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TitleDistinct conformational states of SARS-CoV-2 spike protein.
Journal, issue, pagesScience (New York, N. Y. ), Vol. 369, Issue 6511, Page 1586-1592, Year 2020
Publish dateSep 25, 2020
AuthorsYongfei Cai / Jun Zhang / Tianshu Xiao / Hanqin Peng / Sarah M Sterling / Richard M Walsh / Shaun Rawson / Sophia Rits-Volloch / Bing Chen /
PubMed AbstractIntervention 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 ...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.
External linksScience (New York, N. Y. ) / PubMed:32694201 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3 Å
Structure data

EMDB-22292, PDB-6xr8:
Distinct conformational states of SARS-CoV-2 spike protein
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-22293, PDB-6xra:
Distinct conformational states of SARS-CoV-2 spike protein
Method: EM (single particle) / Resolution: 3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-MAN:
alpha-D-mannopyranose / Mannose

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN

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