| Title: |
In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges. |
| Authors: |
Turonˇová, Beata; Sikora, Mateusz; Schürmann, Christoph; Hagen, Wim J. H.; Welsch, Sonja; Blanc, Florian E. C.; Bülow, Sören von; 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; Locker, Jacomine Krijnse; Beck, Martin |
| Source: |
Science (pre-March 2025); 10/9/2020, Vol. 370 Issue 6513, p203-208, 6p, 1 Color Photograph, 4 Diagrams |
| Subject Terms: |
SARS disease; COVID-19 pandemic; Immunoglobulins; Molecular dynamics; Vaccines |
| Abstract: |
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. [ABSTRACT FROM AUTHOR] |
| : |
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| Database: |
Complementary Index |