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
em En
| MEDLINE
| ID: mdl-32245784
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Coronavírus Relacionado à Síndrome Respiratória Aguda Grave
/
Glicoproteína da Espícula de Coronavírus
/
Betacoronavirus
/
Epitopos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Science
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Estados Unidos