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Structures and distributions of SARS-CoV-2 spike proteins on intact virions

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 ext...

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Main Authors: Ke, Zunlong (Author) , Oton, Joaquin (Author) , Qu, Kun (Author) , Cortese, Mirko (Author) , Zila, Vojtech (Author) , McKeane, Lesley (Author) , Nakane, Takanori (Author) , Zivanov, Jasenko (Author) , Neufeldt, Christopher (Author) , Cerikan, Berati (Author) , Lu, John M. (Author) , Peukes, Julia (Author) , Xiong, Xiaoli (Author) , Kräusslich, Hans-Georg (Author) , Scheres, Sjors H. W. (Author) , Bartenschlager, Ralf (Author) , Briggs, John A. G. (Author)
Format: Article (Journal)
Language:English
Published: 17 December 2020
In: Nature
Year: 2020, Volume: 588, Issue: 7838, Pages: 498-502, [1-16]
ISSN:1476-4687
DOI:10.1038/s41586-020-2665-2
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/s41586-020-2665-2
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/s41586-020-2665-2
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Author Notes:Zunlong Ke, Joaquin Oton, Kun Qu, Mirko Cortese, Vojtech Zila, Lesley McKeane, Takanori Nakane, Jasenko Zivanov, Christopher J. Neufeldt, Berati Cerikan, John M. Lu, Julia Peukes, Xiaoli Xiong, Hans-Georg Kräusslich, Sjors H. W. Scheres, Ralf Bartenschlager & John A.G. Briggs
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Summary: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.
Item Description:Gesehen am 16.04.2026
Physical Description:Online Resource
ISSN:1476-4687
DOI:10.1038/s41586-020-2665-2

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