Ovine scrapie and cervid chronic wasting disease can be transmitted in the absence of animal-to-animal contact, and environmental reservoirs of infectivity have been implicated in their spread and persistence. Investigating environmental factors that influence the interaction of disease-associated PrP with soils is imperative to understanding what is likely to be the complex role of soil in disease transmission. Here, we describe the effects of soil temperature on the binding/desorption and persistence of both ovine scrapie- and bovine BSE-PrP (TSE) . Binding of PrP (TSE) to a sandy loam soil at temperatures of 4°C, 8-12°C and 25-30°C demonstrated that an increase in temperature resulted in (1) a decrease in the amount of PrP (TSE) recovered after 24 h of interaction with soil, (2) an increase in the amount of N-terminal cleavage of the prion protein over 11 d and (3) a decrease in the persistence of PrP (TSE) on soil over an 18 mo period.
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http://dx.doi.org/10.4161/pri.20025 | DOI Listing |
Pathogens
November 2024
Virus and Prion Research Unit, National Animal Disease Center, Agricultural Research Service, United States Department of Agriculture, Ames, IA 50010, USA.
Cornea
September 2024
3rd Faculty of Medicine, Charles University, Prague, Czech Republic.
Purpose: The purpose of this study was to assess the effectiveness of legally mandated testing for pathogenic prion proteins in corneal tissue donors in the Czech Republic, considering its impact on safety, financial, and temporal costs.
Methods: Between January 2007 and December 2023, standardized brain regions were collected from all corneal tissue donors in the Czech Republic. Tissue samples were tested for the presence of pathogenic prion proteins by the Czech Reference Laboratory for Human Prion Diseases.
BMC Res Notes
September 2024
Virus and Prion Research Unit, National Animal Disease Center, USDA-ARS, 1920 Dayton Ave., Ames, IA, 50010, USA.
Pathogens
July 2024
Friedrich-Loeffler-Institut, 17493 Greifswald-Isle of Riems, Germany.
After the detection of bovine spongiform encephalopathy (BSE), and a zoonotic transmissible spongiform encephalopathy (TSE) caused by the pathological prion protein (PrP) in two goats, the investigation of goat prions became of greater interest. Therefore, a broad collection of European goat TSE isolates, including atypical scrapie, CH1641 and goat BSE as reference prion strains were biochemically characterised and subsequently inoculated into seven rodent models for further analysis (already published results of this comprehensive study are reviewed here for comparative reasons). We report here the histopathological and immunohistochemical data of this goat TSE panel, obtained after the first passage in Tgshp IX (tg-shARQ) mice, which overexpress the ovine prion protein.
View Article and Find Full Text PDFBiochem Biophys Res Commun
December 2023
Institute of Immunology and Microbiology, First Faculty of Medicine, Charles University, 128 00, Prague, Czech Republic. Electronic address:
Prions are responsible for a number of lethal neurodegenerative and transmissible diseases in humans and animals. Extracellular vesicles, especially small exosomes, have been extensively studied in connection with various diseases. In contrast, larger microvesicles are often overlooked.
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