期刊
NATURE
卷 588, 期 7838, 页码 498-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41586-020-2665-2
关键词
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资金
- MRC-LMB
- Infectious Diseases Imaging Platform (IDIP) at the Center for Integrative Infectious Disease Research Heidelberg
- European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme [ERC-CoG-648432]
- Medical Research Council as part of UK Research and Innovation [MC_UP_A025_1013, MC_UP_1201/16]
- Deutsche Forschungsgemeinschaft [240245660-SFB 1129]
- Japan Society for the Promotion of Science
- MRC [MC_UP_A025_1013, MC_UP_1201/16] Funding Source: UKRI
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude(1). Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells(2-6). S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes(2,7,8). The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy(2,7,9-12), but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. Cryo-electron microscopy and tomography studies reveal the structures, conformations and distributions of spike protein trimers on intact severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions and provide a basis for understanding the interactions of the spike protein with neutralizing antibodies.
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