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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.

Authors

Stephen D. Carter

Kyle C. Dent

Elizabeth Atkins

Mark Verow

Petra Gorny

Mark Harris

Julian A. Hiscox

Neil A. Ranson

Stephen Griffin

John N. Barr



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., …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 28, 2024
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

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