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

By Xiaoli Xiong, Kun Qu, Katarzyna A Ciazynska, Myra Hosmillo, Andrew Carter, Soraya Ebrahimi, Zunlong Ke, Sjors Scheres, Laura Bergamaschi, Guinevere L. Grice, Ying Zhang, The CITIID-NIHR COVID-19 BioResource Collaboration, James A Nathan, Stephen Baker, Leo C James, Helen E. Baxendale, Ian G. Goodfellow, Rainer Doffinger, John A G Briggs

Posted 17 Jun 2020
bioRxiv DOI: 10.1101/2020.06.15.152835 (published DOI: 10.1038/s41594-020-0478-5)

The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. S 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 which allow production of thermostable, crosslinked, S protein trimers that are trapped in the closed, pre-fusion, state. We have determined the structures of crosslinked and non-crosslinked proteins, identifying two distinct closed 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. ### Competing Interest Statement The authors have declared no competing interest.

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