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 Research Program and Goals:

My research interests are focused on the biochemical and cell biological action of bacterial toxins that target the actin cytoskeleton.  Pathogenic bacteria often secrete toxins that target the cytoskeleton in order to subvert the immune defenses of their host.  These toxins must gain access to the cytosol of target cells via transport across a biological membrane in order to carry out their function.  Once inside the target cell, these bacterial toxins carry out a multitude of different activities including proteolysis, phosphorylation, or other post-translational modification of host proteins in order to down-regulate signaling cascades connected with the actin cytoskeleton in order to inhibit innate immune processes including phagocytosis and chemotaxis.  My goals are to understand the transport of actin-targeting toxins such as iota toxin from Clostridium difficile and RTX from Vibrio cholerae across cellular membranes and their subsequent action on the actin cytoskeleton within target cells.

Selected Publications:

Juris, S.J., Shah, K., Shokat, K., Dixon, J.E., and Vacratsis, P.O. Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry.  FEBS Lett.  580: 179-183. (2006)

Krantz, B.A., Melnyk, R.A., Zhang, S., Juris, S.J., Lacy, D.B., Wu, Z., Finkelstein, A., and Collier, R.J. A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.  Science.  309: 777-781. (2005)

Wigelsworth, D.J., Krantz, B.A., Christensen, K.A., Lacy, D.B., Juris, S.J., and Collier, R.J. Binding stoichiometry and kinetics of the interaction of a human anthrax toxin receptor, CMG2, with protective antigen.  J. Biol. Chem.  279: 23349-23356. (2004)

Juris, S.J., Shao^, F., and Dixon , J.E. Yersinia effectors target mammalian signaling pathways.  Cell. Microbiol.  4: 201-211. (2002)