tetano
Editor, Senior Moderator
Nat Struct Mol Biol. 2016 Aug 8. doi: 10.1038/nsmb.3271. [Epub ahead of print]
[h=1]Cryomicroscopy provides structural snapshots of influenza virus membrane fusion.[/h] Calder LJ[SUP]1[/SUP], Rosenthal PB[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
PMID: 27501535 DOI: 10.1038/nsmb.3271
[PubMed - as supplied by publisher]
[h=1]Cryomicroscopy provides structural snapshots of influenza virus membrane fusion.[/h] Calder LJ[SUP]1[/SUP], Rosenthal PB[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
PMID: 27501535 DOI: 10.1038/nsmb.3271
[PubMed - as supplied by publisher]