Enzymatic degradation of prion protein in brain stem from infected cattle and sheep

J.P.M. Langeveld, J.J. Wang, D.F.M. van de Wiel, G.C. Shih, G.J. Garssen, A. Bossers, J.C.H. Shih

    Research output: Contribution to journalArticleAcademicpeer-review

    123 Citations (Scopus)


    Prions¿infectious agents involved in transmissible spongiform encephalopathies¿normally survive proteolytic and mild protein-destructive processes. Using bacterial keratinase produced by Bacillus licheniformis strain PWD-1, we tested conditions to accomplish the full degradation of prion protein (PrP) in brain-stem tissue from animals with bovine spongiform encephalopathy and scrapie. The detection of PrPSc, the disease-associated isoform of PrP, in homogenates was done by Western blotting and various antibodies. The results indicated that only in the presence of detergents did heat pretreatment at >100°C allow the extensive enzymatic breakdown of PrPSc to a state where it is immunochemically undetectable. Proteinase K and 2 other subtilisin proteases, but not trypsin and pepsin, were also effective. This enzymatic process could lead to the development of a method for the decontamination of medical and laboratory equipment. The ultimate effectiveness of this method of prion inactivation has to be tested in mouse bioassays.
    Original languageEnglish
    Pages (from-to)1782-1789
    JournalThe Journal of Infectious Diseases
    Issue number11
    Publication statusPublished - 2003


    • bovine spongiform encephalopathy
    • scrapie prion
    • rendering procedures
    • prp 27-30
    • agent
    • inactivation
    • bse
    • infectivity
    • transmission
    • keratinase

    Fingerprint Dive into the research topics of 'Enzymatic degradation of prion protein in brain stem from infected cattle and sheep'. Together they form a unique fingerprint.

    Cite this