NR AWPW
AU VerCauteren,K.C.; Nash,P.B.; Pilon,J.L.; Arver,T.A.; Hoglund,D.; Ernst,S.
TI Potential of enzymatic digestion for decontaminating infectious prions
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions SA-14
PT Konferenz-Poster
AB Infectious prions (PrPres) are problematic for decontamination efforts because they are resistant to standard disinfection methods. Decontamination methods currently recommended (i.e., bleach, autoclaving, NaOH) can be damaging to materials, caustic to personnel, and are not possible in many situations. Improved and more versatile disinfection methods are needed. Enzymatic digestion is a potential means to decontaminate prions. Though PrPres is protease resistant, there are proteases with different specificities and conditions for activity. We used a scrapie mouse model to evaluate the effects of two proteases with digesting activity that eliminated in vitro (ELISA and Western blot) detectability of chronic wasting disease prions. At 34 weeks after inoculation, no mice inoculated with untreated prion-positive brain were alive while 81% and 48% of mice inoculated with brain treated with the proteases were alive. No mice inoculated with bleach-treated or autoclaved prion-positive brain died. Results suggest that enzymatic digestion with either of the enzymes can decrease infectivity. Suboptimal conditions may account for these treatments not being as effective as standard bleach and autoclaving decontamination, but the protection afforded provides support for the concept of successful enzymatic decontamination. Further evaluation of digestion under improved conditions should yield more successful decontamination that will allow for more practical treatment of waste, instruments, and surfaces; make environmental decontamination feasible; and provide a method for treating some organic materials. These improvements would greatly facilitate management of prion diseases in a variety of settings.
AD K.C. VerCauteren, P.B. Nash, J.L. Pilon: United States Department of Agriculture, Animal and Plant Health Inspection Service, Wildlife Services, National Wildlife Research Center, Fort Collins, Colorado, USA; T.A. Arver, D. Hoglund: Prion Tech, Raleigh, North Carolina, USA; S. Ernst: Novozymes A/S, Bagsvaerd, Denmark
SP englisch
PO Italien