期刊
SCIENCE
卷 370, 期 6513, 页码 203-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abd5223
关键词
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资金
- Leibniz Supercomputing Centre
- Human Frontier Science Program [RGP0026/2017]
- German Ministry of Health
- German Center for Infection Research
- Loewe Center DRUID from the Justus Liebig University Giessen
- Austrian Science Fund FWF (Schrodinger Fellowship) [J4332-B28]
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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