Accumulation of prion protein (PrPSc) in the central nervous system is the hallmark of transmissible spongiform encephalopathies. However, in some of these diseases such as scrapie or chronic wasting disease, the PrPSc can also accumulate in other tissues, particularly in the lymphoreticular system. In recent years, PrPSc in organs other than nervous and lymphoid have been described, suggesting that distribution of this protein in affected individuals may be much larger than previously thought. In the present study, 11 non-nervous/non-lymphoid organs from 16 naturally scrapie infected sheep in advanced stages of the disease were examined for the presence of PrPSc. Fourteen infected sheep were of the ARQ/ARQ PRNP genotype and 2 of the VRQ/VRQ, where the letters A, R, Q, and V represent the codes for amino-acids alanine, arginine, glutamine and valine, respectively. Adrenal gland, pancreas, heart, skin, urinary bladder and mammary gland were positive for PrPSc by immunohistochemistry and IDEXX HerdChek scrapie/BSE Antigen EIA Test in at least one animal. Lung, liver, kidney and skeletal muscle exhibited PrPSc deposits by immunohistochemistry only. To our knowledge, this is the first report regarding the presence of PrPSc in the heart, pancreas and urinary bladder in naturally acquired scrapie infections. In some other organs examined, in which PrPSc had been previously detected, PrPSc immunolabeling was observed to be associated with new structures within those organs. The results of the present study illustrate a wide dissemination of PrPSc in both ARQ/ARQ and VRQ/VRQ infected sheep, even when the involvement of the lymphoreticular system is scarce or absent, thus highlighting the role of the peripheral nervous system in the spread of PrPSc.
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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0097768 | PLOS |
Front Mol Neurosci
December 2024
Laboratory of Veterinary Hygiene, Faculty of Veterinary Medicine, Graduate School of Infectious Diseases, Hokkaido University, Sapporo, Japan.
The accumulation of a disease-specific isoform of prion protein (PrP) and histopathological lesions, such as neuronal loss, are unevenly distributed in the brains of humans and animals affected with prion diseases. This distribution varies depending on the diseases and/or the combinations of prion strain and experimental animal. The brain region-dependent distribution of PrP and neuropathological lesions suggests a neuronal cell-type-dependent prion propagation and vulnerability to prion infection.
View Article and Find Full Text PDFiScience
December 2024
Université Paris-Saclay, INRAe, UVSQ, VIM, 78350 Jouy-en-Josas, France.
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are neurodegenerative disorders caused by the accumulation of misfolded conformers (PrP) of the cellular prion protein (PrP). During the pathogenesis, the PrP seeds disseminate in the central nervous system and convert PrP leading to the formation of insoluble assemblies. As for conventional infectious diseases, variations in the clinical manifestation define a specific prion strain which correspond to different PrP structures.
View Article and Find Full Text PDFAnimals (Basel)
November 2024
Korea Zoonosis Research Institute, Jeonbuk National University, 820-120 Hana-ro, Iksan 54531, Republic of Korea.
Prion diseases are fatal neurodegenerative disorders caused by the misfolding of the normal cellular prion protein (PrP) into its infectious isoform (PrP). Although prion diseases in humans, sheep, goats, and cattle have been extensively studied, feline spongiform encephalopathy (FSE) remains poorly understood. Genetic factors, particularly polymorphisms in the prion protein gene () and protein gene (), have been linked to prion disease susceptibility in various species.
View Article and Find Full Text PDFFront Vet Sci
November 2024
Department of Biological Sciences, Andong National University, Andong, Republic of Korea.
Background: Prion diseases are irreversible infectious neurodegenerative diseases caused by a contagious form of prion protein (PrP). Since chronic wasting disease (CWD)-infected white-tailed deer are strong carriers of the prion seed through corpses via scavenger animals, preemptive control based on genetic information for a culling system is necessary. However, the risk of CWD-related genetic variants has not been fully evaluated.
View Article and Find Full Text PDFBiomed Environ Sci
November 2024
National Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, NHC Key Laboratory for Medical Virology and Viral Diseases, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 102206, China;Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Zhejiang University, Hangzhou 100084, Zhejiang, China;Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan 430071, Hubei, China;China Academy of Chinese Medical Sciences, Beijing 100700, China;Shanghai Institute of Infectious Disease and Biosafety, Shanghai 200003, China.
Objective: To analyze the relationship between Chemokine IP10 and its receptor CXCR3 during prion infection.
Methods: We investigated the increases in IP10 signals, primarily localized in neurons within the brains of scrapie-infected mice, using western blotting, ELISA, co-immunoprecipitation, immunohistochemistry, immunofluorescence assays, and RT-PCR.
Results: Both CXCR3 levels and activation were significantly higher in the brains of scrapie-infected mice and prion-infected SMB-S15 cells.
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