Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study
2008
Polak, M. P. | Zmudzinski, J. F. | Jacobs, J. G. | Langeveld, J. P. M.
The aim of this study was to analyze molecular features of protease-resistant prion protein (PrPʳᵉˢ) in Western blots of BSE cases diagnosed in Poland with respect to a possible atypical status. Confirmed cases were analyzed by Western blotting with several monoclonal antibodies directed at N-terminal and core epitopes of prion protein (PrP). Most cases showed the classical glycoprofile characterized by the dominance of the di- over the monoglycosylated PrPʳᵉˢ band, yielding di-/mono- ratios well above 2 and by reactivity with antibodies having their epitopes in bovine PrP region 110–242 (C-type cases). Surprisingly, seven cases of BSE were atypical. Six were classified as L-type based on a slightly lower molecular mass (Mᵣ) of the non- glycosylated band with respect to C-types and a conspicuously low di-/mono- ratio of glycosylated PrPʳᵉˢ bands approaching unity. One case was classified as H-type because of a higher Mᵣ of PrPʳᵉˢ bands on the blot when compared with C-type cases. A characteristic epitope of H-type PrPʳᵉˢ occurred in the 101–110 region of PrP for which only antibody 12B2 had a sufficient affinity. The occurrence of atypical cases only in animals 9 years of age and older raises questions about the mechanisms of prion diseases and the origin of BSE.
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