| Literature DB >> 16950919 |
Jyotirmoy Banerjee1, Jitendra Singh, Mohan Chandra Joshi, Shubhendu Ghosh, Nirupama Banerjee.
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.Entities:
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Year: 2006 PMID: 16950919 PMCID: PMC1636316 DOI: 10.1128/JB.00787-06
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490