Major Areas of Research
- Prion diseases
- Molecular mechanisms of neurodegenerative diseases
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.
Roger A. Moore, Ph.D., Staff Scientist
Young Pyo Choi, Ph.D., Postdoctoral Visiting Fellow
Anne Ward, M.S., Biologist
Priola SA, Ward AE, McCall SL, Trifilo M, Choi YP, Solforosi L, Williamson RA, Cruite JT, Oldstone MBA. Lack of prion infectivity in fixed heart tissue from patients with Creutzfeldt-Jakob disease or amyloid heart disease. J Virol. 2013 Sep;87(17):9501-10.
Moore RA, Timmes A, Wilmarth PA, Priola SA. Comparative profiling of highly enriched 22L and Chandler mouse scrapie prion protein preparations. Proteomics. 2010 Aug;10(15):2858-69.
Moore RA, Hayes SF, Fischer ER, Priola SA. Amyloid formation via supramolecular peptide assemblies. Biochemistry. 2007 Jun 19;46(24):7079-87.
Vorberg I, Raines A, Priola SA. Acute formation of protease-resistant prion protein does not always lead to persistent scrapie infection in vitro. J Biol Chem. 2004 Jul 9;279(28):29218-25.
Priola SA, Lawson VA. Glycosylation influences cross-species formation of protease-resistant prion protein. EMBO J. 2001 Dec 3;20(23):6692-9.
Priola SA, Raines A, Caughey WS. Porphyrin and phthalocyanine antiscrapie compounds. Science. 2000 Feb 25;287(5457):1503-6
Chesebro BW, Caughey BW, Chabry J, Priola S, inventors; The United States of America as represented by the Department of Health and Human Services, assignee. Inhibitors of formation of protease resistant prion protein. United States patent US 6,355,610. 12 Mar 2002.
Chesebro BW, Caughey BW, Chabry J, Priola S, inventors; The United States of America as represented by the Department of Health and Human Services, assignee. Inhibitors of formation of protease resistant prion protein. United States patent US 6,211,149. 3 Apr 2001.