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-Structure paper
タイトル | Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 118, Issue 48, Year 2021 |
掲載日 | 2021年11月30日 |
著者 | 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 要旨 | 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. |
リンク | Proc Natl Acad Sci U S A / PubMed:34782481 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 10.9 Å |
構造データ | EMDB-31037, PDB-7e9t: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRUS / SARS-CoV-2 / in situ / post-fusion / spike / cryo-STA |