NR APJD
AU 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.
TI Enzymatic degradation of prion protein in brain stem from infected cattle and sheep
QU Journal of Infectious Diseases 2003 Dec 1; 188(11): 1782-9
PT journal article
AB 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 degrees 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.
MH Animals; Brain Stem/*metabolism; Cattle; Decontamination; Peptide Hydrolases/metabolism; Prion Diseases/*metabolism; Prions/*metabolism; Protein Denaturation; Sheep; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Temperature
AD Division of Infectious Diseases and Food Chain Quality, Institute for Animal Science and Health, Lelystad, The Netherlands. jan.langeveld@wur.nl.
SP englisch
PO USA