Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions

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Zunlong Ke

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Microbiology

Joaquin Oton

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Microbiology

Kun Qu

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Microbiology

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Mirko Cortese

Vojtech Zila

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Microbiology

Lesley McKeane

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Microbiology

Takanori Nakane

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Microbiology

Jasenko Zivanov

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Microbiology

John M Lu

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Microbiology

Julia Peukes

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Microbiology

Xiaoli Xiong

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Microbiology

Hans-Georg Kraeusslich

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Microbiology

Sjors Scheres

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Microbiology

John A G Briggs

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Microbiology

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Published in Nature, 2020-08-17

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells. S exhibits extensive conformational flexibility: it modulates the exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy. The structure and distribution of S on the virion surface, however, has not been characterised. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distributions of S trimers in situ on the virion surface. These results provide a basis for understanding the conformations of S present on the virion, and for studying their interactions with neutralizing antibodies. ### Competing Interest Statement The authors have declared no competing interest.

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