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Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability.

ABSTRACT: Human respiratory syncytial virus (HRSV) is the leading cause of lower respiratory tract disease in infants. The HRSV small hydrophobic (SH) protein plays an important role in HRSV pathogenesis, although its mode of action is unclear. Analysis of the ability of SH protein to induce membrane permeability and form homo-oligomers suggests it acts as a viroporin. For the first time, we directly observed functional SH protein using electron microscopy, which revealed SH forms multimeric ring-like objects with a prominent central stained region. Based on current and existing functional data, we propose this region represents the channel that mediates membrane permeability.

SUBMITTER: Carter SD 

PROVIDER: S-EPMC2896471 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability.

Carter Stephen D SD   Dent Kyle C KC   Atkins Elizabeth E   Foster Toshana L TL   Verow Mark M   Gorny Petra P   Harris Mark M   Hiscox Julian A JA   Ranson Neil A NA   Griffin Stephen S   Barr John N JN  

FEBS letters 20100520 13

Human respiratory syncytial virus (HRSV) is the leading cause of lower respiratory tract disease in infants. The HRSV small hydrophobic (SH) protein plays an important role in HRSV pathogenesis, although its mode of action is unclear. Analysis of the ability of SH protein to induce membrane permeability and form homo-oligomers suggests it acts as a viroporin. For the first time, we directly observed functional SH protein using electron microscopy, which revealed SH forms multimeric ring-like obj  ...[more]

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