The cytotoxic fimbrial structural subunit of Xenorhabdus nematophila is a pore-forming toxin

被引：20

作者：

Banerjee, Jyotirmoy

Singh, Jitendra

Joshi, Mohan Chandra

Ghosh, Shubhendu

Banerjee, Nirupama

机构：

[1] Int Ctr Genet Engn & Biotechnol, New Delhi 110067, India

[2] Jawaharlal Nehru Univ, Ctr Biotechnol, New Delhi 110067, India

[3] Univ Delhi, Dept Biophys, New Delhi 110021, India

来源：

JOURNAL OF BACTERIOLOGY | 2006年 / 188卷 / 22期

关键词：

D O I：

10.1128/JB.00787-06

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

We have purified a fimbrial shaft protein (MrxA) of Xenorhabdus nematophila. The soluble monomeric protein lysed larval hemocytes of Helicoverpa armigera. Osmotic protection of the cells with polyethylene glycol suggested that the 17-kDa MrxA subunit makes pores in the target cell membrane. The internal diameter of the pores was estimated to be > 2.9 nm. Electron microscopy confirmed the formation of pores by the fimbrial subunit. MrxA protein oligomerized in the presence of liposomes. Electrophysiological studies demonstrated that MrxA formed large, voltage-gated passive-diffusion channels in lipid bilayers.

引用

页码：7957 / 7962

页数：6

共 36 条

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