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A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV.
Yuan, Meng; Wu, Nicholas C; Zhu, Xueyong; Lee, Chang-Chun D; So, Ray T Y; Lv, Huibin; Mok, Chris K P; Wilson, Ian A.
  • Yuan M; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Wu NC; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Zhu X; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Lee CD; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • So RTY; HKU-Pasteur Research Pole, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China.
  • Lv H; HKU-Pasteur Research Pole, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China.
  • Mok CKP; HKU-Pasteur Research Pole, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China. ch02mkp@hku.hk wilson@scripps.edu.
  • Wilson IA; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. ch02mkp@hku.hk wilson@scripps.edu.
Science ; 368(6491): 630-633, 2020 05 08.
Article in English | MEDLINE | ID: covidwho-31567
ABSTRACT
The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the "up" conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Severe acute respiratory syndrome-related coronavirus / Spike Glycoprotein, Coronavirus / Betacoronavirus / Epitopes Type of study: Randomized controlled trials Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abb7269

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Severe acute respiratory syndrome-related coronavirus / Spike Glycoprotein, Coronavirus / Betacoronavirus / Epitopes Type of study: Randomized controlled trials Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abb7269