The aim of this study is to investigate the profile of ovine PrP gene by amino acid polymorphism at codons 136, 141, 154, and 171 for determining the genetic predisposition to the Scrapie disease for the tribal sheep and rams, with different numbers and distribution in Bulgaria.
Scrapie infection stimulated Gpc-1 autoprocessing and the generated HS degradation products colocalized with intracellular aggregates of the disease-related scrapie prion protein isoform (PrP(Sc)).
Cerebral and cardiac amyloid deposits have been reported after scrapie infection in transgenic mice expressing variant prion protein (PrP(C)) lacking the glycophosphatidylinositol anchor.
The complex relationships between PrP genotype and the survival of sheep subjected to scrapie infection are now being investigated in terms of the different structure of the PrP protein molecules produced by each allele.
All of the findings with different PrP constructs plus the absence of scrapie pathology in PrP null mice are the strongest argument that the prion protein is the main etiologic and pathogenic factor of prion disorders.
Transgenic mouse studies are emphasized which verify that genetic forms of TSEs are linked to mutations in the host PrP gene and that the host species barrier to scrapie infection, scrapie incubation time and the distribution of neuropathology, which define scrapie prion isolates ('strains'), are determined by the structure of PrP.