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Journal articles on the topic 'Prion, copper, Transmissible spongiform encephalopathy'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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1

Nishida, Yuzo. "Elucidation of Endemic Neurodegenerative Diseases - a Commentary." Zeitschrift für Naturforschung C 58, no. 9-10 (2003): 752–58. http://dx.doi.org/10.1515/znc-2003-9-1028.

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AbstractRecent investigations of scrapie, Creutzfeldt-Jakob disease (CJD), and chronic wasting disease (CWD) clusters in Iceland, Slovakia and Colorado, respectively, have indicated that the soil in these regions is low in copper and higher in manganese, and it has been well-known that patients of ALS or Parkinson’s disease were collectively found in the New Guinea and Papua islands, where the subterranean water (drinking water) contains much Al3+ and Mn2+ ions. Above facts suggest that these neurodegenerative diseases are closely related with the function of a metal ion.We have investigated t

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Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform

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Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform

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Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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Abstract:

(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform

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5

Imran, M., and S. Mahmood. "An overview of animal prion diseases." Virology journal 8, Journal Article (2011): 493–22. https://doi.org/10.5281/zenodo.13525469.

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Abstract:

(Uploaded by Plazi for the Bat Literature Project) Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform

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6

Eduardo, Salcedo. "Prion Diseases in Animals." Transactions of the National Academy of Science and Technology 24, no. 2 (2002): 1–12. https://doi.org/10.57043/transnastphl.2002.5088.

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Prion diseases refer to a group of invariably neurodegenerative diseases in humans and animals, collectively known as transmissible spongiform encephalopathies (TSEs). These diseases are caused by proteinaceous infectious particles that lack nucleic acid, called prions. This paper reviews prion diseases occurring in animals, excluding human spongiform encephalopathies. Prions in animals include scrapie or ovine spongiform encephalopathy, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), chronic wasting disease (CWD) of mule deer and elk, and feline spongiform enc

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Race, Richard E., Anne Raines, Thierry G. M. Baron, Michael W. Miller, Allen Jenny, and Elizabeth S. Williams. "Comparison of Abnormal Prion Protein Glycoform Patterns from Transmissible Spongiform Encephalopathy Agent-Infected Deer, Elk, Sheep, and Cattle." Journal of Virology 76, no. 23 (2002): 12365–68. http://dx.doi.org/10.1128/jvi.76.23.12365-12368.2002.

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ABSTRACT Analysis of abnormal prion protein glycoform patterns from chronic wasting disease (CWD)-affected deer and elk, scrapie-affected sheep and cattle, and cattle with bovine spongiform encephalopathy failed to identify patterns capable of reliably distinguishing these transmissible spongiform encephalopathy diseases. However, PrP-res patterns sometimes differed among individual animals, suggesting infection by different or multiple CWD strains in some species.

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8

Chesebro, Bruce. "Prion Protein and the Transmissible Spongiform Encephalopathy Diseases." Neuron 24, no. 3 (1999): 503–6. http://dx.doi.org/10.1016/s0896-6273(00)81105-8.

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9

Murdoch, Brenda M., and Gordon K. Murdoch. "Genetics of Prion Disease in Cattle." Bioinformatics and Biology Insights 9S4 (January 2015): BBI.S29678. http://dx.doi.org/10.4137/bbi.s29678.

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Bovine spongiform encephalopathy (BSE) is a prion disease that is invariably fatal in cattle and has been implicated as a significant human health risk. As a transmissible disease of livestock, it has impacted food safety, production practices, global trade, and profitability. Genetic polymorphisms that alter the prion protein in humans and sheep are associated with transmissible spongiform encephalopathy susceptibility or resistance. In contrast, there is no strong evidence that nonsynonymous mutations in the bovine prion gene (PRNP) are associated with classical BSE (C-BSE) disease susceptib

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10

Williams, J. L. "Genetics of transmissible spongiform encephalopathy susceptibility and the search for surrogate markers for infection." Australian Journal of Experimental Agriculture 44, no. 11 (2004): 1119. http://dx.doi.org/10.1071/ea03235.

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The transmissible spongiform encephalopathy diseases are unusual in that they can be sporadic or infectious, and that the infectious agent does not contain nucleic acids. Instead, infectivity is associated with a modified host-encoded protein referred to as a prion. During the course of disease, host encoded prion protein (PrP) is converted from the normal cellular form, PrPC, to a disease form, PrPSC/BSE, which is highly resistant to degradation by heat or proteinases. The occurrence of the sporadic form of transmissible spongiform encephalopathy disease in humans, as well as susceptibility t

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Heumüller, Stefanie-Elisabeth, Annika C. Hornberger, Alina S. Hebestreit, André Hossinger, and Ina M. Vorberg. "Propagation and Dissemination Strategies of Transmissible Spongiform Encephalopathy Agents in Mammalian Cells." International Journal of Molecular Sciences 23, no. 6 (2022): 2909. http://dx.doi.org/10.3390/ijms23062909.

