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Faculty
Donald R. Ronning
Associate Professor
Email: Donald.Ronning@utoledo.edu
Office: WO 4203B
Phone: (419) 530-1585
Graphics: (419) 530-1591
Lab: (419) 530-1588
Fax: (419) 530-4033
Professional Background:
B.S., Biochemistry, 1995, University of Minnesota
Ph.D., 2001, Texas A&M University
Postdoctoral Fellow, 2001-2005, National Institutes of Health
Group page
Research Synopsis:
M. tuberculosis pathogenesis and therapy
Gene Regulation - One hallmark of M. tuberculosis is the uncommon ability to survive and readily multiply in human macrophages. The proteomic response by M. tb to the harsh environment within the macrophage is specific and many of the details of this response are coming to light.
We are focusing on two systems that control gene expression, PhoP and Lsr2. While these two system control gene expression
by different mechanisms, the ultimate goal of these projects is to identify compounds that can modulate the binding of these
proteins to their DNA targets.
Host Pathogen Interactions - Another protein that important for the ability of M. tb to survive in macrophages is termed Enhanced Intracellular Survival or Eis. This CoA-dependent transferase enters the macrophage cytoplasm and modulates the release of cytokines by the infected cell. We are attempting to characterize the substrate specificity of the enzyme to better understand its molecular function in mycobacterial pathogenesis.
Folic Acid Biosynthesis - We are also collaborating with Liem Nguyen (Case Western Reserve University) to study the folic acid biosynthetic pathway and to develop compounds that act as potentiators of antifolate drugs for the treatment of Tuberculosis.
Trehalose Biosynthesis - Trehalose is profoundly important for the survival and virulence of M. tuberculosis. We are studying the essential otsAB biosynthetic pathway responsible for the de novosynthesis of trehalose and may play a role in the biosynthesis of trehalose monomycolate, which is an essential donor molecule required for the building of the Mycobacterial Outer Membrane. Since the antigen 85 enzymes use trehalose monomycolate as a substrate to transfer mycolic acids to the MOM and are essential for the viability of M. tuberculosis, we are studying their enzymatic activity, substrate specificity, and post-translational modification in collaboration with Choong-min Kang (Wayne State University).
