tetano
Editor, Senior Moderator
Nature
. 2023 Jun 7.
doi: 10.1038/s41586-023-06273-4. Online ahead of print. Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane
Wei Shi[SUP] #[/SUP][SUP] 1 2 [/SUP], Yongfei Cai[SUP] 1 2 3 [/SUP], Haisun Zhu[SUP] 4 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Jewel Voyer[SUP] 1 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Hong Cao[SUP] 5 [/SUP], Megan L Mayer[SUP] 6 [/SUP], Kangkang Song[SUP] 7 [/SUP], Chen Xu[SUP] 7 [/SUP], Jianming Lu[SUP] 5 8 [/SUP], Jun Zhang[SUP] #[/SUP][SUP] 9 10 [/SUP], Bing Chen[SUP] 11 12 [/SUP]
Affiliations
Entry of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) into host cells depends on refolding of the virus-encoded spike protein from a prefusion conformation, metastable after cleavage, to a lower energy, stable postfusion conformation[SUP]1,2[/SUP]. This transition overcomes kinetic barriers for fusion of viral and target cell membranes[SUP]3,4[/SUP]. We report here a cryo-EM structure of the intact postfusion spike in a lipid bilayer that represents single-membrane product of the fusion reaction. The structure provides structural definition of the functionally critical membrane-interacting segments, including the fusion peptide and transmembrane anchor. The internal fusion peptide forms a hairpin-like wedge that spans almost the entire lipid bilayer and the transmembrane segment wraps around the fusion peptide at the last stage of membrane fusion. These results advance our understanding of the spike protein in a membrane environment and may guide development of intervention strategies.
. 2023 Jun 7.
doi: 10.1038/s41586-023-06273-4. Online ahead of print. Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane
Wei Shi[SUP] #[/SUP][SUP] 1 2 [/SUP], Yongfei Cai[SUP] 1 2 3 [/SUP], Haisun Zhu[SUP] 4 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Jewel Voyer[SUP] 1 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Hong Cao[SUP] 5 [/SUP], Megan L Mayer[SUP] 6 [/SUP], Kangkang Song[SUP] 7 [/SUP], Chen Xu[SUP] 7 [/SUP], Jianming Lu[SUP] 5 8 [/SUP], Jun Zhang[SUP] #[/SUP][SUP] 9 10 [/SUP], Bing Chen[SUP] 11 12 [/SUP]
Affiliations
- PMID: 37285872
- DOI: 10.1038/s41586-023-06273-4
Entry of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) into host cells depends on refolding of the virus-encoded spike protein from a prefusion conformation, metastable after cleavage, to a lower energy, stable postfusion conformation[SUP]1,2[/SUP]. This transition overcomes kinetic barriers for fusion of viral and target cell membranes[SUP]3,4[/SUP]. We report here a cryo-EM structure of the intact postfusion spike in a lipid bilayer that represents single-membrane product of the fusion reaction. The structure provides structural definition of the functionally critical membrane-interacting segments, including the fusion peptide and transmembrane anchor. The internal fusion peptide forms a hairpin-like wedge that spans almost the entire lipid bilayer and the transmembrane segment wraps around the fusion peptide at the last stage of membrane fusion. These results advance our understanding of the spike protein in a membrane environment and may guide development of intervention strategies.