Distinct conformational states of SARS-CoV-2 spike protein.
Science
; 369(6511): 1586-1592, 2020 09 25.
Article
in English
| MEDLINE | ID: covidwho-2038226
ABSTRACT
Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Host-Pathogen Interactions
/
Spike Glycoprotein, Coronavirus
Topics:
Vaccines
Limits:
Humans
Language:
English
Journal:
Science
Year:
2020
Document Type:
Article
Affiliation country:
Science.abd4251
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