Structures and distributions of SARS-CoV-2 spike proteins on intact virions.
Nature
; 588(7838): 498-502, 2020 12.
Article
en En
| MEDLINE
| ID: mdl-32805734
ABSTRACT
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2-6. S exhibits extensive conformational flexibility it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9-12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Virión
/
Microscopía por Crioelectrón
/
Glicoproteína de la Espiga del Coronavirus
/
SARS-CoV-2
Límite:
Humans
Idioma:
En
Año:
2020
Tipo del documento:
Article