Dow Science Complex 338 (Office)
Dow Science Complex 246 (Lab)
Personal Web Page
- B.S., Boston College, 1996
- Ph.D., University of Michigan, 2002
- Postdoc, Harvard Medical School, 2002-2006
Basic Biology, Cell Biology, Biochemistry
Molecular mechanisms of microbial pathogenesis
Current Research Projects
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 the actin-targeting toxin MARTX from
Vibrio cholerae across cellular membranes and its subsequent action on the actin cytoskeleton within target cells. My lab utilizes biochemistry, cell biology, biophysics and genetics to study these questions.
- Hughes, M.A., D.L. Burns, S.J. Juris, W.J. Tang, K.H. Clement, L.J. Eaton, C.D. Kelly-Cirino, M.L. McKee, B.S. Powell, B.L. Bishop, T.L. Rudge, N. Shine, A. Verma, M.S. Willis, and S.A. Morse. 2009. The case for developing consensus standards for research in microbial pathogenesis:
Bacillus anthracis toxins as an example.
Infection and Immunity 77: 4182-4186.
- Basilio, D., S.J. Juris, R.J. Collier, and A. Finkelstein.
Evidence for a proton-protein symport mechanism in the anthrax toxin channel.
Journal of General Physiology 133:307-314.
- Juris, S.J., R.A. Melnyk, R.E. Bolcome III, J. Chan, and R.J. Collier. 2007. Crosslinked forms of the isolated N-terminal domain of the lethal factor are potent inhibitors of anthrax toxin.
Infection and Immunity 75:5052-5058.
- Juris, S.J., K. Shah, K. Shokat, J.E. Dixon, and P.O. Vacratsis. 2006. Identification of otubain 1 as a novel substrate for the
Yersinia protein kinase using chemical genetics and mass spectrometry.
FEBS Letters 580:179-183.
- Krantz, B.A., R.A. Melnyk, S. Zhang, S.J. Juris, D.B. Lacy, Z. Wu, A. Finkelstein, and R.J. Collier. 2005. A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.