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

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 and John A. G. Briggs ()
Additional contact information
Zunlong Ke: Medical Research Council Laboratory of Molecular Biology
Joaquin Oton: Medical Research Council Laboratory of Molecular Biology
Kun Qu: Medical Research Council Laboratory of Molecular Biology
Mirko Cortese: Molecular Virology, Heidelberg University
Vojtech Zila: Virology, Heidelberg University
Lesley McKeane: Medical Research Council Laboratory of Molecular Biology
Takanori Nakane: Medical Research Council Laboratory of Molecular Biology
Jasenko Zivanov: Medical Research Council Laboratory of Molecular Biology
Christopher J. Neufeldt: Molecular Virology, Heidelberg University
Berati Cerikan: Molecular Virology, Heidelberg University
John M. Lu: Medical Research Council Laboratory of Molecular Biology
Julia Peukes: Medical Research Council Laboratory of Molecular Biology
Xiaoli Xiong: Medical Research Council Laboratory of Molecular Biology
Hans-Georg Kräusslich: Virology, Heidelberg University
Sjors H. W. Scheres: Medical Research Council Laboratory of Molecular Biology
Ralf Bartenschlager: Molecular Virology, Heidelberg University
John A. G. Briggs: Medical Research Council Laboratory of Molecular Biology

Nature, 2020, vol. 588, issue 7838, 498-502

Abstract: Abstract 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.

Date: 2020
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DOI: 10.1038/s41586-020-2665-2

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