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

Proc Natl Acad Sci U S A. 2021 Mar 2;118(9):e2022586118. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • COVID-19 / virology*
  • Cryoelectron Microscopy
  • Humans
  • Protein Conformation
  • SARS-CoV-2 / chemistry*
  • SARS-CoV-2 / genetics
  • Spike Glycoprotein, Coronavirus / chemistry*
  • Spike Glycoprotein, Coronavirus / genetics
  • Virus Internalization

Substances

  • Spike Glycoprotein, Coronavirus
  • spike protein, SARS-CoV-2