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Kinetic characterization of VopT, a mono-ADP-ribosyltransferase toxin from Vibrio parahaemolyticus

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dc.contributor.advisor Merrill, Rod Poole, Amanda 2016-09-15T20:25:34Z 2016-09-15T20:25:34Z 2016-09 2016-09-13 2016-09-15
dc.description.abstract Pathogenic bacteria cause many human infections, and most employ virulence factors that cause cell or tissue damage in the host. One important virulence factor group is the mono-ADP-ribosyltransferase (mART) family. Vibrio parahaemolyticus is a pathogenic bacterium that encodes a virulence factor, VopT, a mART toxin. VopT modifies Ras, a small GTPase involved in cell signaling, leading to intestinal epithelial tissue damage. VopT is classified as an ExoS-like toxin as it requires the binding of a 14-3-3 protein for activation and shares high sequence identity to other ExoS-like members. Glycohydrolase activities were assessed for wild-type and catalytic variants, the first inhibitors of VopT were identified with IC50 values between 4 and 45 µM, and an ExoT homology model was produced that provides insight into the FAS-dependent activity of VopT. Characterization of VopT has increased our understanding of mART enzymes and may lead to the development of effective therapeutic compounds. en_US
dc.description.sponsorship NSERC and CIHR en_US
dc.language.iso en en_US
dc.rights Attribution-NonCommercial-ShareAlike 2.5 Canada *
dc.rights.uri *
dc.subject mART toxin en_US
dc.subject Vibrio parahaemolyticus en_US
dc.subject VopT en_US
dc.subject enzyme kinetics en_US
dc.subject virulence factor en_US
dc.title Kinetic characterization of VopT, a mono-ADP-ribosyltransferase toxin from Vibrio parahaemolyticus en_US
dc.type Thesis en_US Molecular and Cellular Biology en_US Master of Science en_US Department of Molecular and Cellular Biology en_US
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Attribution-NonCommercial-ShareAlike 2.5 Canada Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 2.5 Canada