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.

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.

Citation

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., & Barr, J. N. (2010). Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability. FEBS Letters, 584(13), 2786-2790. https://doi.org/10.1016/j.febslet.2010.05.006

• Journal Article Type: Article
• Acceptance Date: May 3, 2010
• Online Publication Date: May 20, 2010
• Publication Date: Jul 2, 2010
• Deposit Date: Mar 22, 2019
• Publicly Available Date: Mar 29, 2020
• Journal: FEBS Letters
• Print ISSN: 0014-5793
• Publisher: Wiley
• Peer Reviewed: Peer Reviewed
• Volume: 584
• Issue: 13
• Pages: 2786-2790
• DOI: https://doi.org/10.1016/j.febslet.2010.05.006
• Keywords: Biophysics; Genetics; Cell Biology; Biochemistry; Molecular Biology; Structural Biology
• Public URL: https://nottingham-repository.worktribe.com/output/1676655
• Publisher URL: https://febs.onlinelibrary.wiley.com/doi/full/10.1016/j.febslet.2010.05.006
• Contract Date: Mar 22, 2019