TSE/Prion Molecular Biology Section
Suzette A. Priola, Ph.D.
Chief, TSE/Prion Molecular Biology Section
Deputy Chief, Laboratory of Neurological Infections and Immunity
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Major Areas of Research
- Prion diseases
- Molecular mechanisms of neurodegenerative diseases
Program Description
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, PrPC, to an insoluble and partially protease-resistant form, PrPSc, is a key event in prion pathogenesis, and PrPC is required for prion infection and disease to occur. Using both in vitro and in vivo model systems, our laboratory studies the role of PrPC and PrPSc 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; 2) the contribution of mitochondria to prion pathogenesis; and 4) the development of prion vaccines and therapeutics.
Biography
Education
Ph.D., 1990, University of California, Los Angeles
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 Deputy Chief of the Laboratory of Neurological Infections and Immunity and Chief of the TSE/Prion Molecular Biology Section.
Selected Publications
Ward A, Jessop F, Faris R, Shoup D, Bosio CM, Peterson KE, Priola SA. Lack of the immune adaptor molecule SARM1 accelerates disease in prion infected mice and is associated with increased mitochondrial respiration and decreased expression of NRF2. PLoS One. 2022 May 4;17(5):e0267720.
Shoup D, Priola SA. The Size and Stability of Infectious Prion Aggregates Fluctuate Dynamically during Cellular Uptake and Disaggregation. Biochemistry. 2021 Feb 9;60(5):398-411.
Ward A, Hollister JR, McNally K, Ritchie DL, Zanusso G, Priola SA. Transmission characteristics of heterozygous cases of Creutzfeldt-Jakob disease with variable abnormal prion protein allotypes. Acta Neuropathol Commun. 2020 Jun 9;8(1):83.
Faris R, Moore RA, Ward A, Race B, Dorward DW, Hollister JR, Fischer ER, Priola SA. Cellular prion protein is present in mitochondria of healthy mice. Sci Rep. 2017 Feb 2;7:41556.
Moore RA, Head MW, Ironside JW, Ritchie DL, Zanusso G, Choi YP, Priola SA. The Distribution of Prion Protein Allotypes Differs Between Sporadic and Iatrogenic Creutzfeldt-Jakob Disease Patients. PLoS Pathog. 2016 Feb 3;12(2):e1005416.
Choi YP, Head MW, Ironside JW, Priola SA. Uptake and degradation of protease-sensitive and -resistant forms of abnormal human prion protein aggregates by human astrocytes. Am J Pathol. 2014 Dec;184(12):3299-307.
Patents
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.
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Research Group
Research focuses on molecular basis of disease in transmissible spongiform encephalopathy or prion diseases. Our lab studies the role of PrPC and PrPSc in prion pathogenesis: 1) molecular pathogenesis of prion species barriers and strains; 2) establishment of acute vs. chronic prion infection; 3) contribution of mitochondria to prion pathogenesis; 4) development of prion vaccines and therapeutics.