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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; Bing Chen.
Afiliação
  • Wei Shi; Boston Childrens Hospital/Harvard Medical School
  • Yongfei Cai; Boston Childrens Hospital/Harvard Medical School
  • Haisun Zhu; Institute for Protein Innovation/Harvard Institutes of Medicine
  • Hanqin Peng; Boston Childrens Hospital
  • Jewel Voyer; Boston Childrens Hospital
  • Sophia Rits-Volloch; Boston Childrens Hospital
  • Hong Cao; Codex BioSolutions, Inc.
  • Megan L. Mayer; The Harvard Cryo-EM Center for Structural Biology
  • Kangkang Song; University of Massachusetts Chan Medical School
  • Chen Xu; University of Massachusetts Medical School
  • Jianming Lu; Codex BioSolutions, Inc.
  • Jun Zhang; Boston Childrens Hospital/Harvard Medical School
  • Bing Chen; Boston Childrens Hospital/Harvard Medical School
Preprint em Inglês | bioRxiv | ID: ppbiorxiv-519151
ABSTRACT
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. This transition overcomes kinetic barriers for fusion of viral and target cell membranes. 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 membraneinteracting 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.
Licença
cc_no
Texto completo: Disponível Coleções: Preprints Base de dados: bioRxiv Idioma: Inglês Ano de publicação: 2022 Tipo de documento: Preprint
Texto completo: Disponível Coleções: Preprints Base de dados: bioRxiv Idioma: Inglês Ano de publicação: 2022 Tipo de documento: Preprint
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