Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion.

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 glycoprotein to the postfusion conformation using limited proteolysis, mass spectromet

SUBMITTER: Walls AC 

PROVIDER: S-EPMC5651768 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature