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J Bacteriol. 2006 Nov;188(22):7957-62. Epub 2006 Sep 1.

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

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1
International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India.

Abstract

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.

PMID:
16950919
PMCID:
PMC1636316
DOI:
10.1128/JB.00787-06
[Indexed for MEDLINE]
Free PMC Article
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