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Langeveld, J. P. M., J. G. Jacobs, N. Hunter, L. J. M. van Keulen, F. Lantier, F. G. van Zijderveld, and A. Bossers. "Prion Type-Dependent Deposition ofPRNPAllelic Products in Heterozygous Sheep." Journal of Virology 90, no. 2 (October 28, 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 encephalopathy (BSE) infection, the polymorphism effect is quite different although the ARR allotype remains the least susceptible. In this study, PrP allotype composition in protease-resistant prion protein (PrPres) from brain of heterozygous ARR/VRQ scrapie-infected sheep was compared with that of BSE-infected sheep with a similar genotype. A triplex Western blotting technique was used to estimate the two allotype PrP fractions in PrPresmaterial from BSE-infected ARR/VRQ sheep. PrPresin BSE contained equimolar amounts of VRQ- and ARR-PrP, which contrasts with the excess (>95%) VRQ-PrP fraction found in PrP in scrapie. This is evidence that transmissible spongiform encephalopathy (TSE) agent properties alone, perhaps structural aspects of prions (such as PrP amino acid sequence variants and PrP conformational state), determine the polymorphic dependence of the PrPresaccumulation process in prion formation as well as the disease-associated phenotypic expressions in the host.IMPORTANCETransmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative and transmissible diseases caused by prions. Amino acid sequence variants of the prion protein (PrP) determine transmissibility in the hosts, as has been shown for classical scrapie in sheep. Each individual produces a separate PrP molecule from its two PrP gene copies. Heterozygous scrapie-infected sheep that produce two PrP variants associated with opposite scrapie susceptibilities (136V-PrP variant, high; 171R-PrP variant, very low) contain in their prion material over 95% of the 136V PrP variant. However, when these sheep are infected with prions from cattle (bovine spongiform encephalopathy [BSE]), both PrP variants occur in equal ratios. This shows that the infecting prion type determines the accumulating PrP variant ratio in the heterozygous host. While the host's PrP is considered a determining factor, these results emphasize that prion structure plays a role during host infection and that PrP variant involvement in prions of heterozygous carriers is a critical field for understanding prion formation.
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Nishida, Yuzo. "Elucidation of Endemic Neurodegenerative Diseases - a Commentary." Zeitschrift für Naturforschung C 58, no. 9-10 (October 1, 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 the chemical functions of the metal ions in detail and established the unique mechanism of the oxygen activation by the transition metal ions such as iron and copper, and pointed out the notable difference in the mechanism among iron, aluminum and manganese ions. Based on these results, it has become apparent that the incorporation of Al(III) or Mn(II) in the cells induces the “iron-overload syndrome”, which is mainly due to the difference in an oxygen activation mechanism between the iron ion and Al(III) or the Mn(II) ion. This syndrome highly promotes formation of hydrogen peroxide, and hydrogen peroxide thus produced can be a main factor to cause serious damages to DNA and proteins (oxidative stress), yielding a copper(II)-or manganese(II)-peptide complex and its peroxide adduct, which are the serious agents to induce the structural changes from the normal prion protein (PrPC) to abnormal disease-causing isoforms, PrPSc, or the formation of PrP 27Ð30 (abnormal cleavage at site 90 of the prion protein).It seems reasonable to consider that the essential origin for the transmissible spongiform encephalopathies (TSEs) should be the incorporation and accumulation of Al(III) and Mn(II) ions in the cells, and the sudden and explosive increase of scrapie and bovine spongiform encephalopathy (BSE) in the last decade may be partially due to “acid rain”, because the acid rain makes Al(III) and Mn(II) ions soluble in the subterranean aquifers.
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Chesebro, Bruce. "Prion Protein and the Transmissible Spongiform Encephalopathy Diseases." Neuron 24, no. 3 (November 1999): 503–6. http://dx.doi.org/10.1016/s0896-6273(00)81105-8.
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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 (December 1, 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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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 (March 8, 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 susceptibility of cell lines to prion infection, exact factors and cellular processes remain broadly obscure. Still, cellular models have uncovered important aspects of prion propagation and revealed intercellular dissemination strategies shared with other intracellular pathogens. Here, we summarize what we learned about the processes of prion invasion, intracellular replication and subsequent dissemination from ex vivo cell models.
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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 susceptibility, though two bovine PRNP insertion/deletion polymorphisms, in the putative region, are associated with susceptibility to C-BSE. However, these associations do not explain the full extent of BSE susceptibility, and loci outside of PRNP appear to be associated with disease incidence in some cattle populations. This article provides a review of the current state of genetic knowledge regarding prion diseases in cattle.
