Research Scientist, Microbial Infection and Immunity
Laboratory of
Dr. Brian Ahmer
Contact information:
750 Biomedical Research Tower (BRT)
460 W 12th Ave, Columbus OH 43210
Phone:
614-292-7666
anice.sabag-daigle@osumc.edu
View publications
Research Interests
Dr. Sabag-Daigle's primary research interest is the regulation of virulence and metabolic gene expression by pathogenic microbes. These investigations provide a mechanistic view of how microorganisms interact with each other and the host. This knowledge can ultimately inform our understanding of pathogenesis and enable selection of novel therapeutic drug targets. Her doctoral work provided an excellent foundation for a career in bacterial gene regulation through the study of transcriptional regulation of carbon and nitrogen pathways in archaeal and bacterial systems. This training afforded her the opportunity to develop a specialized technical and analytical skillset that has proven useful in the study of complex interspecies interactions. It has also allowed her to follow her personal interests by transitioning to the study of medically relevant pathogens. Working in the Ahmer lab provides an exciting platform on which to contribute formative research findings that have the potential to directly impact human lives. Her expertise in transcription regulation and carbon nitrogen metabolism lends itself nicely to the characterization of the fructose-asparagine (F-Asn) utilization pathway (fra) in Salmonella, and is also relevant in the lab's studies with the SdiA regulons of Salmonella, E. coli, and Enterobacter.
Dr. Sabag-Daigle's current focus in the Ahmer lab is elucidation and continued characterization of the fra pathway and its potential for further development as a therapeutic target. The lab is interested in the development of small molecule inhibitors of the fra operon with the expectation that inhibition of this pathway will be detrimental to the growth of Salmonella in the intestine. This is significant because very few bacteria have the genetic potential to utilize F-Asn, which makes a fra inhibitor a potentially Salmonella-specific antimicrobial.
