ArticleCell host & microbe2022
The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants.
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Article in Cell host & microbe, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54citing papers in PubMed
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54 citing papers in PubMed.
- Structural serology of polyclonal antibody responses to mRNA-1273 and NVX-CoV2373 COVID-19 vaccines.Cell reports · 2025Trial
- Explainable convolutional neural network model provides an alternative genome-wide association perspective on mutations in SARS-CoV-2.Scientific reports · 2026Article
- A computational pipeline to discover potential cross-reactive antibodies: a case study on coronavirus.Frontiers in cellular and infection microbiology · 2026Article
- Cross-reactive sarbecovirus antibodies induced by mosaic RBD nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure and function of an unusual R452-dependent monoclonal antibody against SARS-CoV-2.Journal of virology · 2025Article
- Cross-reactive sarbecovirus antibodies induced by mosaic RBD-nanoparticles.bioRxiv : the preprint server for biology · 2025Article
- Allosteric Control and Glycan Shielding Adaptations in the SARS-CoV-2 Spike from Early to Peak Virulence.bioRxiv : the preprint server for biology · 2025Article
- Structural Immunology of SARS-CoV-2.Immunological reviews · 2025Review
- Super broad and protective nanobodies against Sarbecoviruses including SARS-CoV-1 and the divergent SARS-CoV-2 subvariant KP.3.1.1.PLoS pathogens · 2024Article
- Two-dimensional high-throughput on-cell screening of immunoglobulins against broad antigen repertoires.Communications biology · 2024Article
- A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity.Cell reports. Medicine · 2024Article
- Emerging variants develop total escape from potent monoclonal antibodies induced by BA.4/5 infection.Nature communications · 2024Article
- The SARS-CoV-2 neutralizing antibody response to SD1 and its evasion by BA.2.86.Nature communications · 2024Article
- AlphaFold2-Enabled Atomistic Modeling of Structure, Conformational Ensembles, and Binding Energetics of the SARS-CoV-2 Omicron BA.2.86 Spike Protein with ACE2 Host Receptor and Antibodies: Compensatory Functional Effects of Binding Hotspots in Modulating Mechanisms of Receptor Binding and Immune Escape.Journal of chemical information and modeling · 2024Article
- Single-molecule force stability of the SARS-CoV-2-ACE2 interface in variants-of-concern.Nature nanotechnology · 2024Article
- Immunogenicity of Tetravalent Protein Vaccine SCTV01E-2 against SARS-CoV-2 EG.5 Subvaraint: A Phase 2 Trial.Vaccines · 2024Article
- A monoclonal antibody targeting a large surface of the receptor binding motif shows pan-neutralizing SARS-CoV-2 activity.Nature communications · 2024Article
- Structural and biochemical rationale for Beta variant protein booster vaccine broad cross-neutralization of SARS-CoV-2.Scientific reports · 2024Article
- Cryo-electron microscopy in the study of virus entry and infection.Frontiers in molecular biosciences · 2024Review
- Article
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Authors and funding
31 authors.
Chang LiuWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science Oxford Institute, University of Oxford, Oxford, UK.
Daming ZhouChinese Academy of Medical Science Oxford Institute, University of Oxford, Oxford, UK; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Rungtiwa NutalaiWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Helen M E DuyvesteynDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Aekkachai TuekprakhonWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Helen M GinnDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Wanwisa DejnirattisaiWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Piyada SupasaWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Alexander J MentzerWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
Beibei WangWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
James Brett CaseDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Yuguang ZhaoDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Donal T SkellyOxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Nuffield Department of Clinical Neurosciences, University of Oxford, Oxford, UK.
Rita E ChenDepartment of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA; Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Sile Ann JohnsonOxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Thomas G RitterOxford University Hospitals NHS Foundation Trust, Oxford, UK.
Chris MasonOxford University Hospitals NHS Foundation Trust, Oxford, UK.
Tariq MalikNational Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.
Nigel TempertonViral Pseudotype Unit, Medway School of Pharmacy, University of Kent and Greenwich, Chatham Maritime, Kent ME4 4TB, UK.
Neil G PatersonDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Mark A WilliamsDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
David R HallDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Daniel K ClareDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Andrew HoweDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Philip J R GoulderPeter Medawar Building for Pathogen Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Department of Paediatrics, University of Oxford, Oxford, UK.
Elizabeth E FryDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Michael S DiamondDepartment of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA; Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA; Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA; The Andrew M. and Jane M. Bursky Center for Human Immunology and Immunotherapy Programs, Washington University School of Medicine, St. Louis, MO 63110, USA.
Juthathip MongkolsapayaWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science Oxford Institute, University of Oxford, Oxford, UK; Siriraj Center of Research Excellence in Dengue & Emerging Pathogens, Dean Office for Research, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand. Electronic address: jmongkol@well.ox.ac.uk.
Jingshan RenDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK. Electronic address: ren@strubi.ox.ac.uk.
David I StuartWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science Oxford Institute, University of Oxford, Oxford, UK; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK; Instruct-ERIC, Oxford House, Parkway Court, John Smith Drive, Oxford, UK. Electronic address: dave@strubi.ox.ac.uk.
Gavin R ScreatonWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science Oxford Institute, University of Oxford, Oxford, UK. Electronic address: gavin.screaton@medsci.ox.ac.uk.
Funding
Human antibody-based countermeasures against the Wuhan Coronavirus SARS-CoV-2R01AI157155 · NIAID · WASHINGTON UNIVERSITY · PI BARIC, RALPH S, CROWE, JAMES E · 2020 to 2024
$6.0MMedical Research Council MC_PC_17137Medical Research Council MR/N00065X/1Medical Research Council MR/V001329/1NIAID NIH HHS R01 AI157155Wellcome Trust 203224/Z/16/Z
Abstract
Alpha-B.1.1.7, Beta-B.1.351, Gamma-P.1, and Delta-B.1.617.2 variants of SARS-CoV-2 express multiple mutations in the spike protein (S). These may alter the antigenic structure of S, causing escape from natural or vaccine-induced immunity. Beta is particularly difficult to neutralize using serum induced by early pandemic SARS-CoV-2 strains and is most antigenically separated from Delta. To understand this, we generated 674 mAbs from Beta-infected individuals and performed a detailed structure-function analysis of the 27 most potent mAbs: one binding the spike N-terminal domain (NTD), the rest the receptor-binding domain (RBD). Two of these RBD-binding mAbs recognize a neutralizing epitope conserved between SARS-CoV-1 and -2, while 18 target mutated residues in Beta: K417N, E484K, and N501Y. There is a major response to N501Y, including a public IgVH4-39 sequence, with E484K and K417N also targeted. Recognition of these key residues underscores why serum from Beta cases poorly neutralizes early pandemic and Delta viruses.
Indexed as
AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntibody FormationCells, CulturedChlorocebus aethiopsCOVID-19FemaleHEK293 CellsHumansMaleMiceMice, TransgenicNeutralization TestsProtein BindingAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralSpike Glycoprotein, CoronavirusantibodyBeta variantCOVID-19immune responsesneutralizationreceptor-binding domainSARS-CoV-2spike proteinstructurevaccine
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