James M. Rini
Our research is focused on the study of coronavirus-host cell receptor interactions, and the role played by glycosyltransferases in protein folding and subcellular targeting. In all cases, we take a structural approach involving x-ray crystallography and electron cryo-microscopy (Cryo-EM). We are currently working on SARS-CoV-2 and the seasonal coronaviruses that cause common cold-like symptoms. By studying the coronavirus Spike protein in complex with receptors and neutralizing antibodies, we seek to understand the basis for viral neutralization, immune evasion, and cross-species transmission. The work is also contributing to the development of antibody therapeutics and vaccines against SARS-CoV-2.
Our most recent work in the glycosyltransferase area deals with the protein-O-glycosyltransferases specific for the EGF-like domains found primarily in the Notch receptor and its ligands. It is not only uncovering how these enzymes ensure the proper folding and targeting of these important signalling molecules but the likely role that they played in the evolution of multicellular organisms. Our interest in glycosyltransferases also extends to those that modify N-glycans to mediate ER protein folding and lysosomal enzyme targeting, processes that are critical in protein homeostasis.
- BCH440H Protein Homeostasis
- JBB2025H Protein Crystallography
- Department of Biochemistry, University of Toronto