tetano
Editor, Senior Moderator
Proc Natl Acad Sci U S A
. 2021 Mar 2;118(9):e2022586118.
doi: 10.1073/pnas.2022586118.
The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
Donald J Benton[SUP] 1 [/SUP], Antoni G Wrobel[SUP] 1 [/SUP], Chlo? Roustan[SUP] 2 [/SUP], Annabel Borg[SUP] 2 [/SUP], Pengqi Xu[SUP] 3 4 [/SUP], Stephen R Martin[SUP] 4 [/SUP], Peter B Rosenthal[SUP] 5 [/SUP], John J Skehel[SUP] 1 [/SUP], Steven J Gamblin[SUP] 1 [/SUP]
Affiliations
Abstract
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.
Keywords: Coronavirus; D614G; SARS-CoV-2; cryo-EM; spike.
. 2021 Mar 2;118(9):e2022586118.
doi: 10.1073/pnas.2022586118.
The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
Donald J Benton[SUP] 1 [/SUP], Antoni G Wrobel[SUP] 1 [/SUP], Chlo? Roustan[SUP] 2 [/SUP], Annabel Borg[SUP] 2 [/SUP], Pengqi Xu[SUP] 3 4 [/SUP], Stephen R Martin[SUP] 4 [/SUP], Peter B Rosenthal[SUP] 5 [/SUP], John J Skehel[SUP] 1 [/SUP], Steven J Gamblin[SUP] 1 [/SUP]
Affiliations
- PMID: 33579792
- DOI: 10.1073/pnas.2022586118
Abstract
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.
Keywords: Coronavirus; D614G; SARS-CoV-2; cryo-EM; spike.