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Transmissible spongiform encephalopathies or prion disorders are fatal infectious diseases that cause characteristic spongiform degeneration in the central nervous system. The causative agent, the so-called prion, is an unconventional infectious agent that propagates by converting the host-encoded cellular prion protein PrP into ordered protein aggregates with infectious properties. Prions are devoid of coding nucleic acid and thus rely on the host cell machinery for propagation. While it is now established that, in addition to PrP, other cellular factors or processes determine the susceptibil

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Hamir, A. N., J. M. Miller, R. A. Kunkle, S. M. Hall, and J. A. Richt. "Susceptibility of Cattle to First-passage Intracerebral Inoculation with Chronic Wasting Disease Agent from White-tailed Deer." Veterinary Pathology 44, no. 4 (2007): 487–93. http://dx.doi.org/10.1354/vp.44-4-487.

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Fourteen, 3-month-old calves were intracerebrally inoculated with the agent of chronic wasting disease (CWD) from white-tailed deer (CWDwtd) to compare the clinical signs and neuropathologic findings with those of certain other transmissible spongiform encephalopathies (TSE, prion diseases) that have been shown to be experimentally transmissible to cattle (sheep scrapie, CWD of mule deer [CWDmd], bovine spongiform encephalopathy [BSE], and transmissible mink encephalopathy). Two uninoculated calves served as controls. Within 26 months postinoculation (MPI), 12 inoculated calves had lost consid

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13

Takemura, K., M. Kahdre, D. Joseph, A. Yousef, and S. Sreevatsan. "An overview of transmissible spongiform encephalopathies." Animal Health Research Reviews 5, no. 2 (2004): 103–24. http://dx.doi.org/10.1079/ahr200494.

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AbstractTransmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders of humans and animals associated with an accumulation of abnormal isoforms of prion protein (PrP) in nerve cells. The pathogenesis of TSEs involves conformational conversions of normal cellular PrP (PrPc) to abnormal isoforms of PrP (PrPSc). While the protein-only hypothesis has been widely accepted as a causal mechanism of prion diseases, evidence from more recent research suggests a possible involvement of other cellular component(s) or as yet undefined infectious agent(s) in PrP pathogenesis. Alth

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Yasir, Saif Jabbar, and Taghreed Abdul Kareem Al- Makhzoomy. "Prions: Some Details and Diseases." Medical Science Journal for Advance Research 2, no. 3 (2021): 80–94. http://dx.doi.org/10.46966/msjar.v2i3.24.

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Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals. They are distinguished by long incubation periods, characteristic spongiform changes associated with neuronal loss, and a failure to induce inflammatory response. Prion diseases in animals, Scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (commonly known as "mad cow disease") in cattle, and Creutzfeldt-Jakob disease in humans are all examples of infectious diseases. The prion protein (PrP) w

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Smith, J. D., J. J. Greenlee, A. N. Hamir, J. A. Richt, and M. H. West Greenlee. "Retinal Function and Morphology Are Altered in Cattle Infected with the Prion Disease Transmissible Mink Encephalopathy." Veterinary Pathology 46, no. 5 (2009): 810–16. http://dx.doi.org/10.1354/vp.08-vp-0206-w-fl.

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Transmissible spongiform encephalopathies (TSEs) are a group of diseases that result in progressive and invariably fatal neurologic disease in both animals and humans. TSEs are characterized by the accumulation of an abnormal protease-resistant form of the prion protein in the central nervous system. Transmission of infectious TSEs is believed to occur via ingestion of prion protein–contaminated material. This material is also involved in the transmission of bovine spongiform encephalopathy (“mad cow disease”) to humans, which resulted in the variant form of Creutzfeldt-Jakob disease. Abnormal

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Juntes, Polona, Jelka Zabavnik-Piano, and Ambrozic Ivan. "Prions and animal transmissible spongiform encephalopathies." Veterinarski glasnik 71, no. 1 (2017): 1–15. http://dx.doi.org/10.2298/vetgl170302004j.

