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

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.

doi:10.1016/j.febslet.2010.05.006

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Volume 584, Issue 13 , Pages 2786-2790, 2 July 2010

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

Edited by Jacomine Krijnse-Locker

Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK

Received 14 April 2010; received in revised form 29 April 2010; accepted 3 May 2010. published online 14 May 2010.

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.