase the risk of infection in convalescent and/or vaccinated individuals (Greaney et al., 2021; Planas et al., 2021; Wibmer et al., 2021).”
Background
Longitudinal Analysis of Coronavirus-Neutralizing Activity in COVID-19 Patients
Hastert, F. D., Henß, L., von Rhein, C., Gerbeth, J., Wieters, I., Borgans, F., Khodamoradi, Y., Zacharowski, K. D., Rohde, G. G. U., Vehreschild, M. J. G. T., et al. (2022) · Viruses · doi:10.3390/v14050882 · Cited by 6
SARS-CoV-2 evolution and immune escape in immunocompromised patients treated with exogenous antibodies
Scherer, E., Babiker, A., Adelman, M., Allman, B., Key, A., Kleinhenz, J., Langsjoen, R. M., Nguyen, P.-V., Onyechi, I., Sherman, J. D., et al. (2022) · medRxiv · doi:10.1101/2022.04.12.22273675 · Cited by 4
Immune dynamics of SARS-CoV-2 virus evolution
Kamat, M., Kurlawala, V., Ghosh, G., & Vaishnav, R. (2022) · International Journal of Molecular and Immuno Oncology · doi:10.25259/ijmio_26_2021 · Cited by 4
Capturing a crucial ‘disorder-to-order transition’ at the heart of the coronavirus molecular pathology – triggered by highly persistent, interchangeable salt-bridges
Roy, S., Ghosh, P., Bandyopadhyay, A., et al. (2021) · bioRxiv · doi:10.1101/2021.12.29.474439 · Cited by 4
“Following earlier studies on the use of the SARS-CoV-2 Spike glycoprotein [15,52,53], the cryo-EM structure of its pre-fusion form (PDB ID: 6XR8, 2.”
Method
Comprehensive characterization of the antibody responses to SARS-CoV-2 Spike protein after infection and/or vaccination
Garrett, M., Galloway, J. G., Wolf, C., et al. (2021) · bioRxiv · doi:10.1101/2021.10.05.463210 · Cited by 4
Self-citation
Association of E484K and L452R spike protein mutations with SARS-CoV-2 infection in vaccinated persons---Maryland, January - May 2021
Feder, K. A., Patel, A., Vepachedu, V. R., et al. (2021) · medRxiv · doi:10.1101/2021.07.29.21261006 · Cited by 4
“Consistent with past research (7-11,15,16), this suggests that the three COVID-19 vaccines examined here may have been less effective against viruses carrying the E484K mutation than they were against the population of viruses not carrying this mutation that were circulating in Maryland during early 2021.”
Probing the Increased Virulence of Severe Acute Respiratory Syndrome Coronavirus 2 B.1.617 (Indian Variant) From Predicted Spike Protein Structure
Hajj-Hassan, H., Hamze, K., Abdel‐Sater, F., Kizilbash, N., & Khachfe, H. M. (2021) · Cureus · doi:10.7759/cureus.16905 · Cited by 5
COVID- e Vax, an electroporated plasmid DNA vaccine candidate encoding the SARS-CoV-2 Receptor Binding Domain, elicits protective immune responses in animal models of COVID-19Preprint
Conforti, A., Marra, E., Palombo, F., Roscilli, G., Ravà, M., Fumagalli, V., Muzi, A., Maffei, M., Luberto, L., Lione, L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.14.448343 · Cited by 2
SARS-CoV-2 infection of BNT162b2(mRNA)-vaccinated individuals is not restricted to variants of concern or high-risk exposure environmentsPreprint
Magalis, B. R., Mavian, C. N., Tagliamonte, M. S., Rich, S. N., Cash, M. N., Riva, A., Loeb, J. C., Norris, M. H., Amador, D. M., Zhang, Y., et al. (2021) · medRxiv · doi:10.1101/2021.05.19.21257237 · Cited by 4
Review of: "Efficacy of the ChAdOx1 nCoV-19 Covid-19 Vaccine against the B.1.351 Variant"
Lundstrom, K. H. (2021) · Qeios · doi:10.32388/8itiky · Cited by 1
“A question of significant interest is whether enhanced immune responses can be achieved by extending the time between the first and second immunization [6,7], which could also improve the neutralization activity against the B.”
Background
Coronavirus Variants—Will New mRNA Vaccines Meet the Challenge?
Welsh, J. (2021) · Engineering · doi:10.1016/j.eng.2021.04.005 · Cited by 4
“In addition, some mutations may enable the virus to reinfect those who have recovered, with antibodies from people who have recovered from natural infections shown to be less protective against several of the new variants [5].”
Background
SARS‐CoV‐2 mutations: A strain on efficacy of neutralizing monoclonal antibodies?
Boskovic, M., Migo, W., & Likić, R. (2021) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.14849 · Cited by 5
“28 lineages, South Africa and Brazil, respectively) demonstrated an increased affinity for the ACE-2 receptor.(11) Further, they also showed substantial variation in impact of mutations among individuals as well as within the same individual over time.”
BackgroundInfluential
Nasal Mask: An Alternative to Prevent Contagion during Essential Activities
Acosta-Altamirano, G. (2021) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2021.34.005595 · Cited by 4
A novel precision-serology assay for SARS-CoV-2 infection based on linear B-cell epitopes of Spike protein
Lundin, S. B., Kann, H., Fulurija, A., Andersson, B., Nakka, S. S., Andersson, L., Gisslén, M., & Harandi, A. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1166924 · Cited by 3
“It was shown that a mutation in this residue can greatly reduce the neutralisation ability of sera from SARS-CoV-2 infected individuals (23).”
Background
Evaluation of Analytical and Clinical Performance and Usefulness in a Real-Life Hospital Setting of Two in-House Real-Time RT-PCR Assays to Track SARS-CoV-2 Variants of Concern
Moisan, A., Soares, A., Oliveira, F. D., Alessandri-Gradt, É., Lecoquierre, F., Fourneaux, S., Plantier, J., & Gueudin, M. (2023) · Viruses · doi:10.3390/v15051115 · Cited by 3
Multiplex RT Real-Time PCR Based on Target Failure to Detect and Identify Different Variants of SARS-CoV-2: A Feasible Method That Can Be Applied in Clinical Laboratories
Pham, V. H., Pham, H. T., Balzanelli, M. G., Distratis, P., Lazzaro, R., Nguyễn, Q. V., Tran, V. Q., Tran, D. K., Phan, L. D., Pham, S. M., et al. (2023) · Diagnostics · doi:10.3390/diagnostics13081364 · Cited by 4
A SARS-CoV-2 Vaccine Designed for Manufacturability Results in Unexpected Potency and Non-Waning Humoral Response
Campbell, E., Dobkin, J., Osorio, L., Kolloli, A., Ramasamy, S., Kumar, R., Sant’Angelo, D. B., Subbian, S., Denzin, L. K., & Anderson, S. (2023) · Vaccines · doi:10.3390/vaccines11040832 · Cited by 3
“By focusing the immune response on the region of the spike protein, where the bulk of the epitopes for neutralizing (including broadly neutralizing) antibodies reside [34,35], we aimed to enable high potency.”
Background
In Silico Evaluation of CRISPR-Based Assays for Effective Detection of SARS-CoV-2
Kaewsapsak, P., Chantaravisoot, N., Nimsamer, P., Mayuramart, O., Mankhong, S., & Payungporn, S. (2022) · Pathogens · doi:10.3390/pathogens11090968 · Cited by 3
“The E484 mutation was shown to reduce the neutralization of polyclonal human plasma antibodies [11].”
Background
Impact of SARS-CoV-2 RBD Mutations on the Production of a Recombinant RBD Fusion Protein in Mammalian Cells
Gerez, G., Martinez, J., Steinbrugger, C., Bouanich, S., Dimino, J., Piegay, C., Combe, M., Berthier, F., & Daniel, S. (2022) · Biomolecules · doi:10.3390/biom12091170 · Cited by 3
Evolution to increased positive charge on the viral spike protein may be part of the adaptation of SARS-CoV-2 to human transmissionPreprint
Cotten, M. L., & Phan, M. V. T. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.30.502143 · Cited by 2
COVID-19: A Systematic Review of the Transmissibility, Pathogenesis, Entry Factors, and Signature Immune Response
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“Mapping RBD mutations that affect the binding of neutralizing antibodies also reveals E484 to be the most crucial residue [242].”
Background
Next-generation intranasal Covid-19 vaccine: a polymersome-based protein subunit formulation that provides robust protection against multiple variants of concern and early reduction in viral load of the upper airway in the golden Syrian hamster modelPreprint
Lam, J. H., Shivhare, D., Chia, T. W., Chew, S. L., Sinsinbar, G., Aw, T. Y., Wong, S., Venkatraman, S., Lim, F. W. I., Vandepapelière, P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.12.480188 · Cited by 3