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Background. Transmissible spongiform encephalopathies (TSEs) or prion diseases are a unique group of neurodegenerative diseases of animals and humans, which always have a fatal outcome and are transmissible among animals of the same or different species. Scope and Approach. The aim of this work is to review some recent data about animal TSEs, with the emphasis on their causative agents and zoonotic potential, and to discuss why the surveillance and control measures over animal TSEs should remain in force. Key Findings and Conclusions. We still have incomplete knowledge of prions and prion dise

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Casalone, Cristina, Cristiano Corona, Maria Ines Crescio, et al. "Pathological Prion Protein in the Tongues of Sheep Infected with Naturally Occurring Scrapie." Journal of Virology 79, no. 9 (2005): 5847–49. http://dx.doi.org/10.1128/jvi.79.9.5847-5849.2005.

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ABSTRACT Tongue involvement by prion spreading was shown to be a common outcome after oral or intracranial experimental challenge with scrapie and transmissible mink encephalopathy sources in rodent models. It is also known that bovine spongiform encephalopathy, which is pathogenic for humans, is experimentally transmissible to sheep and can lead to a disease indistinguishable from scrapie. A recent European Food Safety Authority opinion recommended research into PrPsc accumulation in the tongues of ruminants. We report on the detection of PrPsc in the tongues of seven scrapie-infected sheep b

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Milroy, A. M., E. Bouzamondo, H. J. Ralston III, S. B. Prusiner, and S. J. DeArmond. "The Plain and the Ugly Prion Infected Neuronal Tissue in an Experimental Animal Model; An Electron Microscopic Study." Microscopy and Microanalysis 6, S2 (2000): 646–47. http://dx.doi.org/10.1017/s1431927600035728.

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Transmissible encephalopathy of animals (scrapie and bovine spongiform encephalopathy) and of man (Creutzfeldt-Jacob disease, new variant Creutzfeldt-Jacob disease, Kuru, Gerstmann-Straussler-Scheinker disease and familial fatal insomnia) have been well characterized as progressive neurodegenerative diseases, often associated with spongiform degeneration, neuronal loss, reactive astrocytic gliosis and variable amyloid plaques, without any sign of an immune response or inflammatory infiltrates. Prion proteins are elements that propagate variability through multiple biologically active conformer

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Goldmann, Wilfred. "Prion protein genetics: Host PrP control of TSE susceptibility." Biochemist 27, no. 4 (2005): 20–23. http://dx.doi.org/10.1042/bio02704020.

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TSEs (transmissible spongiform encephalopathies) are fatal, degenerative disorders of the central nervous system. The best-known members of this disease family are sheep scrapie, cattle BSE (bovine spongiform encephalopathy) and human CJD (Creutzfeldt–Jakob disease). By far the most important host gene in TSEs is the PrP (prion protein) gene. It modulates TSE susceptibility at many levels and is the crucial element in the treatment and eradication of these diseases. This article will highlight the advances in our understanding of PrP genetics in animals and man.

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Dealler, Steve. "Prion disease: advances in diagnosis and treatment." Morecambe Bay Medical Journal 4, no. 10 (2005): 273–78. http://dx.doi.org/10.48037/mbmj.v4i10.877.

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Steve Dealler is a medical microbiologist with Morecambe Bay Hospitals NHS Trust. His work on on the diagnosis, epidemiology and potential treatment of transmissible spongiform encephalopathies has brought him inter-national recognition. He has been at the forefront of work on the epidemiology of human food containing the vector for bovine spongiform encephalopathy (BSE), and the development of prophylaxis against variant Creutzfeldt-Jakob disease (vCJD). He is currently working on a potential treatment, pentosan polysulphate. Here he describes the current state of knowledge in the battle agai

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Sowemimo-Coker, S. O. "Making blood safe: A filtration technology for removing infectious prions from red-cell concentrates." Biochemist 27, no. 4 (2005): 29–32. http://dx.doi.org/10.1042/bio02704029.

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Prion diseases (TSEs, transmissible spongiform encephalopathies) are fatal neurodegenerative diseases that affect both humans and animals, including scrapie in sheep, BSE (bovine spongiform encephalopathy) in cattle and CJD (Creutzfeldt–Jakob disease) and its variant (vCJD) in humans. The recent occurrences of probable cases of transmission of vCJD through blood transfusion raises concerns about the safety of the blood supply and the possibility of transmission of the causative agent by blood transfusion from asymptomatic infected individuals.

