Abstract
Prion disorders, or transmissible spongiform encephalophaties (TSE), are fatal neurodegenerative diseases affecting mammals. Prion-infectious particles comprise of misfolded pathological prion proteins (PrPTSE). Different TSEs are associated with distinct PrPTSE folds called prion strains. The high resistance of prions to conventional sterilization increases the risk of prion transmission in medical, veterinary and food industry practices. Recently, we have demonstrated the ability of disulfonated hydroxyaluminum phthalocyanine to photodynamically inactivate mouse RML prions by generated singlet oxygen. Herein, we studied the efficiency of three phthalocyanine derivatives in photodynamic treatment of seven mouse adapted prion strains originating from sheep, human, and cow species. We report the different susceptibilities of the strains to photodynamic oxidative elimination of PrPTSE epitopes: RML, A139, Fu-1 > mBSE, mvCJD > ME7, 22L. The efficiency of the phthalocyanine derivatives in the epitope elimination also differed (AlPcOH(SO3)2 > ZnPc(SO3)1-3 > SiPc(OH)2(SO3)1-3) and was not correlated to the yields of generated singlet oxygen. Our data suggest that the structural properties of both the phthalocyanine and the PrPTSE strain may affect the effectiveness of the photodynamic prion inactivation. Our finding provides a new option for the discrimination of prion strains and highlights the necessity of utilizing range of prion strains when validating the photodynamic prion decontamination procedures.
Highlights
Prion disorders, known as transmissible spongiform encephalopathies (TSE), represent a group of fatal neurodegenerative diseases affecting man and several other mammalian species
TSE can differ in the length of preclinical phase, clinical signs, speed of progression, location of brain lesions and in biochemical properties of accumulated pathological PrPTSE [1]
Most of the patterns seem to be explained by the existence of so-called prion strains represented by distinct self-propagating PrPTSE conformations [2]
Summary
Known as transmissible spongiform encephalopathies (TSE), represent a group of fatal neurodegenerative diseases affecting man and several other mammalian species. Most of the patterns seem to be explained by the existence of so-called prion strains represented by distinct self-propagating PrPTSE conformations [2]. The World Health Organization recommends the immersion of contaminated instruments in 1 M NaOH or 2% NaOCl for 1 h, followed by autoclaving at 134 ◦ C for 1 h and subsequent routine sterilization. Such harsh treatment is not appropriate for various medical instruments, and several less-damaging procedures have been studied, some with encouraging results [4,5]. Prion strains notably differ in their resistance to inactivation. The hamster Sc237 strain was shown to be five orders of magnitude more sensitive to acidic SDS treatment than human CJD prions [6]
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