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

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 Lett

journal_title

FEBS letters

authors

Carter SD,Dent KC,Atkins E,Foster TL,Verow M,Gorny P,Harris M,Hiscox JA,Ranson NA,Griffin S,Barr JN

doi

10.1016/j.febslet.2010.05.006

subject

Has Abstract

pub_date

2010-07-02 00:00:00

pages

2786-90

issue

13

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(10)00395-9

journal_volume

584

pub_type

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