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Lee, J., S. Y. Kim, K. J. Hwang, Y. R. Ju, and H. J. Woo. "Prion diseases as transmissible zoonotic diseases." Osong public health and research perspectives 4, no. 1 (2013): 57–66. https://doi.org/10.5281/zenodo.13525026.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases, also called transmissible spongiform encephalopathies (TSEs), lead to neurological dysfunction in animals and are fatal. Infectious prion proteins are causative agents of many mammalian TSEs, including scrapie (in sheep), chronic wasting disease (in deer and elk), bovine spongiform encephalopathy (BSE; in cattle), and Creutzfeldt-Jakob disease (CJD; in humans). BSE, better known as mad cow disease, is among the many recently discovered zoonotic diseases. BSE cases were first reported in the United Kingdom in 1986. Variant CJD (

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Lee, J., S. Y. Kim, K. J. Hwang, Y. R. Ju, and H. J. Woo. "Prion diseases as transmissible zoonotic diseases." Osong public health and research perspectives 4, no. 1 (2013): 57–66. https://doi.org/10.5281/zenodo.13525026.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases, also called transmissible spongiform encephalopathies (TSEs), lead to neurological dysfunction in animals and are fatal. Infectious prion proteins are causative agents of many mammalian TSEs, including scrapie (in sheep), chronic wasting disease (in deer and elk), bovine spongiform encephalopathy (BSE; in cattle), and Creutzfeldt-Jakob disease (CJD; in humans). BSE, better known as mad cow disease, is among the many recently discovered zoonotic diseases. BSE cases were first reported in the United Kingdom in 1986. Variant CJD (

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Lee, J., S. Y. Kim, K. J. Hwang, Y. R. Ju, and H. J. Woo. "Prion diseases as transmissible zoonotic diseases." Osong public health and research perspectives 4, no. 1 (2013): 57–66. https://doi.org/10.5281/zenodo.13525026.

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(Uploaded by Plazi for the Bat Literature Project) Prion diseases, also called transmissible spongiform encephalopathies (TSEs), lead to neurological dysfunction in animals and are fatal. Infectious prion proteins are causative agents of many mammalian TSEs, including scrapie (in sheep), chronic wasting disease (in deer and elk), bovine spongiform encephalopathy (BSE; in cattle), and Creutzfeldt-Jakob disease (CJD; in humans). BSE, better known as mad cow disease, is among the many recently discovered zoonotic diseases. BSE cases were first reported in the United Kingdom in 1986. Variant CJD (

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Lee, J., S. Y. Kim, K. J. Hwang, Y. R. Ju, and H. J. Woo. "Prion diseases as transmissible zoonotic diseases." Osong public health and research perspectives 4, no. 1 (2013): 57–66. https://doi.org/10.5281/zenodo.13525026.

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Abstract:

(Uploaded by Plazi for the Bat Literature Project) Prion diseases, also called transmissible spongiform encephalopathies (TSEs), lead to neurological dysfunction in animals and are fatal. Infectious prion proteins are causative agents of many mammalian TSEs, including scrapie (in sheep), chronic wasting disease (in deer and elk), bovine spongiform encephalopathy (BSE; in cattle), and Creutzfeldt-Jakob disease (CJD; in humans). BSE, better known as mad cow disease, is among the many recently discovered zoonotic diseases. BSE cases were first reported in the United Kingdom in 1986. Variant CJD (

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Race, Richard E., and Gregory J. Raymond. "Inactivation of Transmissible Spongiform Encephalopathy (Prion) Agents by Environ LpH." Journal of Virology 78, no. 4 (2004): 2164–65. http://dx.doi.org/10.1128/jvi.78.4.2164-2165.2004.

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ABSTRACT Agents causing transmissible spongiform encephalopathy (TSE) diseases are resistant to inactivation by several conventional decontamination methods. Using an animal bioassay, we compared the TSE agent disinfectant efficacy of a commercially available product referred to alternatively as LpH-SE, LpH-AG, or LpH-st to that of a similarly named but differently formulated product, Environ LpH, which was found to be an effective TSE agent disinfectant in a previous study. Here, we found LpH-SE to be at least 104-fold to 105-fold less effective than Environ LpH.

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Bencsik, Anna A., Sabine O. S. Debeer, and Thierry G. M. Baron. "An Alternative Pretreatment Procedure in Animal Transmissible Spongiform Encephalopathies Diagnosis Using PrPsc Immunohistochemistry." Journal of Histochemistry & Cytochemistry 53, no. 10 (2005): 1199–202. http://dx.doi.org/10.1369/jhc.5c6703.2005.

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Because of its sensitivity, immunohistochemistry (IHC) of abnormal prion protein (PrPsc) is used more often in the diagnosis of transmissible spongiform encephalopathies (TSEs), such as scrapie and bovine spongiform encephalopathy (BSE). PrPsc IHC requires a combination of pretreatments (chemical, heating, and enzymatic). The method of application may depend on the anti-prion antibody considered. If these pretreatments are efficient for diagnostic purpose, it may, however, be interesting to use an alternative method to efficiently detect PrPsc IHC immunohistochemically using chemical pretreatm

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Gayrard, V., N. Picard-Hagen, C. Viguié, C. Delavaud, P. L. loutam, and Y. Chilhard. "Exploration of somatotropic axis, leptin, insulin and blood biochemical parameters in ewes naturally affected with scrapie." Proceedings of the British Society of Animal Science 2002 (2002): 88. http://dx.doi.org/10.1017/s1752756200007444.

