e2022586118.full (1).pdf (952.19 kB)
Download file

The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2.

Download (952.19 kB)
journal contribution
posted on 17.02.2021, 09:52 by Donald J Benton, Antoni G Wrobel, Chloë Roustan, Annabel Borg, Pengqi Xu, Stephen R Martin, Peter B Rosenthal, John J Skehel, Steven J Gamblin
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.

Funding

Crick (Grant ID: 10015, Grant title: STP Structural Biology) Crick (Grant ID: 10143, Grant title: Rosenthal FC001143) Crick (Grant ID: 10078, Grant title: Gamblin FC001078)

History