Glycoproteins and flavoenzymes: mechanism studies and biotechnological application

Our main interests are the understanding of how glycosyltransferases (GTs), glycosylhydrolases, transglycosylases (TGs) and carbohydrate binding proteins bind to its ligands and catalyze chemical reactions as potential drug targets to treat diseases. We work with the following enzymes: a) Gas2, Gel4, Phr1 and Phr2, TGs involved in remodelling of the cell wall and drug targets for Aspergilosis, Candidiasis and Cryptococcosis; b) ppGalNAc transferases (ppGalNAcTs) thattransfer GalNAc into mucins and are relevant in lung diseases, osteoporosis and some type of cancers; c) mucinases, that hydrolyzes mucins; d) NGTs from bacteria, in particular, NleB from Gram-negative and NGTs from Haemophilus influenza and Actinobacillus pleuropneumoniae. These bacteria require these activities to promote infection in their respective hosts; e) FUT8, a fucosyltransferase that fucosylates the innermost GlcNAc of N-glycans, is a drug target for cancer; f) anti-Tn and anti-STn antibodies such as 5E5, G2D11 and mutants and chimeras of G2D11. These antibodies are anti-cancer molecules and likely useful to diagnose cancer; g) core 3 synthases and ST6GalNAcI, that glycosylate the Tn antigen. The overexpression of the latter enzyme is intricately related with the development of cancer. On the other hand, flavoproteins catalyze redox reactions in cells, and those produced by pathogens could become potential targets since many of them play a role in defending against host-induced stress conditions. Our goal is to increase the use of all of these proteins in biotechnological and therapeutic applications by understanding their mechanisms. In addition, we are studying other systems like symbiotic globins from plants that exhibit new functions and also ferric regulators and transcription factors that interact with DNA