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

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-...

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Detalles Bibliográficos
Autores principales: Benton, Donald J., Wrobel, Antoni G., Roustan, Chloë, Borg, Annabel, Xu, Pengqi, Martin, Stephen R., Rosenthal, Peter B., Skehel, John J., Gamblin, Steven J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2021
Materias:
Biological Sciences
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936381/
https://www.ncbi.nlm.nih.gov/pubmed/33579792
http://dx.doi.org/10.1073/pnas.2022586118
Descripción
Sumario: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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