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TitleIn situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges.
Journal, issue, pagesScience, Vol. 370, Issue 6513, Page 203-208, Year 2020
Publish dateOct 9, 2020
AuthorsBeata 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 Landry / Nayara Trevisan Doimo de Azevedo / Shyamal Mosalaganti / Andre Schwarz / Roberto Covino / Michael D Mühlebach / Gerhard Hummer / Jacomine Krijnse Locker / Martin Beck /
PubMed AbstractThe 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- ...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.
External linksScience / PubMed:32817270 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution4.9 - 7.9 Å
Structure data

EMDB-11222:
Structure of SARS-CoV-2 spike glycoprotein (S) trimer determined by sub-tomogram averaging
Method: EM (subtomogram averaging) / Resolution: 7.9 Å

EMDB-11223:
Structure of SARS-CoV-2 spike glycoprotein (S) monomer in a closed conformation determined by sub-tomogram averaging
Method: EM (subtomogram averaging) / Resolution: 4.9 Å

EMDB-11347:
Structure of SARS-CoV-2 spike glycoprotein (S) trimer with one receptor binding domain (RBD) in open-state determined by subtomogram averaging
Method: EM (subtomogram averaging) / Resolution: 5.4 Å

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