Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein
Peng Zhang, Huaxia Luo, Yanyan Li, You Wang, Jiajia Wang, Yu Zheng, Yiwei Niu, Yirong Shi, Honghong Zhou, Tingrui Song, Quan Kang, Tao Xu, Shunmin He
Abstract
The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in β-propiolactone–inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.
附件下载：
Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein, PNAS, 25 Oct 2021
PNAS, 25 October, 2021, DOI：https://doi.org/10.1073/pnas.2112703118
Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein
Peng Zhang, Huaxia Luo, Yanyan Li, You Wang, Jiajia Wang, Yu Zheng, Yiwei Niu, Yirong Shi, Honghong Zhou, Tingrui Song, Quan Kang, Tao Xu, Shunmin He
Abstract
The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in β-propiolactone–inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.
文章链接：https://www.pnas.org/content/118/48/e2112703118
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