EMD-11497
Cryo-EM structure of SARS-CoV-2 Spike Proteins on intact virions: 3 Closed RBDs
EMD-11497
Single-particle3.5 Å
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Map released: 05/08/2020
Last modified: 23/10/2024
Sample Organism:
Severe acute respiratory syndrome coronavirus 2
Sample: Severe acute respiratory syndrome coronavirus 2
Fitted models: 6zwv (Avg. Q-score: 0.402)
Raw data: EMPIAR-10492
Deposition Authors: Ke Z
,
Qu K
,
Nakane T
,
Xiong X
,
Cortese M
,
Zila V
,
Scheres SHW
,
Briggs JAG
Sample: Severe acute respiratory syndrome coronavirus 2
Fitted models: 6zwv (Avg. Q-score: 0.402)
Raw data: EMPIAR-10492
Deposition Authors: Ke Z
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Structures and distributions of SARS-CoV-2 spike proteins on intact virions.
Ke Z
,
Oton J
,
Qu K
,
Cortese M
,
Zila V
,
McKeane L,
Nakane T
,
Zivanov J,
Neufeldt CJ
,
Cerikan B,
Lu JM
,
Peukes J
,
Xiong X
,
Krausslich HG,
Scheres SHW
,
Bartenschlager R
,
Briggs JAG
(2020) Nature , 588 , 498 - 502
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(2020) Nature , 588 , 498 - 502
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.
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.