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

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.

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 Creators:
Turoňová, Beata1, 2, Author           
Sikora, Mateusz3, Author           
Schürmann, Christoph4, Author
Hagen, Wim J. H.1, Author
Welsch, Sonja5, Author           
Blanc, Florian E. C.3, Author           
von Bülow, Sören3, Author           
Gecht, Michael3, Author           
Bagola, Katrin6, Author
Hörner, Cindy4, 7, Author
van Zandbergen, Ger6, 8, 9, Author
Landry, Jonathan10, Author
de Azevedo, Nayara Trevisan Doimo10, Author
Mosalaganti, Shyamal1, Author           
Schwarz, Andre2, Author
Covino, Roberto3, 11, Author           
Mühlebach, Michael D.4, 7, Author
Hummer, Gerhard3, 12, Author                 
Krijnse Locker, Jacomine13, Author
Beck, Martin1, 2, Author                 
Affiliations:
1Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society, ou_3040395              
2European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Heidelberg, Germany, ou_persistent22              
3Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
4Division of Veterinary Medicine, Paul Ehrlich Institute, Langen, Germany, ou_persistent22              
5Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              
6Division of Immunology, Paul Ehrlich Institute, Langen, Germany, ou_persistent22              
7German Center for Infection Research, Gießen-Marburg-Langen, Germany, ou_persistent22              
8Institute for Immunology, University Medical Center, Johannes Gutenberg University Mainz, Mainz, Germany, ou_persistent22              
9Research Center for Immunotherapy (FZI), University Medical Center, Johannes Gutenberg-University Mainz, Mainz, Germany, ou_persistent22              
10European Molecular Biology Laboratory (EMBL), Genomics Core Facility, Heidelberg, Germany, ou_persistent22              
11Frankfurt Institute for Advanced Studies, Frankfurt am Main, Germany, ou_persistent22              
12Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
13Electron Microscopy of Pathogens Unit, Paul Ehrlich Institute, Langen, Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2020-06-262020-08-132020-08-182020-10-09
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.abd5223
BibTex Citekey: turonova_situ_2020
 Degree: -

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Title: Science
  Other : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 370 (6513) Sequence Number: - Start / End Page: 203 - 208 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1