Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 118, Issue 9, Pages -Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2022586118
Keywords
SARS-CoV-2; Coronavirus; spike; cryo-EM; D614G
Categories
Funding
- Francis Crick Institute
- Cancer Research UK [FC001078, FC001143]
- UK Medical Research Council [FC001078, FC001143]
- Wellcome Trust [FC001078, FC001143]
- 100 Top Talents Program of Sun Yat-sen University
- Sanming Project of Medicine in Shenzhen [SZSM201911003]
- Shenzhen Science and Technology Innovation Committee [JCY.120190809151611269]
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Studies indicate that the G614 mutant spike adopts more open conformations, which may facilitate binding to the SARS-CoV-2 receptor ACE2 and the subsequent structural rearrangements required for viral membrane fusion.
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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