Suzette A. Priola, Ph.D.Bldg. 3, Room 3115903 S 4th StreetHamilton, MT 59840-2932Phone: 406-363-9319Fax: firstname.lastname@example.org
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 currently chief of the TSE/Prion Molecular Biology Section and serves on the editorial boards of both the Journal of Biological Chemistry and Virology.
Research in this laboratory focuses on the molecular basis of disease in the transmissible spongiform encephalopathies (TSEs). TSEs are a group of neurodegenerative diseases which include both sporadic and familial Creutzfeldt-Jakob disease (CJD) in humans, scrapie in sheep, chronic wasting disease (CWD) in deer and elk, and bovine spongiform encephalopathy (BSE).
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 PrP-res formation, especially in regard to familial TSE diseases; 3) the establishment of acute versus chronic TSE infection; and 4) the development of TSE vaccines and therapeutics.
Roger A. Moore, Ph.D., Postdoctoral IRTA Fellow; Kristin McNally, Ph.D., Postdoctoral IRTA Fellow; Christopher S. Greil, B.S., Graduate Student; Anne Ward, M.S., Biologist
(View list in PubMed.)
Moore RA, Hayes SF, Fischer ER, Priola SA. Amyloid formation via supramolecular peptide assemblies. Biochemistry. 2007 Jun 19;46(24):7079-87.
Moore RA, Herzog C, Errett J, Kocisko DA, Arnold KM, Hayes SF, Priola SA. Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation. Protein Sci. 2006 Mar;15(3):609-19.
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.
Vorberg I, Priola SA. Molecular basis of scrapie strain glycoform variation. J Biol Chem. 2002 Sep 7;277(39):36775-81.
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.
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Last Updated February 18, 2008