Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane

Wei Shi, Yongfei Cai, Haisun Zhu, Hanqin Peng, Jewel Voyer, Sophia Rits-Volloch, Hong Cao, Megan L. Mayer, Kangkang Song, Chen Xu, Jianming Lu, Jun Zhang () and Bing Chen ()
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Wei Shi: Boston Children’s Hospital
Yongfei Cai: Boston Children’s Hospital
Haisun Zhu: Harvard Institutes of Medicine
Hanqin Peng: Boston Children’s Hospital
Jewel Voyer: Boston Children’s Hospital
Sophia Rits-Volloch: Boston Children’s Hospital
Hong Cao: Codex BioSolutions
Megan L. Mayer: The Harvard Cryo-EM Center for Structural Biology
Kangkang Song: University of Massachusetts Chan Medical School
Chen Xu: University of Massachusetts Chan Medical School
Jianming Lu: Codex BioSolutions
Jun Zhang: Boston Children’s Hospital
Bing Chen: Boston Children’s Hospital

Nature, 2023, vol. 619, issue 7969, 403-409

Abstract: Abstract The entry of SARS-CoV-2 into host cells depends on the refolding of the virus-encoded spike protein from a prefusion conformation, which is metastable after cleavage, to a lower-energy stable postfusion conformation1,2. This transition overcomes kinetic barriers for fusion of viral and target cell membranes3,4. Here we report a cryogenic electron microscopy (cryo-EM) structure of the intact postfusion spike in a lipid bilayer that represents the 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.

Date: 2023
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DOI: 10.1038/s41586-023-06273-4

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