Research

Antibody-antigen recognition is a critically important biological process, underlying the immune response and the mechanism of action of biotherapeutics and vaccines. Due to the size and complexity of intact antibody-antigen complexes, our understanding of what constitutes an effective antibody interaction is often limited to static structures of isolated subunits. Using emerging biophysical and structural tools such as structural mass spectrometry, our lab seeks to characterize the interactions of intact antibody-antigen complexes in their native solution state and use this information to advance the development of biotherapeutic approaches against infectious diseases and cancer. We are currently investigating such interactions for understanding antibody-mediated neutralization of staphylococcal enterotoxins and cancer recognition by immunoglobulin μ (IgM).

Glycosylation plays a role in nearly all aspects of biology, it is estimated that over 50% of the human proteome is decorated with glycosylation. Yet despite its importance, our knowledge of glycobiology has been hindered by the analytical challenges posed by the structural complexity of carbohydrates. Mass spectrometry provides a sensitive and rapid tool for analyzing protein glycosylation, but it provides little regarding stereochemistry or linkage information. Another focus of our lab is developing and implementing novel mass spectrometry-based methods for obtaining a higher level of structural information for biologically relevant glycans and oligosaccharides.