| Literature DB >> 33579792 |
Donald J Benton1, Antoni G Wrobel1, Chloë Roustan2, Annabel Borg2, Pengqi Xu3,4, Stephen R Martin4, Peter B Rosenthal5, John J Skehel1, Steven J Gamblin1.
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.Entities:
Keywords: Coronavirus; D614G; SARS-CoV-2; cryo-EM; spike
Mesh:
Substances:
Year: 2021 PMID: 33579792 PMCID: PMC7936381 DOI: 10.1073/pnas.2022586118
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 12.779