2. Academic Validation
  3. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV

A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV

  • Science. 2020 May 8;368(6491):630-633. doi: 10.1126/science.abb7269.
Meng Yuan  # 1,  Nicholas C Wu  # 1,  Xueyong Zhu 1,  Chang-Chun D Lee 1,  Ray T Y So 2,  Huibin Lv 2,  Chris K P Mok 3,  Ian A Wilson 4 5
Affiliations

Affiliations

  • 1 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • 2 HKU-Pasteur Research Pole, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China.
  • 3 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.
  • 4 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. ch02mkp@hku.hk wilson@scripps.edu.
  • 5 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.
  • # Contributed equally.
PMID: 32245784 DOI: 10.1126/science.abb7269
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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