tetano
Editor, Senior Moderator
Proc Natl Acad Sci U S A
. 2021 Nov 30;118(48):e2112703118.
doi: 10.1073/pnas.2112703118.
Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein
Linhua Tai[SUP] 1 2 [/SUP], Guoliang Zhu[SUP] 1 2 [/SUP], Minnan Yang[SUP] 1 [/SUP], Lei Cao[SUP] 1 [/SUP], Xiaorui Xing[SUP] 1 [/SUP], Guoliang Yin[SUP] 1 2 [/SUP], Chun Chan[SUP] 3 [/SUP], Chengfeng Qin[SUP] 4 [/SUP], Zihe Rao[SUP] 1 [/SUP], Xiangxi Wang[SUP] 5 6 [/SUP], Fei Sun[SUP] 5 2 7 8 [/SUP], Yun Zhu[SUP] 5 [/SUP]
Affiliations
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 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.
Keywords: SARS-CoV-2; cryo-electron tomography; postfusion state; spike protein; subtomogram analysis.
. 2021 Nov 30;118(48):e2112703118.
doi: 10.1073/pnas.2112703118.
Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein
Linhua Tai[SUP] 1 2 [/SUP], Guoliang Zhu[SUP] 1 2 [/SUP], Minnan Yang[SUP] 1 [/SUP], Lei Cao[SUP] 1 [/SUP], Xiaorui Xing[SUP] 1 [/SUP], Guoliang Yin[SUP] 1 2 [/SUP], Chun Chan[SUP] 3 [/SUP], Chengfeng Qin[SUP] 4 [/SUP], Zihe Rao[SUP] 1 [/SUP], Xiangxi Wang[SUP] 5 6 [/SUP], Fei Sun[SUP] 5 2 7 8 [/SUP], Yun Zhu[SUP] 5 [/SUP]
Affiliations
- PMID: 34782481
- DOI: 10.1073/pnas.2112703118
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 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.
Keywords: SARS-CoV-2; cryo-electron tomography; postfusion state; spike protein; subtomogram analysis.