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Abstract
Prions are comprised principally of aggregates of a misfolded host protein and cause fatal transmissible neurodegenerative disorders of mammals, such as variant Creutzfeldt–Jakob disease in humans and bovine spongiform encephalopathy in cattle. Prions pose significant public health concerns through contamination of blood products and surgical instruments, and can resist conventional hospital sterilization methods. Prion infectivity binds avidly to surgical steel and can efficiently transfer infectivity to a suitable host, and much research has been performed to achieve effective prion decontamination of metal surfaces. Here, we exploit the highly sensitive Standard Steel-Binding Assay (SSBA) to perform a direct comparison of a variety of commercially available decontamination reagents marketed for the removal of prions, alongside conventional sterilization methods. We demonstrate that the efficacy of marketed prion decontamination reagents is highly variable and that the SSBA is able to rapidly evaluate current and future decontamination reagents.
Highlights
Transmissible spongiform encephalopathies or prion diseases are a closely related group of fatal neurodegenerative disorders that affect the central nervous system (CNS) of mammals
While RML prions seem highly suitable as a model strain on this basis, it is important when considering efficacy of decontamination reagents involving proteolysis to ensure that the disease-associated PrP is not unusually protease sensitive when compared to variant CJD (vCJD) prions
It was observed that disease-associated PrP from both RML and vCJD prion-infected brain homogenates were degraded at two distinct rates by proteinase K (PK), indicating the presence of at least two distinct subpopulations of protease-resistant material
Summary
Transmissible spongiform encephalopathies or prion diseases are a closely related group of fatal neurodegenerative disorders that affect the central nervous system (CNS) of mammals. They include Creutzfeldt–Jakob disease (CJD), Gerstmann– Straussler–Scheinker disease, fatal familial insomnia and kuru in humans, bovine spongiform encephalopathy (BSE) in cattle and scrapie in sheep. Prions can be generated sporadically, as a result of an as yet uncharacterized stochastic event causing PrPC to PrPSc conversion, or by dominant mutations in the gene encoding PrP (PRNP in humans), producing mutant PrPC that is hypothesized to more readily undergo spontaneous conversion to PrPSc. uniquely among neurodegenerative disorders, prion disease can be caused through infection with exogenous prions; the latter inducing host-encoded PrPC to undergo conformational change, via seeding or template-directed refolding and replication and spread (reviewed by Collinge & Clarke, 2007)
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