TY  - JOUR
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  - Landry, Jonathan
A1  - Trevisan Doimo de Azevedo, Nayara
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  - Science
N2  - 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.
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/73421
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-734212
SN  - 0036-8075
VL  - 370
IS  - 6513
SP  - 203
EP  - 208
PB  - American Association for the Advancement of Science
CY  - Washington, DC [u.a.]
ER  -