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

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Author Name

Meng Yuan

Published 11 Projects

Immunology Microbiology

Nicholas C Wu

Chang-Chun D. Lee

Ray T. Y. So

Published 1 Project


Huibin Lv

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Chris K. P. Mok

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Published in Science, 2020-04-03

The outbreak of COVID-19, which is caused by SARS-CoV-2 virus, continues to spread globally, but there is currently very little understanding of the epitopes on the virus. In this study, we have determined the crystal structure of the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein in complex with CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient. CR3022 targets a highly conserved epitope that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding site can only be accessed when at least two RBDs on the trimeric S protein are in the ″up″ conformation. Overall, this study provides structural and molecular insight into the antigenicity of SARS-CoV-2.

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