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The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants.
Liu, Chang; Zhou, Daming; Nutalai, Rungtiwa; Duyvesteyn, Helen M E; Tuekprakhon, Aekkachai; Ginn, Helen M; Dejnirattisai, Wanwisa; Supasa, Piyada; Mentzer, Alexander J; Wang, Beibei; Case, James Brett; Zhao, Yuguang; Skelly, Donal T; Chen, Rita E; Johnson, Sile Ann; Ritter, Thomas G; Mason, Chris; Malik, Tariq; Temperton, Nigel; Paterson, Neil G; Williams, Mark A; Hall, David R; Clare, Daniel K; Howe, Andrew; Goulder, Philip J R; Fry, Elizabeth E; Diamond, Michael S; Mongkolsapaya, Juthathip; Ren, Jingshan; Stuart, David I; Screaton, Gavin R.
  • Liu C; Wellcome 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.
  • Zhou D; 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.
  • Nutalai R; Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
  • Duyvesteyn HME; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
  • Tuekprakhon A; Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
  • Ginn HM; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Dejnirattisai W; Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
  • Supasa P; Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
  • Mentzer AJ; Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
  • Wang B; Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
  • Case JB; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
  • Zhao Y; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
  • Skelly DT; Oxford 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.
  • Chen RE; Department 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.
  • Johnson SA; Oxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
  • Ritter TG; Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
  • Mason C; Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
  • Malik T; National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.
  • Temperton N; Viral Pseudotype Unit, Medway School of Pharmacy, University of Kent and Greenwich, Chatham Maritime, Kent ME4 4TB, UK.
  • Paterson NG; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Williams MA; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Hall DR; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Clare DK; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Howe A; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Goulder PJR; Peter Medawar Building for Pathogen Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Department of Paediatrics, University of Oxford, Oxford, UK.
  • Fry EE; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
  • Diamond MS; Department 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,
  • Mongkolsapaya J; Wellcome 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
  • Ren J; Division 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.
  • Stuart DI; Wellcome 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
  • Screaton GR; Wellcome 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.
Cell Host Microbe ; 30(1): 53-68.e12, 2022 01 12.
Article in English | MEDLINE | ID: covidwho-1536483
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral / Antibody Formation Topics: Vaccines / Variants Limits: Animals / Female / Humans / Male Language: English Journal: Cell Host Microbe Journal subject: Microbiology Year: 2022 Document Type: Article Affiliation country: J.chom.2021.11.013

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral / Antibody Formation Topics: Vaccines / Variants Limits: Animals / Female / Humans / Male Language: English Journal: Cell Host Microbe Journal subject: Microbiology Year: 2022 Document Type: Article Affiliation country: J.chom.2021.11.013