Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein

作者：Linhua Tai, Guoliang Zhu, Minnan Yang, Lei Cao, Xiaorui Xing, Guoliang Yin, Chun Chan, Cheng‐Feng Qin, Zihe Rao, Xiangxi Wang, Fei Sun, Yun Zhu · 发表于：Proceedings of the National Academy of Sciences · 年份：2021 · DOI：10.1073/pnas.2112703118 · 被引用次数：61 · 研究领域：SARS-CoV-2 and COVID-19 Research、Bacteriophages and microbial interactions、Lipid Membrane Structure and Behavior

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.