Research
Our work is kindly funded by NIH, NSF (Biofgreat.org), and the Michael J. Fox Foundation
Mutations in O-GlcNAc transferase (OGT) cause X-linked intellectual disability by altering protein modification, interactions, and gene regulation. Our work combines biochemistry, genome engineering, and functional genomics to define shared disease mechanisms and identify potential therapeutic targets.
Dystroglycanopathies are a subset of congenital muscular dystrophies caused by defects in the M3 glycosylation pathway that modifies alpha-dystroglycan with matriglycan, a structure essential for extracellular matrix binding and viral interactions. Our work investigates how M3 enzymes function, how disease-associated variants alter this pathway, and identifies new genes involved in dystroglycanopathies, with the goal of advancing both fundamental biology and early therapeutic strategies.
The glycan shield is a major driver of heterogeneity in HIV viruses and has a major impact on immunogenicity. We work with Dr. Alon Herschorn's laboratory to characterize various trimers and pseudovirus glycosylation patterns as correlates of immunity and antibody development.
The reduction of the O-GlcNAc modification in the brain has been tightly associated with a number of neurodegenerative conditions. Working with researchers at University of Southern California and California Institute of Technology, we are evaluating the O-GlcNAcome in patient and control brain regions.
BioF:GREAT is a multidisciplinary biofoundry advancing glycoscience research, technology, and education to bring glycans into the scientific mainstream. Leveraging expertise in glycoenzymes, mass spectrometry, AI, and pedagogy, the program develops new tools, training, and instructional resources while providing equitable access to cutting-edge infrastructure for researchers and educators, with broad impacts across bioenergy, biomedicine, and biomaterials.