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