Authors: Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D.
Affiliations: University of Washington (US)
Howard Hughes Medical Institute (US)
Fred Hutch Cancer Center (US)
Corresponding author: Bloom, Jesse D.
ORCID: Greaney, Allison J.
Loes, Andrea N.
Crawford, Katharine H.D.
Starr, Tyler N.
Chu, Helen Y.
Bloom, Jesse D.
Venue: Cell Host & Microbe
Publisher: openRxiv
Published: 2021-01-04
Volume: 29
Issue: 3
Pages: 463-476.e6
ISSN: 1931-3128 (ISSN-L)
DOI: 10.1101/2020.12.31.425021
PMC: PMC7869748
OpenAlex: W3127852352
Cited by: 1,178
References: 58
Citations by year: 2026: 43 · 2025: 64 · 2024: 79 · 2023: 158 · 2022: 361 · 2021: 459
FWCI: 83.77
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Cell Host & Microbe (publishedVersion)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Howard Hughes Medical Institute
Bill and Melinda Gates Foundation (INV-004949)
Damon Runyon Cancer Research Foundation (DRG-2381-19)
Washington Research Foundation
Vanderbilt University
University of Washington
National Institutes of Health (1s10od028685-01)
National Institute of Allergy and Infectious Diseases (R01AI127893, T32AI083203, F30AI149928, R01AI140891, R01AI141707)
Office of Research Infrastructure Programs, National Institutes of Health (S10OD028685)
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
Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 detection and testing
Keywords: SARS-CoV-2, spike protein receptor-binding domain, antibody escape mutations, neutralizing antibodies, E484K mutation, antibody epitopes, convalescent plasma, humoral immunity
MeSH terms: Protein Domains, COVID-19, SARS-CoV-2, Adult, Aged, Antibodies, Monoclonal, Antibodies, Viral, Binding Sites, Cell Line, Female, Humans, Male, Middle Aged, Mutation, Prospective Studies, Protein Binding, Receptors, Virus, Young Adult, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus

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Comprehensive mapping of mutations to the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human serum antibodies

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