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Escherichia coli  (ETEC) strain 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 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.

LeoA, B and C from Enterotoxigenic Escherichia coli (ETEC) Are Bacterial Dynamins