Structures and distributions of SARS-CoV-2 spike proteins on intact virions.
Nature
; 588(7838): 498-502, 2020 12.
Article
in English
| MEDLINE | ID: covidwho-1343462
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.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Virion
/
Cryoelectron Microscopy
/
Spike Glycoprotein, Coronavirus
/
SARS-CoV-2
Topics:
Vaccines
Limits:
Humans
Language:
English
Journal:
Nature
Year:
2020
Document Type:
Article
Affiliation country:
S41586-020-2665-2
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