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

Beata Turoňová | Zendy; Mateusz Sikora | Zendy; Christoph Schürmann | Zendy; Wim J. H. Hagen | Zendy; Sonja Welsch | Zendy; Florian E.C. Blanc | Zendy; Sören von Bülow | Zendy; Michael Gecht | Zendy; Katrin Bagola | Zendy; Cindy Hörner | Zendy; Ger van Zandbergen | Zendy; Jonathan J. M. Landry | Zendy; Nayara Azevedo | Zendy; Shyamal Mosalaganti | Zendy; Andre Schwarz | Zendy; Roberto Covino | Zendy; Michael D. Mühlebach | Zendy; Gerhard Hummer | Zendy; Jacomine Krijnse Locker | Zendy; Martin Beck | Zendy

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

Author(s) -

Beata Turoňová,

Mateusz Sikora,

Christoph Schürmann,

Wim J. H. Hagen,

Sonja Welsch,

Florian E.C. Blanc,

Sören von Bülow,

Michael Gecht,

Katrin Bagola,

Cindy Hörner,

Ger van Zandbergen,

Jonathan J. M. Landry,

Nayara Azevedo,

Shyamal Mosalaganti,

Andre Schwarz,

Roberto Covino,

Michael D. Mühlebach,

Gerhard Hummer,

Jacomine Krijnse Locker,

Martin Beck

Publication year - 2020

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.abd5223

Subject(s) - spike (software development) , covid-19 , hinge , flexibility (engineering) , computational biology , virology , biology , computer science , engineering , structural engineering , medicine , mathematics , statistics , software engineering , disease , pathology , outbreak , infectious disease (medical specialty)

The spike protein (S) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is required for cell entry and is the primary focus for vaccine development. In this study, we combined cryo-electron tomography, subtomogram averaging, and molecular dynamics simulations to structurally analyze S in situ. Compared with the recombinant S, the viral S was more heavily glycosylated and occurred mostly in the closed prefusion 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 potentially to the development of safe vaccines.

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