Transmission of iatrogenic prion disease has occurred from contaminated neurosurgical tools, transplant materials, and occupational exposure to prion-contaminated laboratory tools. Prions cause disease by the templated misfolding of the normal cellular form of the prion protein, PrP, into the misfolded and pathogenic form PrP and are invariably fatal. Reducing iatrogenic and occupational prion transmission is challenging. First, prions can bind to and persist on surfaces for long periods of time. Second, prions are highly resistant to inactivation. Given this, surfaces can retain infectivity for long periods of time following ineffective decontamination. Not only can this pose a potential occupational risk for prion laboratory workers, but it could potentially cross-contaminate laboratory experiments utilizing sensitive prion amplification techniques. The protocol described here for a prion safety laboratory swipe test includes steps for the identification and documentation of high-traffic laboratory areas, recommended swabbing controls to ensure the validity of results, steps to identify proper responses to positive surface swabbing sites, representative results from prion swipe testing, as well as potential artifactual results. Overall, the prion safety laboratory swipe test can be implemented as part of a broader prion safety program to assess decontamination of surfaces, monitor common spaces for prion contamination, and implement the documentation of prion decontamination status.
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http://dx.doi.org/10.3791/67889 | DOI Listing |
J Vis Exp
February 2025
Department of Medical Microbiology and Immunology, School of Medicine, Creighton University;
Transmission of iatrogenic prion disease has occurred from contaminated neurosurgical tools, transplant materials, and occupational exposure to prion-contaminated laboratory tools. Prions cause disease by the templated misfolding of the normal cellular form of the prion protein, PrP, into the misfolded and pathogenic form PrP and are invariably fatal. Reducing iatrogenic and occupational prion transmission is challenging.
View Article and Find Full Text PDFCureus
January 2025
Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, JPN.
Prion diseases are fatal neurodegenerative disorders. Previous studies have indicated the presence of "prion carriers" who remain asymptomatic, but scrapie prion protein (PrP) has begun to accumulate in the brain. Indeed, we identified an undiagnosed case of prion disease in a cadaver used for the anatomical practice of medical students.
View Article and Find Full Text PDFLife Sci
April 2025
National Key Laboratory of Veterinary Public Health and Safety, Key Laboratory of Animal Epidemiology of the Ministry of Agriculture and Rural Affairs, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing, China. Electronic address:
Prion diseases are neurodegenerative diseases that are transmitted between humans and animals, which cause spongiform brain degeneration and neuronal death. Prion diseases are difficult to treat. Mitochondrial damage and oxidative stress occurring early in disease progression.
View Article and Find Full Text PDFNeurology
April 2024
Neurosciences.
Objective: NA.
Background: Creutzfeldt-Jakob disease (CJD) is a rapidly progressive, fatal brain disease. Sporadic CJD (sCJD) is the most common subtype without genetic cause.
Cell Death Dis
February 2025
National Key Laboratory of Veterinary Public Health and Safety, Key Laboratory of Animal Epidemiology of the Ministry of Agriculture and Rural Affairs, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing, China.
Prion diseases are a group of fatal neurodegenerative disorders characterized by the abnormal folding of cellular prion proteins into pathogenic forms. The development of these diseases is intricately linked to oxidative stress and mitochondrial dysfunction. Irisin, an endogenous myokine, has demonstrated considerable neuroprotective potential due to its antioxidative properties.
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