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Scrapie is an ovine sub-acute transmissible spongiform encephalopathy (TSE) caused by unconventional transmissible agents. In several species, TSE are associated to major endocrinopathy, such as hyperinsulinemia and hypercorticism (Carp et al, 1990, Gayrard et al, 2000). Cachexia is commonly observed in the clinical phase of the prion disease. Our objective was to investigate if scrapie is associated to alterations of GH axis, leptin, insulin and metabolic parameters. In addition, central adrenergic system being affected in TSE (Braun et al, 1999), we investigated a possible alteration of α2-a

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Gavier-Widén, Dolores, Michael J. Stack, Thierry Baron, Aru Balachandran, and Marion Simmons. "Diagnosis of Transmissible Spongiform Encephalopathies in Animals: A Review." Journal of Veterinary Diagnostic Investigation 17, no. 6 (2005): 509–27. http://dx.doi.org/10.1177/104063870501700601.

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Transmissible spongiform encephalopathies (TSEs) in animals include, among others, bovine spongiform encephalopathy (BSE), scrapie, chronic wasting disease, and atypical forms of prion diseases. Diagnosis of TSEs is based on identification of characteristic lesions or on detection of the abnormal prion proteins in tissues, often by use of their partial proteinase K resistance property. Correctly sampling of target tissues is of utmost importance as this has a considerable effect on test sensitivity. Most of the rapid or screening tests are based on ELISA or Western immunoblot (WB) analysis, an

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Frigg, Rico, Michael A. Klein, Ivan Hegyi, Rolf M. Zinkernagel, and Adriano Aguzzi. "Scrapie Pathogenesis in Subclinically Infected B-Cell-Deficient Mice." Journal of Virology 73, no. 11 (1999): 9584–88. http://dx.doi.org/10.1128/jvi.73.11.9584-9588.1999.

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ABSTRACT Prion infections can present without clinical manifestations. B-cell deficiency may be a model for subclinical transmissible spongiform encephalopathy, since it protects mice from disease upon intraperitoneal administration of scrapie prions; however, a proportion of B-cell-deficient mice accumulate protease-resistant prion protein in their brains. Here, we have characterized this subclinical disease. In addition, we have studied the possibility that a neurotoxic factor secreted by B cells may contribute to pathogenesis.

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Klug, Genevieve M., Alison Boyd, Sharron Sarros, et al. "Creutzfeldt-Jakob disease surveillance in Australia, update to December 2014." Communicable Diseases Intelligence 40 (June 1, 2016): 217–15. https://doi.org/10.33321/cdi.2016.40.15.

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Nation-wide surveillance of human transmissible spongiform encephalopathies (also known as prion diseases), the most common being Creutzfeldt-Jakob disease, is performed by the Australian National Creutzfeldt-Jakob Disease Registry, based at the University of Melbourne. Prospective surveillance has been undertaken since 1993 and over this dynamic period in transmissible spongiform encephalopathy research and understanding, the unit has evolved and adapted to changes in surveillance practices and requirements concomitant with the emergence of new disease subtypes, improvements in diagnostic cap

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Klug, Genevieve M., Alison Bod, Shannon Sarros, et al. "Creutzfeldt-Jakob disease surveillance in Australia: update to December 2015." Communicable Diseases Intelligence 40 (September 1, 2016): 368–76. https://doi.org/10.33321/cdi.2016.40.40.

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Nation-wide surveillance of human transmissible spongiform encephalopathies (also known as prion diseases), the most common being Creutzfeldt-Jakob disease, is performed by the Australian National Creutzfeldt-Jakob Disease Registry, based at the University of Melbourne. Prospective surveillance has been undertaken since 1993 and over this dynamic period in transmissible spongiform encephalopathy research and understanding, the unit has evolved and adapted to changes in surveillance practices and requirements concomitant with the delineation of new disease subtypes, improvements in diagnostic c

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Bastian, Frank O., Dearl E. Sanders, Will A. Forbes, et al. "Spiroplasma spp. from transmissible spongiform encephalopathy brains or ticks induce spongiform encephalopathy in ruminants." Journal of Medical Microbiology 56, no. 9 (2007): 1235–42. http://dx.doi.org/10.1099/jmm.0.47159-0.

