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

Carter, S. D. et al. (2010) Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability. FEBS Letters, 584(13), pp. 2786-2790. (doi: 10.1016/j.febslet.2010.05.006) (PMID:20471980) (PMCID:PMC2896471)

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.

• Item Type: Articles
• Additional Information: K.D. and T.F. are supported by Wellcome Trust studentships. E.A. is supported by a BBSRC/Pfizer CASE studentship. J.N.B. is an RCUK fellow and S.G. is recipient of a University of Leeds Biomedical Health Research Centre senior translational research fellowship. HPLC was performed in the Wellcome Trust-funded centre for biomolecular interactions.
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Carter, Dr Stephen
• Authors: Carter, S. D., Dent, K. C., Atkins, E., Foster, T. L., Verow, M., Gorny, P., Harris, M., Hiscox, J. A., Ranson, N. A., Griffin, S., and Barr, J. N.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity; College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research
• Journal Name: FEBS Letters
• Publisher: Elsevier
• ISSN: 0014-5793
• ISSN (Online): 1873-3468
• Published Online: 20 May 2010
• Copyright Holders: Copyright © 2010 Federation of European Biochemical Societies
• First Published: First published in FEBS Letters 584(13): 2786-2790
• Publisher Policy: Reproduced under a Creative Commons License