生物物理学
低温电子显微
化学
脂质双层融合
冠状病毒
脂质双层
蛋白质结构
低温电子层析成像
严重急性呼吸综合征冠状病毒2型(SARS-CoV-2)
结晶学
细胞生物学
生物
2019年冠状病毒病(COVID-19)
生物化学
膜
物理
医学
病理
断层摄影术
传染病(医学专业)
光学
疾病
作者
Zunlong Ke,Joaquı́n Otón,Kun Qu,Mirko Cortese,Vojtěch Žíla,Lesley McKeane,Takanori Nakane,Jasenko Zivanov,Christopher J. Neufeldt,Berati Cerikan,John M. Lu,Julia Peukes,Xiaoli Xiong,Hans Georg Kräusslich,S.H.W. Scheres,Ralf Bartenschlager,John Briggs
出处
期刊:Nature
[Springer Nature]
日期:2020-08-17
卷期号:588 (7838): 498-502
被引量:897
标识
DOI:10.1038/s41586-020-2665-2
摘要
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2–6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9–12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. Cryo-electron microscopy and tomography studies reveal the structures, conformations and distributions of spike protein trimers on intact severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions and provide a basis for understanding the interactions of the spike protein with neutralizing antibodies.
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