Structures and distributions of SARS-CoV-2 spike proteins on intact virions.

ABSTRACT: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude¹. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells^2-6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes^2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy^2,7,9-12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron

SUBMITTER: Ke Z 

PROVIDER: S-EPMC7116492 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature