Enzymes for Glycobiology
Our research has been focused on the investigation of the structure and function of the enzymes involved in making various glycoconjugates. The lab studies bacterial enzymes which make cell surface carbohydrate structure mimics of the host they infect, as well as the corresponding eukaryotic enzymes. We are also applying these enzymes to the synthesis of bioactive glycoconjugates for various therapeutic applications. Part of this work is the creation of designer enzymes for these applications.
Synthetic biology and its application for Glycobiology
We have been working on improving therapeutic proteins through their glycosylation. We have been engineering in vivo protein glycosylation through improving landing sites for glycosyltransferases. Our work includes design of synthetic operons to add biosynthetic pathways for glycosylation into various host organisms. The lab is also working on a natural protein glycosylation system (O-mannosylation) in bacteria which has is conserved all the way up the evolutionary ladder. The fundamental question is what does this protein modification do for these bacteria? We are applying synthetic biology and glycoproteomics to address this complex problem in the hope we can uncover fundamental knowledge of how this glycosylation process plays a role in biology.