TY  - INPR
A1  - Turoňová, Beata
A1  - Sikora, Mateusz
A1  - Schürmann, Christoph
A1  - Hagen, Wim
A1  - Welsch, Sonja
A1  - Blanc, Florian E. C.
A1  - Bülow, Sören von
A1  - Gecht, Michael
A1  - Bagola, Katrin
A1  - Hörner, Cindy
A1  - Zandbergen, Ger van
A1  - Mosalaganti, Shyamal Narayan
A1  - Schwarz, Andre
A1  - Covino, Roberto
A1  - Mühlebach, Michael D.
A1  - Hummer, Gerhard
A1  - Krijnse-Locker, Jacomine
A1  - Beck, Martin
T1  - In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges
T2  - bioRxiv
N2  - 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. We combine cryo electron tomography, subtomogram averaging and molecular dynamics simulations to structurally analyze S in situ. Compared to recombinant S, the viral S is more heavily glycosylated and occurs predominantly in a closed pre-fusion conformation. We show that the stalk domain of S contains three hinges that give the globular domain 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. The large scale tomography data set of SARS-CoV-2 used for this study is therefore sufficient to resolve structural features to below 5 Ångstrom, and is publicly available at EMPIAR-10453.
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/72774
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-727745
IS  - 2020.06.26.173476
ER  -