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Spiroplasma, small motile wall-less bacteria, are linked by molecular and serological studies to the transmissible spongiform encephalopathies (TSEs), which include scrapie in sheep, chronic wasting disease (CWD) in deer and Creutzfeldt–Jakob disease in humans. In this study, two experiments were undertaken to determine the role of spiroplasma in the pathogenesis of TSE. In experiment 1, Spiroplasma mirum, a rabbit tick isolate that had previously been shown to experimentally induce spongiform encephalopathy in rodents, was inoculated intracranially (IC) into ruminants. S. mirum-inoculated dee

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Burgener, Kate, Stuart Siegfried Lichtenberg, Daniel P. Walsh, Heather N. Inzalaco, Aaron Lomax, and Joel A. Pedersen. "Prion Seeding Activity in Plant Tissues Detected by RT-QuIC." Pathogens 13, no. 6 (2024): 452. http://dx.doi.org/10.3390/pathogens13060452.

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Prion diseases such as scrapie, bovine spongiform encephalopathy (BSE), and chronic wasting disease (CWD) affect domesticated and wild herbivorous mammals. Animals afflicted with CWD, the transmissible spongiform encephalopathy of cervids (deer, elk, and moose), shed prions into the environment, where they may persist and remain infectious for years. These environmental prions may remain in soil, be transported in surface waters, or assimilated into plants. Environmental sampling is an emerging area of TSE research and can provide more information about prion fate and transport once shed by in

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Andréoletti, Olivier, Nathalie Morel, Caroline Lacroux, et al. "Bovine spongiform encephalopathy agent in spleen from an ARR/ARR orally exposed sheep." Journal of General Virology 87, no. 4 (2006): 1043–46. http://dx.doi.org/10.1099/vir.0.81318-0.

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Oral contamination with bovine spongiform encephalopathy (BSE) agent in susceptible PRNP genotype sheep results in widespread distribution of prion in the host. Because ARR homozygous sheep are considered to be resistant to transmissible spongiform encephalopathies, they have been selected to eradicate scrapie from sheep flocks and to protect the human food chain from small ruminant BSE risk. However, results presented here show that several months after an oral challenge with BSE agent, healthy ARR/ARR sheep can accumulate significant amounts of PrPSc in the spleen.

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Coulthart, Michael B., Rhonda Mogk, Jason M. Rancourt, Deborah L. Godal, and Stefanie Czub. "Prion protein gene sequence of Canada's first non-imported case of bovine spongiform encephalopathy (BSE)." Genome 46, no. 6 (2003): 1005–9. http://dx.doi.org/10.1139/g03-124.

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In May 2003, Canada became the 22nd country outside of the United Kingdom to report a case of bovine spongiform encephalopathy (BSE) in an animal not known to be imported from a country with cattle previously affected by this fatal, transmissible prion disease. Despite extensive testing of thousands of other animals that may have been exposed to contaminated feed at the same time as the affected animal, no evidence has been found for other infections. This finding leaves room for conjectures that the single confirmed case arose spontaneously, perhaps (by analogy with human Creutzfeldt–Jakob di

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Langeveld, J. P. M., J. G. Jacobs, N. Hunter, et al. "Prion Type-Dependent Deposition ofPRNPAllelic Products in Heterozygous Sheep." Journal of Virology 90, no. 2 (2015): 805–12. http://dx.doi.org/10.1128/jvi.02316-15.

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ABSTRACTSusceptibility or resistance to prion infection in humans and animals depends on single prion protein (PrP) amino acid substitutions in the host, but the agent's modulating role has not been well investigated. Compared to disease incubation times in wild-type homozygous ARQ/ARQ (where each triplet represents the amino acids at codons 136, 154, and 171, respectively) sheep, scrapie susceptibility is reduced to near resistance in ARR/ARR animals while it is strongly enhanced in VRQ/VRQ carriers. Heterozygous ARR/VRQ animals exhibit delayed incubation periods. In bovine spongiform encepha

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Bian, Jifeng, Dana Napier, Vadim Khaychuck, Rachel Angers, Catherine Graham, and Glenn Telling. "Cell-Based Quantification of Chronic Wasting Disease Prions." Journal of Virology 84, no. 16 (2010): 8322–26. http://dx.doi.org/10.1128/jvi.00633-10.

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ABSTRACT Cell-based measurement of prion infectivity is currently restricted to experimental strains of mouse-adapted scrapie. Having isolated cell cultures with susceptibility to prions from diseased elk, we describe a modification of the scrapie cell assay allowing evaluation of prions causing chronic wasting disease, a naturally occurring transmissible spongiform encephalopathy. We compare this cervid prion cell assay to bioassays in transgenic mice, the only other existing method for quantification, and show this assay to be a relatively economical and expedient alternative that will likel

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Brown, D. R. "Copper and prion diseases." Biochemical Society Transactions 30, no. 4 (2002): 742–45. http://dx.doi.org/10.1042/bst0300742.

