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

Author:

Turoňová Beata12ORCID,Sikora Mateusz3ORCID,Schürmann Christoph4ORCID,Hagen Wim J. H.1ORCID,Welsch Sonja5ORCID,Blanc Florian E. C.3ORCID,von Bülow Sören3ORCID,Gecht Michael3ORCID,Bagola Katrin6ORCID,Hörner Cindy47ORCID,van Zandbergen Ger689ORCID,Landry Jonathan10ORCID,de Azevedo Nayara Trevisan Doimo10ORCID,Mosalaganti Shyamal12ORCID,Schwarz Andre1ORCID,Covino Roberto311ORCID,Mühlebach Michael D.47ORCID,Hummer Gerhard312ORCID,Krijnse Locker Jacomine13ORCID,Beck Martin12ORCID

Affiliation:

1. Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstr. 1, 69117 Heidelberg, Germany.

2. Department of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.

3. Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.

4. Division of Veterinary Medicine, Paul Ehrlich Institute, Paul Ehrlich Strasse 51-59, 63225 Langen, Germany.

5. Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.

6. Division of Immunology, Paul Ehrlich Institute, Paul Ehrlich Strasse 51-59, 63225 Langen, Germany.

7. German Center for Infection Research, Gießen-Marburg-Langen, Germany.

8. Institute for Immunology, University Medical Center, Johannes Gutenberg University Mainz, Mainz, Germany.

9. Research Center for Immunotherapy (FZI), University Medical Center, Johannes Gutenberg-University Mainz, Mainz, Germany.

10. Genomics Core Facility, EMBL, Meyerhofstr. 1, 69117 Heidelberg, Germany.

11. Frankfurt Institute for Advanced Studies, Ruth-Moufang-Str. 1, 60438 Frankfurt am Main, Germany.

12. Institute of Biophysics, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany.

13. Electron Microscopy of Pathogens Unit, Paul Ehrlich Institute, Paul Ehrlich Strasse 51-59, 63225 Langen, Germany.

Abstract

Flexible spikes The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein enables viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor and is a major target for neutralizing antibodies. About 20 to 40 spikes decorate the surface of virions. Turoňová et al. now show that the spike is flexibly connected to the viral surface by three hinges that are well protected by glycosylation sites. The flexibility imparted by these hinges may explain how multiple spikes act in concert to engage onto the flat surface of a host cell. Science , this issue p. 203

Funder

Human Frontier Science Program

Max-Planck-Gesellschaft

Austrian Science Fund FWF

Loewe Centre DRUID

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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