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A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV
Preprint
in English
| bioRxiv
| ID: ppbiorxiv-991570
ABSTRACT
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. ONE SENTENCE SUMMARYStructural study of a cross-reactive SARS antibody reveals a conserved epitope on the SARS-CoV-2 receptor-binding domain.
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Full text:
Available
Collection:
Preprints
Database:
bioRxiv
Type of study:
Rct
Language:
English
Year:
2020
Document type:
Preprint
