Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion

University of Washington · Centre National de la Recherche Scientifique · +3 more institutions

PubMed
Indexed incrossrefpubmed

Abstract

The tremendous pandemic potential of coronaviruses was demonstrated twice in the past few decades by two global outbreaks of deadly pneumonia. The coronavirus spike (S) glycoprotein initiates infection by promoting fusion of the viral and cellular membranes through conformational changes that remain largely uncharacterized. Here we report the cryoEM structure of a coronavirus S glycoprotein in the postfusion state, showing large-scale secondary, tertiary, and quaternary rearrangements compared with the prefusion trimer and rationalizing the free-energy landscape of this conformational machine. We also biochemically characterized the molecular events associated with refolding of the metastable prefusion S…

Citation impact

625
total citations
FWCI
39.35
Percentile
100%
References
64
Citations per year

Authors

7

Topics & keywords

Keywords
  • Lipid bilayer fusion
  • Coronavirus
  • Glycoprotein
  • Biology
  • Viral entry
  • Virology
  • Protein subunit
  • Protein structure
UN Sustainable Development Goals
  • Good health and well-being
No related works found for this paper.

Funding