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Transmissible spongiform encephalopathies are diseases of animals and humans that are also termed prion diseases. These diseases are linked together because a normal brain glycoprotein termed the prion protein is converted to a readily detectable protease-resistant isoform. There is now strong evidence to suggest that apart from this difference in resistance a major difference between the isoforms is that the normal prion protein binds copper and has an anti-oxidant function. Brains from Creutzfeldt-Jakob disease patients and brains from mice with experimental mouse scrapie have been shown to

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Orge, Leonor, Carla Lima, Carla Machado, et al. "Neuropathology of Animal Prion Diseases." Biomolecules 11, no. 3 (2021): 466. http://dx.doi.org/10.3390/biom11030466.

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Transmissible Spongiform Encephalopathies (TSEs) or prion diseases are a fatal group of infectious, inherited and spontaneous neurodegenerative diseases affecting human and animals. They are caused by the conversion of cellular prion protein (PrPC) into a misfolded pathological isoform (PrPSc or prion- proteinaceous infectious particle) that self-propagates by conformational conversion of PrPC. Yet by an unknown mechanism, PrPC can fold into different PrPSc conformers that may result in different prion strains that display specific disease phenotype (incubation time, clinical signs and lesion

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Foliaki, Simote T., Brent Race, Katie Williams, Chase Baune, Bradley R. Groveman, and Cathryn L. Haigh. "Reduced SOD2 expression does not influence prion disease course or pathology in mice." PLOS ONE 16, no. 11 (2021): e0259597. http://dx.doi.org/10.1371/journal.pone.0259597.

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Prion diseases are progressive, neurodegenerative diseases affecting humans and animals. Also known as the transmissible spongiform encephalopathies, for the hallmark spongiform change seen in the brain, these diseases manifest increased oxidative damage early in disease and changes in antioxidant enzymes in terminal brain tissue. Superoxide dismutase 2 (SOD2) is an antioxidant enzyme that is critical for life. SOD2 knock-out mice can only be kept alive for several weeks post-birth and only with antioxidant therapy. However, this results in the development of a spongiform encephalopathy. Conse

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Cronier, Sabrina, Vincent Beringue, Anne Bellon, Jean-Michel Peyrin, and Hubert Laude. "Prion Strain- and Species-Dependent Effects of Antiprion Molecules in Primary Neuronal Cultures." Journal of Virology 81, no. 24 (2007): 13794–800. http://dx.doi.org/10.1128/jvi.01502-07.

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ABSTRACT Transmissible spongiform encephalopathies (TSE) arise as a consequence of infection of the central nervous system by prions and are incurable. To date, most antiprion compounds identified by in vitro screening failed to exhibit therapeutic activity in animals, thus calling for new assays that could more accurately predict their in vivo potency. Primary nerve cell cultures are routinely used to assess neurotoxicity of chemical compounds. Here, we report that prion strains from different species can propagate in primary neuronal cultures derived from transgenic mouse lines overexpressin

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Glatzel, Markus. "Sympathetic Prions." Scientific World JOURNAL 1 (2001): 555–56. http://dx.doi.org/10.1100/tsw.2001.258.

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Transmissible spongiform encephalopathies are a group of invariably fatal neurodegenerative diseases. The infectious agent is termed prion and is thought to be composed of a modified protein (PrPSc or PrPRES), a protease-resistant conformer of the normal host-encoded membrane glycoprotein, PrPC[1]. Bovine spongiform encephalopathy, scrapie of sheep, and Creutzfeldt-Jakob disease are among the most notable transmissible spongiform encephalopathies. Prions are most efficiently propagated trough intracerebral inoculation, yet the entry point of the infectious agent is often through peripheral sit

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Properzi, Francesca, and Maurizio Pocchiari. "Identification of Misfolded Proteins in Body Fluids for the Diagnosis of Prion Diseases." International Journal of Cell Biology 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/839329.

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Transmissible spongiform encephalopathy (TSE) or prion diseases are fatal rare neurodegenerative disorders affecting man and animals and caused by a transmissible infectious agent. TSE diseases are characterized by spongiform brain lesions with neuronal loss and the abnormal deposition in the CNS, and to less extent in other tissues, of an insoluble and protease resistant form of the cellular prion protein (PrPC), namedPrPTSE. In man, TSE diseases affect usually people over 60 years of age with no evident disease-associated risk factors. In some cases, however, TSE diseases are unequivocally l

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Dagvadorj, Ayush, Robert B. Petersen, Hee Suk Lee, et al. "Spontaneous mutations in the prion protein gene causing transmissible spongiform encephalopathy." Annals of Neurology 52, no. 3 (2002): 355–59. http://dx.doi.org/10.1002/ana.10267.

