The ability of prions to convert normal prion protein into additional prions can be exploited for
the purpose of diagnosing and studying prion diseases. Prions can be detected by infecting
susceptible cells or by using a technique called RT-QuIC. In both experimental systems, it is
important that a compatible version of the normal prion protein is used for detecting prions. One
such version is the prion protein from the bank vole. Bank voles are rodents that are remarkably
susceptible to prions, and the bank vole prion protein can easily be converted into prions by
prion aggregates from several different animal species. The goal of this proposal is to further
optimize the normal bank vole prion protein so that it becomes even more susceptible to prions,
enhancing the ability of prions to be studied using cells and improving the diagnostic sensitivity
of the RT-QuIC test.
Dr. Watts obtained his PhD in Laboratory Medicine and Pathobiology from the University of Toronto and then conducted postdoctoral research in the lab of Stanley Prusiner at the University of California San Francisco. He is currently a Principal Investigator at the Tanz Centre for Research in Neurodegenerative Diseases, an Associate Professor within the Department of Biochemistry at the University of Toronto, and is the Canada Research Chair in Protein Misfolding Disorders. His research interests include studying the role of protein aggregate strains in Alzheimer’s disease and Parkinson’s disease as well as exploiting the unique properties of the bank vole prion protein to understand how prions form spontaneously in the brain.