Abstract
Transmissible spongiform encephalopathies such as scrapie in sheep and goats, Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in cattle, are neurodegenerative disorders. A proposed causative agent for these diseases is an infectious protein, the so called 'prion'. An abnormal isoform of prion protein (PrPSc) can be detected according to the prion propagation method used. As PrPSc appears to constitute the main, if not the only, infectious entity its detection for the diagnosis of prion diseases is important. Immunodetection methods for PrPSc analysis are popular tools for diagnosis and research studies. In this paper, a review of the present knowledge concerning immunodetection is presented and the enhancement of the immunoreactivity of antisera to mouse and hamster prion protein peptides using the techniques of Western blotting and immunohistochemistry is summarized.
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