A key quest of my research during the past 35 years has been to understand the structure and function of glycoconjugates in cell adhesion and signaling, studying the molecular and biochemical functions of surface and secreted glycoproteins in normal biological processes and disease. We study the molecular nature and specificity of protein-glycan interactions and their roles in biology, and how glycans are recognized by glycan-binding proteins (GBPs). My laboratory has been instrumental in developing new technologies in glycoscience, discovering novel functions of glycans in immune recognition and modulation, viral (influenza), parasitic (helminth) and bacterial infections, cell adhesion, selectin biology and leukocyte trafficking, new enzymes and molecular chaperones that regulate protein glycosylation, and educating students in the field of glycoscience.
Early work in our laboratory established the identities and specificities of many glycosyltransferases and glycan-binding proteins and plant lectins. In our translational studies, we are exploring glycoimmunology, and the roles of adaptive and innate immune responses to pathogens, as well as human diseases that are both heritable and acquired, and which involve altered glycosylation. We have developed novel techniques in the field for glycan analysis and for exploring the structure/function relationships of glycans, using genetic/molecular approaches, biophysical and biochemical strategies, and multiple glycan microarray and glycan bead strategies. We are also developing semi-synthetic methods for making glycoconjugates and for isolating, characterizing, and derivatizing glycans. Such technologies are revolutionary and are growing at a rapid pace; thus, I expect such microarray (and flow cytometry-based arrays) to be a major contributor to the field of glycoscience going forward.