We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability
- Authors
Carter, Stephen D.; Dent, Kyle C.; Atkins, Elizabeth; Foster, Toshana L.; Verow, Mark; Gorny, Petra; Harris, Mark; Hiscox, Julian A.; Ranson, Neil A.; Griffin, Stephen; Barr, John N.
- Abstract
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. Structured summary: MINT-7890792, MINT-7890805: SH (uniprotkb:P04852) and SH (uniprotkb:P04852) bind (MI:0407) by chromatography technology (MI:0091) MINT-7890784, MINT-7890776: SH (uniprotkb:P04852) and SH (uniprotkb:P04852) bind (MI:0407) by electron microscopy (MI:0040)
- Subjects
RESPIRATORY infections in children; FUNGAL proteins; RESPIRATORY syncytial virus; OLIGOMERS; ELECTRON microscopy; CELL membranes; PERMEABILITY
- Publication
FEBS Letters, 2010, Vol 584, Issue 13, p2786
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2010.05.006