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  A thermostable, closed SARS-CoV-2 spike protein trimer

Xiong, X. L., Qu, K., Ciazynska, K. A., Hosmillo, M., Carter, A. P., Ebrahimi, S., et al. (2020). A thermostable, closed SARS-CoV-2 spike protein trimer. Nature Structural & Molecular Biology, 27(10), 934-941. doi:10.1038/s41594-020-0478-5.

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Xiong, X. L., Author
Qu, K., Author
Ciazynska, K. A., Author
Hosmillo, M., Author
Carter, A. P., Author
Ebrahimi, S., Author
Ke, Z. L., Author
Scheres, S. H. W., Author
Bergamaschi, L., Author
Grice, G. L., Author
Zhang, Y., Author
Nathan, J. A., Author
Baker, S., Author
James, L. C., Author
Baxendale, H. E., Author
Goodfellow, I., Author
Doffinger, R., Author
Briggs, John A. G.1, Author              
Bradley, J., Author
Lyons, P. A., Author
Smith, K. G. C., AuthorToshner, M., AuthorElmer, A., AuthorRibeiro, C., AuthorKourampa, J., AuthorJose, S., AuthorKennet, J., AuthorRowlands, J., AuthorMeadows, A., AuthorO'Brien, C., AuthorRastall, R., AuthorCrucusio, C., AuthorHewitt, S., AuthorPrice, J., AuthorCalder, J., AuthorLaura, C., AuthorBucke, A., AuthorTordesillas, H., AuthorHarris, J., AuthorRuffolo, V., AuthorDomingo, J., AuthorGraves, B., AuthorButcher, H., AuthorCaputo, D., AuthorLe Gresley, E., AuthorDunmore, B. J., AuthorMartin, J., AuthorLegchenko, E., AuthorTreacy, C., AuthorHuang, C., AuthorWood, J., AuthorSutcliffe, R., AuthorHodgson, J., AuthorShih, J., AuthorGraf, S., AuthorTong, Z., AuthorMescia, F., AuthorTilly, T., AuthorO'Donnell, C., AuthorHunter, K., AuthorPointon, L., AuthorPond, N., AuthorWylot, M., AuthorJones, E., AuthorFawke, S., AuthorBullman, B., AuthorBergamaschi, L., AuthorTurner, L., AuthorJarvis, I., AuthorOmarjee, O., AuthorDe Sa, A., AuthorMarsden, J., AuthorBetancourt, A., AuthorPerera, M., AuthorEpping, M., AuthorRichoz, N., AuthorBower, G., AuthorSharma, R., AuthorNice, F., AuthorHuhn, O., AuthorStark, H., AuthorWalker, N., AuthorStirrups, K., AuthorOvington, N., AuthorDewhust, E., AuthorLi, E., AuthorPapadia, S., AuthorC, Citiid-Nihr Covid- BioResource, Author more..
Affiliations:
1MRC Laboratory of Molecular Biology, External Organizations, ou_3346673              

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Free keywords: beam-induced motion cryo-em coronavirus vaccine Biochemistry & Molecular Biology Biophysics Cell Biology
 Abstract: The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. It exhibits substantial conformational flexibility. It transitions from closed to open conformations to expose its receptor-binding site and, subsequently, from prefusion to postfusion conformations to mediate fusion of viral and cellular membranes. S-protein derivatives are components of vaccine candidates and diagnostic assays, as well as tools for research into the biology and immunology of SARS-CoV-2. Here we have designed mutations in S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in the closed, prefusion state. Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer. We demonstrate that the designed, thermostable, closed S trimer can be used in serological assays. This protein has potential applications as a reagent for serology, virology and as an immunogen. The SARS-CoV-2 spike glycoprotein is flexible, and its receptor-binding domain (RBD) fluctuates between open and closed conformations. Disulfide bonds are engineered into the spike ectodomain to lock the RBD in the closed state, leading to a construct with high thermostability.

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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:000555383400001
DOI: 10.1038/s41594-020-0478-5
ISSN: 1545-9993
 Degree: -

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Title: Nature Structural & Molecular Biology
  Alternative Title : Nat. Struct. Mol. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 27 (10) Sequence Number: - Start / End Page: 934 - 941 Identifier: -