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

Ke, Z. L.; Oton, J. Q.; Qu, K.; Cortese, M.; Zila, V.; McKeane, L.; Nakane, T.; Zivanov, J.; Neufeldt, C. J.; Cerikan, B.; Lu, J. M.; Peukes, J.; Xiong, X. L.; Krausslich, H. G.; Scheres, S. H. W.; Bartenschlager, R.; Briggs, John A. G.

doi:10.1038/s41586-020-2665-2

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

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Ke, Z. L., Oton, J. Q., Qu, K., Cortese, M., Zila, V., McKeane, L., et al. (2020). Structures and distributions of SARS-CoV-2 spike proteins on intact virions. Nature, 588(7838), 498-502. doi:10.1038/s41586-020-2665-2.

Cite as: https://hdl.handle.net/21.11116/0000-0009-7227-B

Abstract

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.