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

被引：113

作者：

Benton, Donald J. ^{[1
]}

Wrobel, Antoni G. ^{[1
]}

Roustan, Chloe ^{[2
]}

Borg, Annabel ^{[2
]}

Xu, Pengqi ^{[1
,3
]}

Martin, Stephen R. ^{[1
]}

Rosenthal, Peter B. ^{[4
]}

Skehel, John J. ^{[1
]}

Gamblin, Steven J. ^{[1
]}

机构：

[1] Francis Crick Inst, Struct Biol Dis Proc Lab, London NW1 1AT, England

[2] Francis Crick Inst, Struct Biol Sci Technol Platform, London NW1 1AT, England

[3] Sun Yat Sen Univ, Affiliated Hosp 7, Precis Med Ctr, Shenzhen 518107, Guangdong, Peoples R China

[4] Francis Crick Inst, Struct Biol Cells & Viruses Lab, London NW1 1AT, England

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2021年 / 118卷 / 09期

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

SARS-CoV-2; Coronavirus; spike; cryo-EM; D614G; CRYO-EM STRUCTURE; BEAM-INDUCED MOTION; BAYESIAN-APPROACH;

D O I：

10.1073/pnas.2022586118

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页数：4

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