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Vaccari, Gabriele, Claudia D'Agostino, Romolo Nonno, et al. "Prion Protein Alleles Showing a Protective Effect on the Susceptibility of Sheep to Scrapie and Bovine Spongiform Encephalopathy." Journal of Virology 81, no. 13 (2007): 7306–9. http://dx.doi.org/10.1128/jvi.02880-06.

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ABSTRACT The susceptibility of sheep to classical scrapie and bovine spongiform encephalopathy (BSE) is mainly influenced by prion protein (PrP) polymorphisms A136V, R154H, and Q171R, with the ARR allele associated with significantly decreased susceptibility. Here we report the protective effect of the amino acid substitution M137T, I142K, or N176K on the ARQ allele in sheep experimentally challenged with either scrapie or BSE. Such observations suggest the existence of additional PrP alleles that significantly decrease the susceptibility of sheep to transmissible spongiform encephalopathies,

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Murakami-Kubo, Ikuko, Katsumi Doh-ura, Kensuke Ishikawa, et al. "Quinoline Derivatives Are Therapeutic Candidates for Transmissible Spongiform Encephalopathies." Journal of Virology 78, no. 3 (2004): 1281–88. http://dx.doi.org/10.1128/jvi.78.3.1281-1288.2004.

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ABSTRACT We previously reported that quinacrine inhibited the formation of an abnormal prion protein (PrPres), a key molecule in the pathogenesis of transmissible spongiform encephalopathy, or prion disease, in scrapie-infected neuroblastoma cells. To elucidate the structural aspects of its inhibiting action, various chemicals with a quinoline ring were screened in the present study. Assays of the scrapie-infected neuroblastoma cells revealed that chemicals with a side chain containing a quinuclidine ring at the 4 position of a quinoline ring (represented by quinine) inhibited the PrPres forma

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Pradnya D Jadhav, Vaibhav V Kakade, and Aniket E Indrale. "The review on: “Creutzfeldt-Jakob disease”." International Journal of Research in Pharmaceutical Sciences 13, no. 1 (2022): 50–56. http://dx.doi.org/10.26452/ijrps.v13i1.19.

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This review will explore the information about Creutzfeldt -Jakob disease (CJD), which is the human prion disease. CJD is a rare brain disorder and rapidly progressive. CJD belongs to the family of human prion disease, which is caused by misfolded, transmissible infections particles, or prions. Transmissible spongiform encephalopathy (TSEs), also known as prion disease. Spongiform refers to the characteristic appearance of infected brains. CJD affects about one person in every one million people per year worldwide. CJD is a fatal neurodegenerative disorder which is having a higher mortality ra

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Davies, Gwynivere A., Adam R. Bryant, John D. Reynolds, Frank R. Jirik, and Keith A. Sharkey. "Prion Diseases and the Gastrointestinal Tract." Canadian Journal of Gastroenterology 20, no. 1 (2006): 18–24. http://dx.doi.org/10.1155/2006/184528.

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The gastrointestinal (GI) tract plays a central role in the pathogenesis of transmissible spongiform encephalopathies. These are human and animal diseases that include bovine spongiform encephalopathy, scrapie and Creutzfeldt-Jakob disease. They are uniformly fatal neurological diseases, which are characterized by ataxia and vacuolation in the central nervous system. Alhough they are known to be caused by the conversion of normal cellular prion protein to its infectious conformational isoform (PrPsc) the process by which this isoform is propagated and transported to the brain remains poorly un

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Martucci, Francesca, Pierluigi Acutis, Maria Mazza, et al. "Detection of typical and atypical bovine spongiform encephalopathy and scrapie prion strains by prion protein motif-grafted antibodies." Journal of General Virology 90, no. 4 (2009): 1048–53. http://dx.doi.org/10.1099/vir.2008.007120-0.

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To evaluate further the reactivity of prion-specific monoclonal antibodies containing the 89–112 or 136–158 prion protein (PrP) polypeptides, immunoprecipitations were performed on brain extracts from Italian bovines, sheep and goats with transmissible spongiform encephalopathies. No binding of IgG 89–112 or IgG 136–158 to PrP in normal brain extracts was detected. Conversely, both reagents immunoprecipitated PrP from bovine and bovine amyloidotic spongiform encephalopathies, and from typical and atypical scrapie brain extracts. The immunoprecipitated PrP bands mirrored the Western blot (WB) p

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