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

FEBS Lett. 2010 Jul 2;584(13):2786-90. doi: 10.1016/j.febslet.2010.05.006. Epub 2010 May 20.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Liposomes / chemistry
  • Microscopy, Electron
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*
  • Recombinant Fusion Proteins / ultrastructure*
  • Respiratory Syncytial Virus, Human / metabolism*
  • Retroviridae Proteins, Oncogenic / chemistry
  • Retroviridae Proteins, Oncogenic / genetics
  • Retroviridae Proteins, Oncogenic / metabolism*
  • Retroviridae Proteins, Oncogenic / ultrastructure*


  • Liposomes
  • Recombinant Fusion Proteins
  • Retroviridae Proteins, Oncogenic
  • small hydrophobic protein, virus