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Larvin: The characterization of a novel mono-ADP-ribosyltransferase toxin

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dc.contributor.advisor Merrill, Rod Krska, Daniel 2014-05-12T16:43:43Z 2014-05-12T16:43:43Z 2014-04 2014-04-14 2014-05-12
dc.description.abstract Mono-ADP-ribosyltransferase (mART) toxins are a class of bacterial proteins which function by cleaving the nicotinamide moiety from NAD+ and attaching the ADP-ribose to a host protein, to alter its function. These are important virulence factors for many diseases. Larvin is a novel mART toxin from Paenibacillus larvae, the causative agent of American Foulbrood in honey bees. Larvin targets RhoA as a substrate for its transferase reaction, and kinetics for the RhoA substrate were characterized for the first time for the mART C3 subgroup. A small molecule inhibitor of Larvin enzymatic activity was discovered, the first known inhibitor for C3 toxins. Larvin was crystallized, and its crystal structure was solved to 2.3 Å resolution. Larvin was also shown to have a different mechanism of cell entry from other C3 toxins. Characterization of Larvin allows for a fuller understanding of the mART family, and for development of better inhibitors as potential therapeutics. en_US
dc.language.iso en en_US
dc.rights Attribution-NonCommercial-NoDerivs 2.5 Canada *
dc.rights.uri *
dc.subject Biochemistry en_US
dc.subject Enzyme Kinetics en_US
dc.subject mono-ADP-ribostyltransferase en_US
dc.subject Protein Structure en_US
dc.subject Protein Toxin en_US
dc.subject Enzyme Inhibition en_US
dc.subject Fluorescence Assay en_US
dc.title Larvin: The characterization of a novel mono-ADP-ribosyltransferase toxin en_US
dc.type Thesis en_US Biophysics en_US Master of Science en_US Department of Molecular and Cellular Biology en_US
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Attribution-NonCommercial-NoDerivs 2.5 Canada Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 2.5 Canada