ArticleNature structural & molecular biology2020
Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient.
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Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 211 papers.
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211citing papers in PubMed
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211 citing papers in PubMed, 329 citations in OpenAlex.
- Antibody Affinity Maturation by Yeast Mating against a Diverse Antigen Library Enhances Antibody Resistance to Viral Mutations.ACS pharmacology & translational science · 2026Article
- Variant-specific spike conformational dynamics shape memory B cell selection during recall.bioRxiv : the preprint server for biology · 2026Article
- Development of a recombinant single-cycle influenza viral vector as an intranasal vaccine against SARS-CoV-2.Scientific reports · 2026Article
- ST-Analyzer: A Packaged Web and Command-Line Interface for Simulation Trajectory Analysis.bioRxiv : the preprint server for biology · 2026Article
- IgG-Bridging-Seeded Synergistic Aggregation of SARS-CoV-2 Spikes Underlies Potent Neutralization by a Low-Affinity Antibody.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Humoral epitope dominance and immune imprinting by SARS-CoV-1 and SARS-CoV-2 vaccines.Immunology and cell biology · 2026Article
- Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM.Nature chemical biology · 2026Article
- Development of a Recombinant Single-Cycle Influenza Viral Vector as an Intranasal Vaccine against SARS-CoV-2 and SARS-like Betacoronaviruses.bioRxiv : the preprint server for biology · 2025Article
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- An RBD-Fc mucosal vaccine provides variant-proof protection against SARS-CoV-2 in mice and hamsters.NPJ vaccines · 2025Article
- A bivalent spike-targeting nanobody with anti-sarbecovirus activity.Journal of nanobiotechnology · 2025Article
- Affinity maturation endows potent activity onto class 6 SARS-CoV-2 broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Viral glycoprotein-mediated entry and antibody-mediated immunity in HIV-1 and SARS-CoV-2 infection.Frontiers in immunology · 2025Review
- A human monoclonal antibody neutralizing SARS-CoV-2 Omicron variants containing the L452R mutation.Journal of virology · 2024Article
- Profiling serum immunodominance following SARS-CoV-2 primary and breakthrough infection reveals distinct variant-specific epitope usage and immune imprinting.PLoS pathogens · 2024Article
- Mosaic sarbecovirus nanoparticles elicit cross-reactive responses in pre-vaccinated animals.Cell · 2024Article
- Proactive vaccination using multiviral Quartet Nanocages to elicit broad anti-coronavirus responses.Nature nanotechnology · 2024Article
- Neutralizing antibodies reveal cryptic vulnerabilities and interdomain crosstalk in the porcine deltacoronavirus spike protein.Nature communications · 2024Article
- The presence of broadly neutralizing anti-SARS-CoV-2 RBD antibodies elicited by primary series and booster dose of COVID-19 vaccine.PLoS pathogens · 2024Article
151 more citing papers are in PubMed but not listed here.
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Authors and funding
40 authors at 12 institutions in 4 countries.
Daming Zhou *Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
Helen M E Duyvesteyn *Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
Cheng-Pin Chen *Department of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and National Yang-Ming University, Taipei, Taiwan.
Chung-Guei HuangResearch Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
Ting-Hua ChenGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Shin-Ru ShihResearch Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
Yi-Chun LinDepartment of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and Taipei Medical University, Taipei, Taiwan.
Chien-Yu ChengDepartment of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and National Yang-Ming University, Taipei, Taiwan.
Shu-Hsing ChengDepartment of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and Taipei Medical University, Taipei, Taiwan.
Yhu-Chering HuangDivision of Pediatric Infectious Diseases, Department of Pediatrics, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
Tzou-Yien LinDivision of Pediatric Infectious Diseases, Department of Pediatrics, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
Che MaGenomics Research Center, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0000-0002-4741-2307
Jiandong HuoDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
Loic CarriqueDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
Tomas MalinauskasDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.ORCID http://orcid.org/0000-0002-4847-5529
Reinis R RuzaDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
Pranav N M ShahDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
Tiong Kit TanMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.ORCID http://orcid.org/0000-0001-8746-8308
Pramila RijalMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.
Robert F DonatMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.
Kerry GodwinNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Karen R ButtigiegNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Julia A TreeNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Julika RadeckeDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Neil G PatersonDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.ORCID http://orcid.org/0000-0003-4292-6971
Piyada SupasaNuffield Department of Medicine, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
Juthathip MongkolsapayaNuffield Department of Medicine, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
Gavin R ScreatonNuffield Department of Medicine, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3549-4309
Miles W CarrollNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Javier Gilbert-JaramilloWilliam Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0003-1268-2304
Michael L KnightWilliam Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-8780-1630
William JamesWilliam Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-2506-1198
Raymond J OwensDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.ORCID http://orcid.org/0000-0002-3705-2993
James H NaismithDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.ORCID http://orcid.org/0000-0001-6744-5061
Alain R TownsendMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.
Elizabeth E FryDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.ORCID http://orcid.org/0000-0001-9754-5303
Yuguang Zhao *Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.ORCID http://orcid.org/0000-0001-8916-8552
Jingshan RenDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.ORCID http://orcid.org/0000-0003-4015-1404
David I StuartDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK. dave@strubi.ox.ac.uk.ORCID http://orcid.org/0000-0002-3426-4210
Kuan-Ying A HuangResearch Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan. arthur1726@cgmh.org.tw.ORCID http://orcid.org/0000-0001-6891-6945
Centre for Human Genetics · GBChang Gung University · TWPublic Health England · GBUniversity of Oxford · GBChang Gung Memorial Hospital · TWChinese Academy of Medical Sciences & Peking Union Medical College · CNDiamond Light Source · GBGenomics Research Center, Academia Sinica · TWJohn Radcliffe Hospital · GBMinistry of Health and Welfare · TWNational Yang Ming Chiao Tung University · TWSiriraj Hospital · TH
Funding
Cancer Research UK 26752Medical Research Council MR/N00065X/1Medical Research Council MR/V001329/1Wellcome Trust 090532/Z/09/ZWellcome Trust 101122/Z/13/Z
Abstract
The COVID-19 pandemic has had an unprecedented health and economic impact and there are currently no approved therapies. We have isolated an antibody, EY6A, from an individual convalescing from COVID-19 and have shown that it neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1. EY6A Fab binds the receptor binding domain (RBD) of the viral spike glycoprotein tightly (K
Indexed as
AdultAngiotensin-Converting Enzyme 2AnimalsAntibodies, NeutralizingAntibodies, ViralBetacoronavirusBinding SitesChlorocebus aethiopsCoronavirus InfectionsCOVID-19Cross ReactionsCryoelectron MicroscopyCrystallography, X-RayEpitopesHumansImmunoglobulin Fab FragmentsACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralEpitopesImmunoglobulin Fab FragmentsPeptidyl-Dipeptidase ASpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2
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