Priola Research Group

Research in this laboratory focuses on the molecular basis of disease in transmissible spongiform encephalopathy (TSE) or prion diseases. Prion diseases are a group of neurodegenerative diseases that include sporadic, iatrogenic, and familial Creutzfeldt-Jakob disease (CJD) in humans: scrapie in sheep; chronic wasting disease (CWD) in deer, elk, and moose; and bovine spongiform encephalopathy (BSE) in cattle.

The conversion of the normally soluble and protease-sensitive host prion protein, PrP^C, to an insoluble and partially protease-resistant form, PrP^Sc, is a key event in prion pathogenesis, and PrP^C is required for prion infection and disease to occur. Using both in vitro and in vivo model systems, our laboratory studies the role of PrP^C and PrP^Sc in several aspects of prion pathogenesis, including: 1) the molecular pathogenesis of prion species barriers and strains; 2) the establishment of acute versus chronic prion infection; 3) the contribution of mitochondria to prion pathogenesis; and 4) the development of prion vaccines and therapeutics.