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

Meng Yuan, Nicholas C. Wu, Xueyong Zhu, Chang Chun D. Lee, Ray T.Y. So, Huibin Lv, Chris K.P. Mok, Ian A. Wilson

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)630-633
Number of pages4
JournalScience
Volume368
Issue number6491
DOIs
StatePublished - May 8 2020
Externally publishedYes

Keywords

  • COVID-19
  • severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)

ASJC Scopus subject areas

  • General

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