Richard E. Race, D.V.M.
Chief, Veterinary Biology Unit
Senior Investigator
Veterinary Biology Unit
Dr. Race received his B.S. and D.V.M. degrees from Colorado State University. After short assignments with the federal government in the Division of Air Pollution, Division of Radiological Health and Animal Blood Donor Program, he began work with Dr. William Hadlow at RML in 1970. He is currently a senior investigator.
Description of Research Program
Agents that cause fatal spongiform encephalopathies of animals and humans are unique and have not been well characterized. Scrapie of sheep, bovine spongiform encephalopathy of cattle ("mad cow disease") and Creutzfeldt-Jacob disease of humans are the best characterized of these transmissible spongiform encephalopathies (TSEs).
Experimental evidence suggests that the proteinase K-resistant form of an endogenous protein designated "prion protein" is important to disease pathogenesis. We are determining the role of prion protein in the pathogenesis of TSEs. Animal and cell culture systems, including several transgenic mouse models, are being used. Biochemical, molecular, genetic, and biological approaches are all utilized.
Research Group Members
Brent Race, D.V.M.; Kimberly Meade-White, M.S., Biologist
Selected Recent Publications
Chesebro B, Trifilo M, Race R, Meade-White K, Teng C, LaCasse R, Raymond L, Favara C, Baron G, Priola S, Caughey B, Masliah E, Oldstone M. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science. 2005. 308: 1435-9.
Race RE. Crossing the species barrier. Nature 2003. 423: 118-119.
Race R, Meade-White K, Raines A, Raymond GJ, Caughey B, Chesebro B. Subclinical scrapie infection in a resistant species: persistence, replication, and adaptation of infectivity during four passages. J Infect Dis. 2002. 186 Supp 2: S166-S170.
Race R, Raines A, Raymond GJ, Caughey B, Chesebro B. Long-term subclinical carrier state precedes scrapie replication and adaptation in a resistant species: analogies to bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease in humans. J Virol. 2001. 75: 10106-10112.
Race R, Oldstone M, Chesebro B. Entry versus blockade of brain infection following oral or intraperitoneal scrapie administration: role of prion protein expression in peripheral nerves and spleen. J Vitol. 2000. 74: 828-33.
Race R, Chesebro B. Scrapie infectivity found in resistant species. Nature. 1998. 392(6678): 770.
Race R, Jenny A, Sutton D. Scrapie infectivity and proteinase K-resistant prion protein in sheep placenta, brain, spleen, and lymph node: implications for transmission and antemortem diagnosis. J infect Dis. 1998. 178: 949-53.
Race R, Priola SA, Bessen RA, Ernst DR, Dockter J, Rall GF, Mucke L, Chesebro B, Oldstone MBA. Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron. 1995. 15: 1183-1191.
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