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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 to infection in humans and some animal species has been correlated with particular alleles of the host PrP gene. Scrapie has been endemic in sheep populations in many countries for over 100 years, with no apparent adverse effects on human health, however the occurrence of bovine spongiform encephalopathy in the mid 1980s in the United Kingdom and subsequently other countries has stimulated interest in the transmissible spongiform encephalopathy diseases. Bovine spongiform encephalopathy seems to have arisen from the recycling of ruminant offals, although it is not clear whether bovine spongiform encephalopathy was already endemic in the cattle population and this practice simply increased the incidence, or if the disease was newly introduced to cattle by transmission of scrapie from sheep. A new form of Creutzfeldt-Jacob disease that bares all the hallmarks of bovine spongiform encephalopathy was recently described in humans, suggesting that it arose from consumption of bovine spongiform encephalopathy-infected beef. Subsequent studies have demonstrated that transmissible spongiform encephalopathy disease can be experimentally transmitted between species and has alerted us to the potential risk of allowing scrapie to remain in the sheep population. In the United Kingdom, the sheep population is being PrP-genotyped and breeding stock selected from animals with genotypes that have been shown to be more resistant to scrapie. However, the resistant sheep genotypes may still harbour disease. There is no convincing evidence for PrP genotypes in cattle that are resistant to bovine spongiform encephalopathy. Work in cattle and mice has shown that there are loci other than PrP that influence the host response to a transmissible spongiform encephalopathy challenge. In order to monitor, and ultimately control, transmissible spongiform encephalopathy diseases in livestock it is important to identify markers for infection that are robust, appear early in infection and can be measured in an easily obtained sample, such as blood. We have developed a bovine ‘non-redundant’ cDNA set from brain to allow expression profiling using macro- and micro array technology. The identities of genes represented the in the non-redundant cDNAs set were assigned by oligo-nucleotide fingerprinting and have been confirmed by sequencing. This non-redundant cDNA set has been used to create a bovine array that is being used to examine expression in tissues from cattle during a time course of experimental bovine spongiform encephalopathy infection in order to identify genes with expression profiles that are altered following infection. Such genes may provide surrogate markers to detect transmissible spongiform encephalopathy infection during the early stages of disease. Ultimately knowledge of such genes may suggest targets for pharmacological intervention to arrest the disease process before the onset of the major neurological damage associated with the terminal stage of the disease.
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Takemura, K., M. Kahdre, D. Joseph, A. Yousef, and S. Sreevatsan. "An overview of transmissible spongiform encephalopathies." Animal Health Research Reviews 5, no. 2 (December 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. Although the underlying mechanisms of PrP strain variation and the determinants of interspecies transmissibility have not been fully elucidated, biochemical and molecular findings indicate that bovine spongiform encephalopathy in cattle and new-variant Creutzfeldt–Jakob disease in humans are caused by indistinguishable etiological agent(s). Cumulative evidence suggests that there may be risks of humans acquiring TSEs via a variety of exposures to infected material. The development of highly precise ligands is warranted to detect and differentiate strains, allelic variants and infectious isoforms of these PrPs. This article describes the general features of TSEs and PrP, the current understanding of their pathogenesis, recent advances in prion disease diagnostics, and PrP inactivation.
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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 (July 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 considerable weight and eventually became recumbent. Of the 12 inoculated calves, 11 (92%) developed clinical signs. Although spongiform encephalopathy (SE) was not observed, abnormal prion protein (PrPd) was detected by immunohistochemistry (IHC) and Western blot (WB) in central nervous system tissues. The absence of SE with presence of PrPd has also been observed when other TSE agents (scrapie and CWDmd) were similarly inoculated into cattle. The IHC and WB findings suggest that the diagnostic techniques currently used to confirm BSE would detect CWDwtd in cattle, should it occur naturally. Also, the absence of SE and a distinctive IHC pattern of CWDwtd and CWDmd in cattle suggests that it should be possible to distinguish these conditions from other TSEs that have been experimentally transmitted to cattle.
