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

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• 作者：Stephen D. Carter ; Kyle C. Dent ; Elizabeth Atkins ; Toshana L. Foster ; Mark Verow ; Petra Gorny ; Mark Harris ; Julian A. Hiscox ; Neil A. Ranson ; Stephen Griffin ; John N. Barr
• 关键词：Respiratory syncytial virus ; Viroporin ; Channel ; SH protein
• 刊名：FEBS Letters
• 出版年：2010
• 出版时间：2 July 2010
• 年：2010
• 卷：584
• 期：13
• 页码：2786-2790
• 全文大小：1101 K

文摘

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.

Structured summary

MINT-7890792, MINT-7890805: SH (uniprotkb:P04852) and SH (uniprotkb:P04852) bind (MI:0407) by chromatography technology (MI:0091)

MINT-7890784, MINT-7890776: SH (uniprotkb:P04852) and SH (uniprotkb:P04852) bind (MI:0407) by electron microscopy (MI:0040)