Author: Turoňová, Beata; Sikora, Mateusz; Schürmann, Christoph; Hagen, Wim J. H.; Welsch, Sonja; Blanc, Florian E. C.; von Bülow, Sören; Gecht, Michael; Bagola, Katrin; Hörner, Cindy; van Zandbergen, Ger; Landry, Jonathan; de Azevedo, Nayara Trevisan Doimo; Mosalaganti, Shyamal; Schwarz, Andre; Covino, Roberto; Mühlebach, Michael D.; Hummer, Gerhard; Krijnse Locker, Jacomine; Beck, Martin
Title: In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges Cord-id: 4yi9iup2 Document date: 2020_10_9
ID: 4yi9iup2
Snippet: 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
Document: 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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