Natural scrapie, a degenerative disease affecting the central nervous system of domestic sheep, and less commonly of domestic goats, has been known for over two hundred years in Great Britain and other countries in Europe. Research on this progressive and invariably fatal neurological disorder began in the 19th Century, and theories on the cause and the mode of transmission of the disease have been debated for many years (14, 15). According to Prusiner et al. (38, 39), the scrapie agent is an infectious protein, i.e. an abnormal form of a host-encoded protein, prion protein (PrP), which accumulates in the central nervous system of affected animals (PrP for prionproteinaceous infectious particle-protein). Investigations on natural and experimentally induced scrapie in sheep have shown that genetic susceptibility to the disease is modulated by at least three different codons (136, 154, 171) of the sheep PrP gene. Studies reported so far on the PrP genotypes relevant to the scrapie susceptibility status reveal the resistance of homozygous ARR/ARR (ARR: alanine, arginine, arginine) animals and the high liability to disease of VRQ/VRQ (VRQ: valine, arginine, glutamine) and VRQ/ARQ (ARQ: alanine, arginine, glutamine) animals in scrapie-affected flocks (47). However, a new disease, referred to as bovine spongiform encephalopathy (BSE), emerged in the mid-1980s in the United Kingdom (UK), and the first case of BSE was confirmed in November 1986 on the basis of histopathological examination of affected brains (57). Rapidly, BSE was recognised as being a new member of the scrapie-like family of neurodegenerative diseases. This finding provided new impetus