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Journal Article

In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

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Turoňová,  Beata
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;
European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Heidelberg, Germany;

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Sikora,  Mateusz       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

Hagen,  Wim J. H.
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Welsch,  Sonja       
Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society;

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Blanc,  Florian E. C.
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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von Bülow,  Sören       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Gecht,  Michael       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Mosalaganti,  Shyamal
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Covino,  Roberto
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Frankfurt Institute for Advanced Studies, Frankfurt am Main, Germany;

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Hummer,  Gerhard       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany;

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Beck,  Martin       
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;
European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Heidelberg, Germany;

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Citation

Turoňová, B., Sikora, M., Schürmann, C., Hagen, W. J. H., Welsch, S., Blanc, F. E. C., et al. (2020). In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges. Science, 370(6513), 203-208. doi:10.1126/science.abd5223.


Cite as: https://hdl.handle.net/21.11116/0000-0006-E15B-6
Abstract
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. Here, we combine cryo electron tomography, subtomogram averaging and molecular dynamics simulations to structurally analyze S in situ. Compared to recombinant S, the viral S was more heavily glycosylated and occurred mostly in the closed pre-fusion conformation. We show that the stalk domain of S contains three hinges, giving the head 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.