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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 (February 15, 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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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 diseases. Scrapie has been present for a very long time and controlled with varied success. Bovine spongiform encephalopathy (BSE) emerged unnoticed, and spread within a few years to epidemic proportions, entailing enormous economic consequences and public concerns. Currently, the classical BSE epidemic is under control, but atypical cases do, and probably will, persist in bovine populations. The Chronic Wasting Disease (CWD) of the cervids has been spreading in North America and has recently been detected in Europe. Preventive measures for the control of classical BSE remain in force, including the feed ban and removal of specified risk materials. However, active BSE surveillance has considerably decreased. In the absence of such preventive and control measures, atypical BSE cases in healthy slaughtered bovines might persist in the human food chain, and BSE prions might resurface. Moreover, other prion strains might emerge and spread undetected if the appropriate preventive and surveillance measures were to cease, leaving behind inestimable consequences.
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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 (September 30, 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) was identified in a patient in 2015, and it was previously believed to be the cause of all known mammalian prion diseases. However, The protein alpha-synuclein, which is thought to be responsible for MSA, was suggested to be the cause of the disease in 2015.
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Bastian, Frank O., Dearl E. Sanders, Will A. Forbes, Sue D. Hagius, Joel V. Walker, William G. Henk, Fred M. Enright, and Philip H. Elzer. "Spiroplasma spp. from transmissible spongiform encephalopathy brains or ticks induce spongiform encephalopathy in ruminants." Journal of Medical Microbiology 56, no. 9 (September 1, 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 deer manifested clinical signs of TSE after 1.5 to 5.5 months incubation. The deer, as well as sheep and goats, inoculated with S. mirum developed spongiform encephalopathy in a dose-dependent manner. In experiment 2, spiroplasma closely related to S. mirum were isolated from TSE-affected brains via passage in embryonated eggs, and propagated in cell-free M1D media. Spiroplasma spp. isolates from scrapie-affected sheep brain and from CWD-affected deer brain inoculated IC into sheep and goats induced spongiform encephalopathy closely resembling natural TSE in these animals. These data show spiroplasma to be consistently associated with TSE, and able experimentally to cause TSE in ruminant animal models, therein questioning the validity of studies that have concluded the prion, a miss-folded protease-resistant protein that builds up in TSE brains during the course of the disease, to be the sole causal agent. The spiroplasma infection models reported here will be important for investigating factors involved in the pathogenesis of TSE since ruminants are the natural hosts.
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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 (May 9, 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 prion protein has been reported in the retina of TSE-affected cattle, but despite these observations, the specific effect of abnormal prion protein on retinal morphology and function has not been assessed. The objective of this study was to identify and characterize potential functional and morphologic abnormalities in the retinas of cattle infected with a bovine-adapted isolate of transmissible mink encephalopathy. We used electroretinography and immunohistochemistry to examine retinas from 10 noninoculated and 5 transmissible mink encephalopathy–inoculated adult Holstein steers. Here we show altered retinal function, as evidenced by prolonged implicit time of the electroretinogram b-wave, in transmissible mink encephalopathy–infected cattle before the onset of clinical illness. We also demonstrate disruption of rod bipolar cell synaptic terminals, indicated by decreased immunoreactivity for the alpha isoform of protein kinase C and vesicular glutamate transporter 1, and activation of Müller glia, as evidenced by increased glial fibrillary acidic protein and glutamine synthetase expression, in the retinas of these cattle at the time of euthanasia due to clinical deterioration. This is the first study to identify both functional and morphologic alterations in the retinas of TSE-infected cattle. Our results support future efforts to focus on the retina for the development of new strategies for the diagnosis of TSEs.
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Casalone, Cristina, Cristiano Corona, Maria Ines Crescio, Francesca Martucci, Maria Mazza, Giuseppe Ru, Elena Bozzetta, Pier Luigi Acutis, and Maria Caramelli. "Pathological Prion Protein in the Tongues of Sheep Infected with Naturally Occurring Scrapie." Journal of Virology 79, no. 9 (May 1, 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 by immunohistochemistry and Western blotting.
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Dealler, Steve. "Prion disease: advances in diagnosis and treatment." Morecambe Bay Medical Journal 4, no. 10 (January 1, 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 against this devastating disease and the political inertia that frustrated earlier attempts to prevent the epidemic.
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Goldmann, Wilfred. "Prion protein genetics: Host PrP control of TSE susceptibility." Biochemist 27, no. 4 (August 1, 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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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 (August 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 conformers of a host encoded sialoglycoprotein (PrPc). The agent responsible for transmissible encephalopathies is composed mainly, if not exclusively, of an isoform of PrP, designated PrPSc. Extensive information of post-mortem material has been described at the light microscopic level, where the emphasis has been on spongiform tissue and amyloid plaques. Our study provides ultrastructural observations of the central nervous system, specifically of degenerating neurons and their associated changes during the course of scrapie infection in a hamster model.
