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  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., 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.

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Genre: Journal Article

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 Creators:
Ke, Z. L., Author
Oton, J. Q., Author
Qu, K., Author
Cortese, M., Author
Zila, V., Author
McKeane, L., Author
Nakane, T., Author
Zivanov, J., Author
Neufeldt, C. J., Author
Cerikan, B., Author
Lu, J. M., Author
Peukes, J., Author
Xiong, X. L., Author
Krausslich, H. G., Author
Scheres, S. H. W., Author
Bartenschlager, R., Author
Briggs, John A. G.1, Author              
Affiliations:
1MRC Laboratory of Molecular Biology, External Organizations, ou_3346673              

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Free keywords: cryo-em cryoelectron tomography supramolecular architecture coronavirus virus visualization resolution Science & Technology - Other Topics
 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.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000585787300001
DOI: 10.1038/s41586-020-2665-2
ISSN: 0028-0836
 Degree: -

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Title: Nature
  Alternative Title : Nature
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 588 (7838) Sequence Number: - Start / End Page: 498 - 502 Identifier: -