期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 23, 期 9, 页码 853-858出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3271
关键词
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资金
- Francis Crick Institute
- Cancer Research UK
- UK Medical Research Council [U117581334]
- Wellcome Trust
- The Francis Crick Institute [10143] Funding Source: researchfish
The lipid-enveloped influenza virus enters host cells during infection by binding cell-surface receptors and, after receptor-mediated endocytosis, fusing with the membrane of the endosome and delivering the viral genome and transcription machinery into the host cell. These events are mediated by the hemagglutinin (HA) surface glycoprotein. At the low pH of the endosome, an irreversible conformational change in the HA, including the exposure of the hydrophobic fusion peptide, activates membrane fusion. Here we used electron cryomicroscopy and cryotomography to image the fusion of influenza virus with target membranes at low pH. We visualized structural intermediates of HA and their interactions with membranes during the course of membrane fusion as well as ultrastructural changes in the virus that accompany membrane fusion. Our observations are relevant to a wide range of protein mediated membrane-fusion processes and demonstrate how dynamic membrane events may be studied by cryomicroscopy.
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