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

By Zunlong Ke, Joaquin Oton, Kun Qu, Mirko Cortese, Vojtech Zila, Lesley McKeane, Takanori Nakane, Jasenko Zivanov, Christopher J. Neufeldt, John M Lu, Julia Peukes, Xiaoli Xiong, Hans-Georg Kräusslich, Sjors Scheres, Ralf Bartenschlager, John A G Briggs

Posted 27 Jun 2020
bioRxiv DOI: 10.1101/2020.06.27.174979 (published DOI: 10.1038/s41586-020-2665-2)

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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