Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study

M.P. Polak, J.F. Zmudzinski, J.G. Jacobs, J.P.M. Langeveld

    Research output: Contribution to journalArticleAcademicpeer-review

    33 Citations (Scopus)

    Abstract

    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 (M-r) 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 M-r 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.
    Original languageEnglish
    Pages (from-to)69-79
    Number of pages11
    JournalArchives of Virology
    Volume153
    Issue number1
    DOIs
    Publication statusPublished - 2008

    Keywords

    • creutzfeldt-jakob-disease
    • natural sheep scrapie
    • prion protein
    • strain variation
    • bse
    • identification
    • agent
    • mice
    • discrimination
    • transmission

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