E-resources
PDF-
Benton, Donald J; Wrobel, Antoni G; Roustan, Chloë; Borg, Annabel; Xu, Pengqi; Martin, Stephen R; Rosenthal, Peter B; Skehel, John J; Gamblin, Steven J
Proceedings of the National Academy of Sciences - PNAS, 03/2021, Volume: 118, Issue: 9Journal Article
The majority of currently circulating severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) viruses have mutant spike glycoproteins that contain the D614G substitution. Several studies have suggested that spikes with this substitution are associated with higher virus infectivity. We use cryo-electron microscopy to compare G614 and D614 spikes and show that the G614 mutant spike adopts a range of more open conformations that may facilitate binding to the SARS-CoV-2 receptor, ACE2, and the subsequent structural rearrangements required for viral membrane fusion.
