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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.
  • Benton DJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London NW1 1AT, United Kingdom; Donald.Benton@crick.ac.uk John.Skehel@crick.ac.uk Antoni.Wrobel@crick.ac.uk Steve.Gamblin@crick.ac.uk.
  • Wrobel AG; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London NW1 1AT, United Kingdom; Donald.Benton@crick.ac.uk John.Skehel@crick.ac.uk Antoni.Wrobel@crick.ac.uk Steve.Gamblin@crick.ac.uk.
  • Roustan C; Structural Biology Science Technology Platform, Francis Crick Institute, London NW1 1AT, United Kingdom.
  • Borg A; Structural Biology Science Technology Platform, Francis Crick Institute, London NW1 1AT, United Kingdom.
  • Xu P; Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, 518107 Shenzhen, Guangdong, China.
  • Martin SR; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London NW1 1AT, United Kingdom.
  • Rosenthal PB; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London NW1 1AT, United Kingdom.
  • Skehel JJ; Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, London NW1 1AT, United Kingdom.
  • Gamblin SJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London NW1 1AT, United Kingdom; Donald.Benton@crick.ac.uk John.Skehel@crick.ac.uk Antoni.Wrobel@crick.ac.uk Steve.Gamblin@crick.ac.uk.
Proc Natl Acad Sci U S A ; 118(9)2021 03 02.
Article in English | MEDLINE | ID: covidwho-1080743
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Experimental Studies Limits: Humans Language: English Year: 2021 Document Type: Article

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Experimental Studies Limits: Humans Language: English Year: 2021 Document Type: Article