Abstract
To date, there have been no studies on the sterilization of prions by non-concentrated and concentrated vaporized hydrogen peroxide (VHP) applied by the same instrument. Here, the effect of the two types of VHP applied using an ES-700 sterilizer on prions was investigated. Brain homogenate from scrapie (Chandler) prion-infected mice was spotted on a cover glass and subjected to ES-700 treatment in soft (non-concentrated VHP from 59% hydrogen peroxide) or standard (concentrated VHP from 80% hydrogen peroxide) mode. Proteinase K-resistant prion protein (PrPres), an indicator of the abnormal isoform of prion protein (PrPSc), was reduced by ES-700 treatment under several conditions: SFT1/4 (soft mode, quarter cycle), SFT1/2 (soft mode, half cycle), SFT1 (soft mode, full cycle), and STD1/2 (standard mode, half cycle). PrPres was detected after the first and second rounds of protein misfolding cyclic amplification (PMCA) of untreated samples, but was undetectable in SFT1/4, SFT1/2, SFT1, and STD1/2 treated samples. In a mouse bioassay, SFT1/2 and STD1/2 treatment of prions significantly prolonged survival time, suggesting that prion infectivity is reduced after ES-700 treatment. In summary, both non-concentrated and concentrated VHP inactivate prions and may be useful for the low-temperature sterilization of prion-contaminated medical devices.
Highlights
Prion diseases are a group of progressive and fatal neurodegenerative disorders caused by a proteinaceous infectious prion that can affect both humans and animals
Samples of prion (Chandler)-infected mouse brain homogenate were subjected to ES-700 treatment, followed by proteinase K (PK) treatment and Western blotting using an anti-PrP antibody (SAF83) (Figure 1)
A strong band corresponding to PrPres, which was resistant to PK digestion, was readily detected in the untreated (Control) sample
Summary
Prion diseases are a group of progressive and fatal neurodegenerative disorders caused by a proteinaceous infectious prion that can affect both humans and animals. The major component of the pathogen is the abnormal isoform of the prion protein (PrPSc ) [1]. Human prion diseases may be caused by infection (e.g., Kuru disease and iatrogenic Creutzfeldt–Jakob disease (CJD)) or inheritance (e.g., Gerstmann-Sträussler-Scheinker syndrome (GSS), familial CJD, and fatal familial insomnia (FFI)), but most types of human prion disease (85–90%) are of unknown origin and are referred to as sporadic. All types of prion disease are transmissible [1,2]. Representative animal prion diseases include scrapie in sheep and goat, bovine spongiform encephalopathy (BSE) in cattle, and chronic wasting disease (CWD) in cervids. When individuals and animals are infected with prions, the cellular isoform of prion protein
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