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| 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 / PubMed Central |
| Methods | EM (subtomogram averaging) |
| Resolution | 10.9 Å |
| Structure data | EMDB-31037, PDB-7e9t: |
| Chemicals |  ChemComp-NAG: |
| Source |
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 Keywords | VIRUS / SARS-CoV-2 / in situ / post-fusion / spike / cryo-STA |
severe acute respiratory syndrome coronavirus 2
