Author: Benton, Donald J.; Wrobel, Antoni G.; Roustan, Chloë; Borg, Annabel; Xu, Pengqi; Martin, Stephen R.; Rosenthal, Peter B.; Skehel, John J.; Gamblin, Steven J.
Title: The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2 Cord-id: a0vyh7wr Document date: 2021_3_2
ID: a0vyh7wr
Snippet: 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
Document: 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.
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