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 protrude 1 . Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells 2 – 6 . S exhibi...

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Vydáno v:Nature (London) Ročník 588; číslo 7838; s. 498 - 502
Hlavní autoři: Ke, Zunlong, Oton, Joaquin, Qu, Kun, Cortese, Mirko, Zila, Vojtech, McKeane, Lesley, Nakane, Takanori, Zivanov, Jasenko, Neufeldt, Christopher J., Cerikan, Berati, Lu, John M., Peukes, Julia, Xiong, Xiaoli, Kräusslich, Hans-Georg, Scheres, Sjors H. W., Bartenschlager, Ralf, Briggs, John A. G.
Médium: Journal Article
Jazyk:angličtina
Vydáno: London Nature Publishing Group UK 17.12.2020
Nature Publishing Group
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ISSN:0028-0836, 1476-4687, 1476-4687
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Shrnutí:Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude 1 . Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells 2 – 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 membranes 2 , 7 , 8 . The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy 2 , 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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ISSN:0028-0836
1476-4687
1476-4687
DOI:10.1038/s41586-020-2665-2