Suzette Alise Priola, Ph.D.
TSE / Prion Molecular Biology Section
Rocky Mountain Laboratories
Building 3, Room 3115
903 South 4th Street
Hamilton, MT 59840
Research in this laboratory focuses on the molecular basis of disease in transmissible spongiform encephalopathy (TSE) diseases. TSEs are a group of neurodegenerative diseases that include sporadic 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-sen, to an insoluble and partially protease-resistant form, PrP-res, is a key event in TSE pathogenesis and PrP is necessary for disease to occur. Using both in vitro and in vivo model systems, our laboratory studies the role of PrP-sen and PrP-res in several aspects of TSE pathogenesis, including: 1) the molecular pathogenesis of TSE species barriers and strains; 2) the mechanism of formation of amyloid and non-amyloid forms of PrP-res, especially with regard to familial TSE diseases; 3) the establishment of acute versus chronic TSE infection; and 4) the development of TSE vaccines and therapeutics.
Dr. Priola received her Ph.D. in microbiology and immunology in 1990 from the University of California, Los Angeles. In 1991, she joined the Rocky Mountain Laboratories where she is now a senior investigator. She is a former chair of the FDA TSE Advisory Committee and is currently chief of the TSE/Prion Molecular Biology Section. She currently serves on the editorial board of the journal Virology.
Moore RA, Sturdevant DE, Chesebro B, Priola SA. Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesis. J Proteome Res. 2014;13(11):4620-34.
Priola SA, Raines A, Caughey WS. Porphyrin and phthalocyanine antiscrapie compounds. Science. 2000;287(5457):1503-6.
Faris R, Moore RA, Ward A, Sturdevant DE, Priola SA. Mitochondrial Respiration Is Impaired during Late-Stage Hamster Prion Infection. J Virol. 2017;91(18).
Ward A, Hollister JR, Choi YP, Race B, Williams K, Shoup DW, Moore RA, Priola SA. Altered distribution, aggregation, and protease resistance of cellular prion protein following intracranial inoculation. PLoS One. 2019;14(7):e0219457.
Priola SA, Lawson VA. Glycosylation influences cross-species formation of protease-resistant prion protein. EMBO J. 2001;20(23):6692-9.
Related Scientific Focus Areas
Molecular Biology and Biochemistry
Microbiology and Infectious Diseases
This page was last updated on August 12th, 2019