James Rini

Dr. James Rini obtained his Ph.D. from the department of Medical Biophysics at the University of Toronto studying protein-carbohydrate interactions.  He then did postdoctoral training at the Research Institute of Scripps Clinic where he worked on antibody-mediated viral neutralization.  He is currently a professor in the departments of Molecular Genetics and Biochemistry.

Our research focuses on coronavirus-receptor interactions and the role played by ER-resident glycosyltransferases in protein folding and subcellular targeting.  In all cases, we take a structural approach using electron cryo-microscopy (Cryo-EM) and x-ray crystallography supported by a range of biophysical and cell-based assays. 

The coronavirus project is currently centred on the spike proteins of the four seasonal coronaviruses that account for 15-30% of common colds.  The work ranges from receptor identification to efforts aimed at understanding how spike protein conformational changes mediate receptor binding, immune escape and the evasion of decoy receptors.  It is fundamental in nature and seeks to characterize the mechanistic basis for how these coronaviruses have adapted to their human hosts.  Over the long-term this knowledge will be valuable in the development of vaccines and antivirals against emerging coronavirus threats.  Our work on the SARS-CoV-2 spike protein, for example, has already led to the design of candidate multivalent antibody therapeutics and vaccines. 

Our most recent work in the glycosyltransferase area deals with the protein-O-glycosyltransferases specific for the EGF-like domains found in the Notch receptor and its ligands.  It is not only uncovering how these enzymes ensure the proper folding and targeting of these signaling molecules but the likely role that they played in the evolution of multicellular organisms.  Our work on glycosyltransferases also extends to those that modify N-glycans to mediate ER protein folding and lysosomal enzyme targeting.  How these enzymes recognize their folded and unfolded substrates remains essentially unknown, and the goal is to fill that knowledge gap through structural and biochemical analysis.  Proper functioning of these enzymes is essential for maintaining protein homeostasis, and our work promises to elucidate how their failure gives rise to a range of human diseases.

Appointments, Cross Affiliations, Memberships

Professor Department of Molecular Genetics

Courses Taught

BCH374Y1 Research Project in Biochemistry
JBB2025H Protein Crystallography
BCH473Y Advanced Research Project in Biochemistry
BCH440H (BCH1440H) Protein Homeostasis
BCH444H Protein Trafficking in the Secretory and Endocytic Pathways