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.
- bovine spongiform encephalopathy
- scrapie prion
- rendering procedures
- prp 27-30
Langeveld, J. P. M., Wang, J. J., van de Wiel, D. F. M., Shih, G. C., Garssen, G. J., Bossers, A., & Shih, J. C. H. (2003). Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. The Journal of Infectious Diseases, 188(11), 1782-1789. https://doi.org/10.1086/379664