Transmissible spongiform encephalopathies (TSEs), or prions, are neurodegenerative diseases that affect a variety of animal species, including humans. Cruetzfeldt-Jakob disease (CJD) in humans, sheep and goat scrapie, chronic wasting disease (CWD) of cervids, and transmissible mink encephalopathy (TME) of mink are classified as TSEs. According to the "protein-only" hypothesis (Prusiner, 1982),1 prions are devoid of nucleic acids and consist of assemblies of misfolded host-encoded normal protein, the prion protein (PrPC). Prion propagation is thought to occur by a templating mechanism during which PrPC is recruited, converted to a disease-associated isoform (PrPD), and assembled onto the growing amyloid fibril. This fibular assembly is infectious, with ability to initiate disease processes similar to other pathogenic agents. Evidence indicates that scrapie, CWD, and TME disease processes follow this rule.