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USDA, Agricultural Research Service, Animal Disease Research Unit, 337 Bustad Hall WSU, Pullman, WA 99164-7030, USA1
Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA 99164-7040, USA2
Colorado Division of Wildlife, 317 W. Prospect, Fort Collins, CO 80526, USA3
South Dakota Animal Industry Board, 411 S. Fort St, Pierre, SD 57501, USA4
Diagnostic Laboratories, College of Veterinary Medicine and Biomedical Sciences, Fort Collins, CO 80523, USA5
USDA, APHIS National Veterinary Services Laboratories, Ames, IA 50010, USA6
Elk Research Council, North American Elk Breeders' Association, 3901 Hwy 29, Alexandria, MN 56308, USA 7
Wyoming State Veterinary Laboratory, University of Wyoming, 1174 Snowy Range Road, Laramie, WY 82070, USA8
Author for correspondence: Katherine O'Rourke.Fax +1 509 335 8328. e-mail korourke{at}vetmed.wsu.edu
The PrP gene encodes the putative causative agent of the transmissible spongiform encephalopathies (TSEs), a heterogeneous group of fatal, neurodegenerative disorders including human Creutzfeldt–Jakob disease, bovine spongiform encephalopathy, ovine scrapie and chronic wasting disease (CWD) of North American deer and elk. Polymorphisms in the PrP gene are associated with variations in relative susceptibility, pathological lesion patterns, incubation times and clinical course of TSEs of humans, mice and sheep. Sequence analysis of the PrP gene from Rocky Mountain elk showed only one amino acid change (Met to Leu at cervid codon 132). Homozygosity for Met at the corresponding polymorphic site (Met to Val) in humans (human codon 129) predisposes exposed individuals to some forms of Creutzfeldt–Jakob disease. In this study, Rocky Mountain elk homozygous for PrP codon 132 Met were over-represented in both free- ranging and farm-raised CWD-affected elk when compared to unaffected control groups.
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