NR AOVK
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 International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - IV-31
PT Konferenz-Poster
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, conditions were tested to accomplish full degradation of prion protein PrP in brain stem tissue of animals suffering from bovine spongiform encephalopathy and scrapie. The detection of PrPsc - the disease associated isoform of PrP - in homogenates was performed by Western blotting and various antibodies. The results indicate that only in the presence of detergents heat pretreatment above 100° allows extensive enzymatic break down of PrPsc to a state where it is immunochemically undetectable. Proteinase K and two other subtilisin proteases, but not trypsin and pepsin were also effective. This enzymatic process promises the potential for development of a method for decontamination of medical and laboratory equipment. Ultimate effectiveness of this way of prion inactivation has to be tested in mouse bioassays.
AD
Jan P.M. Langeveld, G. Jan Garssen, Alex Bossers, Central Institute for Animal Disease Control (CIDC-Lelystad), Lelystad, The Netherlands; Jeng-Jie Wang, Giles C. Shih, BioResource International, Inc., Raleigh, NC 27606, USA; Dick F.M. van de Wiel, Animal Sciences Group (ASG), PO Box 65, 8200-AB, Lelystad, The Netherlands; Jason C.H. Shih, Department of Poultry Science, North Carolina State University, Raleigh, NC 27695-7608, USA
SP englisch
PO Deutschland