The focus of my research is centered on understanding the fundamental aspects on transferase enzymes (TEs) from bacteria. In fact, many bacterial TEs are toxins inactivating protein targets in host cells.
The aim is to
1. Elucidate the reaction mechanism of TEs
2. Identify new TE toxins causing elevated virulence in bacteria
3. Identify and characterize new TE inhibitors
Much of this work is based on X-ray crystallography and enzyme kinetics, but also relies on small angle Xray scattering, mass spectrometry, capillary electrophoresis and fluorescence spectroscopy. Since X-ray structures only provide static images of a molecule of interest, it is crucial to find alternative approaches to capture different reaction states that can elucidate the dynamics and mechanism of the enzyme. Recently, I have used inhibitors and substrate analogues in binding experiments, which have led to breakthroughs in learning about the reaction mechanism of TEs and have resulted in several high-impact publications.
Currently, I work on consolidating a research group at SSI continuing the identification and characterization of bacterial TE virulence factors. SSI has a highly competitive research program on developing antimicrobial drugs and methods for diagnosis of bacterial infections. One of the main pillars of this research is based on gaining detailed knowledge on host-bacterial interactions during infections. Therefore, our lab is in a perfect position to supplement this ongoing research with functional and structural studies on the factors responsible for disease symptoms during an infection.
Recently, the group has initiated a side project studying a newly identified TE, called Fic, from C. difficile. In general, Fic proteins are very scarcely described. Our work on this Fic has already resulted in one publication and more are under way. We constantly make new discoveries on this group of enzymes and we still have only scraped the surface in trying to understand how Fic proteins work.