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Christina R. Bourne

Christina R. Bourne

Christina R. Bourne

Associate Professor

Research Areas: Biochemistry, Structural Biology
Office: SLSRC 2610

B.S., 1998, University of Oklahoma 
Ph.D., 2003, Oklahoma Medical Research Foundation and University of Oklahoma Health Sciences Center
Postdoc, 2003-2007, University of Oklahoma Health Sciences Center 
Associate Research Scientist, 2007-2013, Oklahoma State University

Research Keywords: 
structural biology, anti-bacterial, microbiology, biochemistry

Structure-Activity Guided Innovation of Antibacterial Strategies

Our research interests are in the relation of protein function to macromolecular structure. We are integrating X-ray crystallography with microbiology and biochemistry to answer questions about toxin-antitoxin systems and other proteins, and their roles in bacteria that cause human disease.

Analysis of Type II Toxin-Antitoxin Systems in Bacteria 

This work focuses on understanding the mechanistic details of the RelE/ParE structural family. Our emphasis is on ParE toxin inhibition of DNA gyrase, the impact this has on bacterial cells, and the potential to use this in a novel therapeutic approach. Our work is leading the field in understanding the roles for these TA systems.
We have found that chromosomally-encoded ParE toxins have an attenuated activity, providing a window for bacterial cells to co-opt this into pathways for homeostasis. Current investigations are evaluating a role for this activity in driving mutations during adaptation, a known risk factor in the development of antimicrobial resistance.

Crystallographic analysis of folate enzymes with substrate-mimetic probes

Targeting Bacterial Folate Biosynthetic Enzymes

This work is focued on a validated pathway with a proven highly efficacious target, dihydrofolate reductase (DHFR). Trimethoprim, a WHO "essential medicine", effectively inhibits this enzyme but rising resistance is jeopardizing this target. We are pioneering new anti-DHFR compounds and an approach to inhibit multiple folate enzymes simulatenously, reducing the emergence of resistance while preserving this critical class of anti-bacterial therapeutics.

Our lab strives to maintain a strongly positive and encouraging environment for continual learning by all members.