|Title||Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein.|
|Journal, issue, pages||Proc Natl Acad Sci U S A, Vol. 118, Issue 48, Year 2021|
|Publish date||Nov 30, 2021|
|Authors||Linhua Tai / Guoliang Zhu / Minnan Yang / Lei Cao / Xiaorui Xing / Guoliang Yin / Chun Chan / Chengfeng Qin / Zihe Rao / Xiangxi Wang / Fei Sun / Yun Zhu /|
|PubMed 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 ...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.|
|External links||Proc Natl Acad Sci U S A / PubMed:34782481|
|Methods||EM (subtomogram averaging)|
|Keywords||VIRUS / SARS-CoV-2 / in situ / post-fusion / spike / cryo-STA|
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