Distinct conformational states of SARS-CoV-2 spike protein-Reference-Cited by-同舟云学术

Distinct conformational states of SARS-CoV-2 spike protein

Published:2020-09-25 Issue:6511 Volume:369 Page:1586-1592
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Cai Yongfei¹²^ORCID,Zhang Jun¹²,Xiao Tianshu¹²^ORCID,Peng Hanqin¹^ORCID,Sterling Sarah M.³⁴^ORCID,Walsh Richard M.³⁴^ORCID,Rawson Shaun³⁴⁵^ORCID,Rits-Volloch Sophia¹,Chen Bing¹²^ORCID

Affiliation:

1. Division of Molecular Medicine, Boston Children’s Hospital, Boston, MA 02115, USA.

2. Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA.

3. The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, Boston, MA 02115, USA.

4. Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.

5. SBGrid Consortium, Harvard Medical School, Boston, MA 02115, USA.

Abstract

A dynamic viral spike Efforts to protect human cells against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have focused on the trimeric spike (S) protein. Several structures have shown a stabilized ectodomain of the spike in its prefusion conformation. Cai et al. now provide insight into the structural changes in the S protein that result in the fusion of the viral and host cell membranes. They purified full-length S protein and determined cryo–electron microscopy structures of both the prefusion and postfusion conformations. These structures add to our understanding of S protein function and could inform vaccine design. Science , this issue p. 1586

Funder

National Institutes of Health

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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