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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Carter SD,Dent KC,Atkins E,Foster TL,Verow M,Gorny P,Harris M,Hiscox JA,Ranson NA,Griffin S,Barr JNdoi
10.1016/j.febslet.2010.05.006subject
Has Abstractpub_date
2010-07-02 00:00:00pages
2786-90issue
13eissn
0014-5793issn
1873-3468pii
S0014-5793(10)00395-9journal_volume
584pub_type
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