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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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
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author Benton, Donald J.
Wrobel, Antoni G.
Roustan, Chloë
Borg, Annabel
Xu, Pengqi
Martin, Stephen R.
Rosenthal, Peter B.
Skehel, John J.
Gamblin, Steven J.
author_facet Benton, Donald J.
Wrobel, Antoni G.
Roustan, Chloë
Borg, Annabel
Xu, Pengqi
Martin, Stephen R.
Rosenthal, Peter B.
Skehel, John J.
Gamblin, Steven J.
author_sort Benton, Donald J.
collection PubMed
description 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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spelling pubmed-79363812021-03-11 The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2 Benton, Donald J. Wrobel, Antoni G. Roustan, Chloë Borg, Annabel Xu, Pengqi Martin, Stephen R. Rosenthal, Peter B. Skehel, John J. Gamblin, Steven J. Proc Natl Acad Sci U S A Biological Sciences 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. National Academy of Sciences 2021-03-02 2021-02-12 /pmc/articles/PMC7936381/ /pubmed/33579792 http://dx.doi.org/10.1073/pnas.2022586118 Text en Copyright © 2021 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by/4.0/This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Biological Sciences
Benton, Donald J.
Wrobel, Antoni G.
Roustan, Chloë
Borg, Annabel
Xu, Pengqi
Martin, Stephen R.
Rosenthal, Peter B.
Skehel, John J.
Gamblin, Steven J.
The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
title The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
title_full The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
title_fullStr The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
title_full_unstemmed The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
title_short The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2
title_sort effect of the d614g substitution on the structure of the spike glycoprotein of sars-cov-2
topic Biological Sciences
url 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
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