The Cytotoxic Fimbrial Structural Subunit of Xenorhabdus nematophila Is a Pore-Forming Toxin
Open Access
- 15 November 2006
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 188 (22) , 7957-7962
- https://doi.org/10.1128/jb.00787-06
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.Keywords
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