Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:118 |
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| Enthalten in: |
Proceedings of the National Academy of Sciences of the United States of America - 118(2021), 48 vom: 30. Nov. |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Tai, Linhua [VerfasserIn] |
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| Links: |
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| Themen: |
Cryo-electron tomography |
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| Anmerkungen: |
Date Completed 25.11.2021 Date Revised 14.12.2021 published: Print Citation Status MEDLINE |
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| doi: |
10.1073/pnas.2112703118 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM33320218X |
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| 245 | 1 | 0 | |a Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein |
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| 500 | |a Date Revised 14.12.2021 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a SARS-CoV-2 | |
| 650 | 4 | |a cryo-electron tomography | |
| 650 | 4 | |a postfusion state | |
| 650 | 4 | |a spike protein | |
| 650 | 4 | |a subtomogram analysis | |
| 650 | 7 | |a Spike Glycoprotein, Coronavirus |2 NLM | |
| 650 | 7 | |a spike protein, SARS-CoV-2 |2 NLM | |
| 700 | 1 | |a Zhu, Guoliang |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Minnan |e verfasserin |4 aut | |
| 700 | 1 | |a Cao, Lei |e verfasserin |4 aut | |
| 700 | 1 | |a Xing, Xiaorui |e verfasserin |4 aut | |
| 700 | 1 | |a Yin, Guoliang |e verfasserin |4 aut | |
| 700 | 1 | |a Chan, Chun |e verfasserin |4 aut | |
| 700 | 1 | |a Qin, Chengfeng |e verfasserin |4 aut | |
| 700 | 1 | |a Rao, Zihe |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Xiangxi |e verfasserin |4 aut | |
| 700 | 1 | |a Sun, Fei |e verfasserin |4 aut | |
| 700 | 1 | |a Zhu, Yun |e verfasserin |4 aut | |
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