Author
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Miller, Janice |
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Submitted to: Conference on Emerging Diseases Veterinary Medicine University of Georgia
Publication Type: Abstract Only Publication Acceptance Date: 8/13/1999 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Spongiform encephalopathies are fatal, transmissible diseases of the central nervous system that were initially recognized on the basis of characteristic clinical signs and histopathologic changes. In 1982, Dr. Stanley Prusiner reported that these diseases are caused by a conformationally altered normal cellular protein (prion protein or PrP). To appreciate spongiform encephalopathies, it is necessary to understand their origin and modes of transmission. In human beings, we have examples of the 3 ways in which a prion disease can be initiated. The first example is familial disease, caused by an inherited mutation in the prion gene. The second category, acquired, includes kuru, a disease associated with ritualistic cannabilism,iatrogenic transmissions, and variant Creutzfeld-Jacob Disease (CJD), which apparently has resulted from exposure to bovine spongiform encephalopathy (BSE). The third type of prion disease is sporadic, a designation given to cases without recognized prion gene mutations or exposure to contaminated materials. Based on the information from human beings, it seems likely that prion diseases in other animals could be initiated through the same 3 mechanisms. Fortunately, the non-human spongiform encephalopathies that have been recognized, i.e., scrapie in sheep, BSE in ruminants and cats, transmissible mink encephalopathy (TSE), and chronic wasting disease (CWD) in deer and elk, are acquired prion diseases, thus providing an opportunity for development of control methods. However, we should remember that any animal species might have unrecognized familial or sporadic forms of prion disease that could develop into an acquired disease due to natural transmission or artificial (man-made) interventions. |
