LeoA,B and C from Enterotoxigenic Escherichia coli (ETEC) Are Bacterial Dynamins |
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| Authors: | Katharine A. Michie Anders Boysen Harry H. Low Jakob M?ller-Jensen Jan L?we |
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| Affiliation: | 1. MRC Laboratory of Molecular Biology, Structural Studies Division, Cambridge, United Kingdom.; 2. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark.; University of Osnabrueck, Germany, |
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| Abstract: | Escherichia coli (ETEC) strain {"type":"entrez-nucleotide","attrs":{"text":"H10407","term_id":"875229","term_text":"H10407"}}H10407 contains a GTPase virulence factor, LeoA, which is encoded on a pathogenicity island and has been shown to enhance toxin release, potentially through vesicle secretion. By sequence comparisons and X-ray structure determination we now identify LeoA as a bacterial dynamin-like protein (DLP). Proteins of the dynamin family remodel membranes and were once thought to be restricted to eukaryotes. In ETEC {"type":"entrez-nucleotide","attrs":{"text":"H10407","term_id":"875229","term_text":"H10407"}}H10407 LeoA localises to the periplasm where it forms a punctate localisation pattern. Bioinformatic analyses of leoA and the two upstream genes leoB and leoC suggest that LeoA works in concert with a second dynamin-like protein, made up of LeoB and LeoC. Disruption of the leoAB genes leads to a reduction in secretion of periplasmic Tat-GFP and outer membrane OmpA. Our data suggest a role for LeoABC dynamin-like proteins in potentiating virulence through membrane vesicle associated toxin secretion. |
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