In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges
Wim J. H. Hagen,
Florian E. C. Blanc,
Sören von Bülow,
Ger van Zandbergen,
Michael D. Mühlebach,
Jacomine Krijnse Locker,
Posted 26 Jun 2020
bioRxiv DOI: 10.1101/2020.06.26.173476 (published DOI: 10.1126/science.abd5223)
Posted 26 Jun 2020
The spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is required for cell entry and is the major focus for vaccine development. We combine cryo electron tomography, subtomogram averaging and molecular dynamics simulations to structurally analyze S in situ . Compared to recombinant S, the viral S is more heavily glycosylated and occurs predominantly in a closed pre-fusion conformation. We show that the stalk domain of S contains three hinges that give the globular domain unexpected orientational freedom. We propose that the hinges allow S to scan the host cell surface, shielded from antibodies by an extensive glycan coat. The structure of native S contributes to our understanding of SARS-CoV-2 infection and the development of safe vaccines. The large scale tomography data set of SARS-CoV-2 used for this study is therefore sufficient to resolve structural features to below 5 Ångstrom, and is publicly available at EMPIAR-10453. ### Competing Interest Statement The authors have declared no competing interest.
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