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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 (November 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, and many are officially approved. Confirmatory testing is normally performed by use of histologic examination, immunohistochemical analysis, certain WB protocols, or detection of prion fibrils by use of electron microscopy (scrapie-associated fibril). The discriminatory methods for diagnostic use are mostly based on WB technology and provide initial identification of the prion strain, particularly for differentiation of BSE from scrapie in small ruminants. Definitive prion strain characterization is performed by use of bioassays, usually in mice. A burgeoning number of transgenic mice have been developed for TSE studies. Development of new tests with higher sensitivity and of more reliable diagnostic applications for live animals tested for food safety reasons is a rapidly developing field. Ultimately, the choice of a test for TSE diagnosis depends on the rationale for the testing.
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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 (August 1, 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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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 (June 27, 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 pretreatments solely. Here we describe such pretreatments reporting the difficulty (section adhesion) but also the potential advantages of such methods (easy, quick, inexpensive, and amplifying effect).
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Dagvadorj, Ayush, Robert B. Petersen, Hee Suk Lee, Larisa Cervenakova, Alexey Shatunov, Herbert Budka, Paul Brown, Pierluigi Gambetti, and Lev G. Goldfarb. "Spontaneous mutations in the prion protein gene causing transmissible spongiform encephalopathy." Annals of Neurology 52, no. 3 (August 30, 2002): 355–59. http://dx.doi.org/10.1002/ana.10267.
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Brown, D. R. "Copper and prion diseases." Biochemical Society Transactions 30, no. 4 (August 1, 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 have changes in the levels of both copper and manganese. There is growing evidence that links prion diseases to disturbances of metal metabolism.
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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-adrenergic control of GH axis associated to the prion disease.
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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 (November 1, 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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Andréoletti, Olivier, Nathalie Morel, Caroline Lacroux, Virginie Rouillon, Céline Barc, Guillaume Tabouret, Pierre Sarradin, et al. "Bovine spongiform encephalopathy agent in spleen from an ARR/ARR orally exposed sheep." Journal of General Virology 87, no. 4 (April 1, 2006): 1043–46. http://dx.doi.org/10.1099/vir.0.81318-0.
Full textAbstract:
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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Murakami-Kubo, Ikuko, Katsumi Doh-ura, Kensuke Ishikawa, Satoshi Kawatake, Kensuke Sasaki, Jun-ichi Kira, Shigeru Ohta, and Toru Iwaki. "Quinoline Derivatives Are Therapeutic Candidates for Transmissible Spongiform Encephalopathies." Journal of Virology 78, no. 3 (February 1, 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 formation at a 50% inhibitory dose ranging from 10−1 to 101 μM. On the other hand, chemicals with a side chain at the 2 position of a quinoline ring (represented by 2,2′-biquinoline) more effectively inhibited the PrPres formation at a 50% inhibitory dose ranging from 10−3 to 10−1 μM. A metabolic labeling study revealed that the action of quinine or biquinoline was not due to any alteration in the biosynthesis or turnover of normal prion protein, whereas surface plasmon resonance analysis showed a strong binding affinity of biquinoline with a recombinant prion protein. In vivo studies revealed that 4-week intraventricular infusion of quinine or biquinoline was effective in prolonging the incubation period in experimental mouse models of intracerebral infection. The findings suggest that quinoline derivatives with a nitrogen-containing side chain have the potential of both inhibiting PrPres formation in vitro and prolonging the incubation period of infected animals. These chemicals are new candidates for therapeutic drugs for use in the treatment of transmissible spongiform encephalopathies.
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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 (June 2, 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 likely facilitate studies of this important prion disease.
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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 (December 1, 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 disease) as a result of a somatic protein misfolding event or a novel germline mutation. Here we present DNA sequence data from the affected animal's prion protein coding sequence that argue definitively against the latter hypothesis.Key words: bovine spongiform encephalopathy, spontaneous origin, prions, mutation, Canada.
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KALDRYMIDOU (Ε. ΚΑΛΔΡΥΜΙΔΟΥ), E., G. KANAKOUDIS (Γ. ΚΑΝΑΚΟΥΔΗΣ), K. KATSARAS (Κ. ΚΑΤΣΑΡΑΣ), Th TSANGARIS (Θ. ΤΣΑΓΓΑΡΗΣ), and N. PAPAIOANNOU (Ν. ΠAΠΑΪΩΑNNOΥ). "Bovine Spongiform Encephalopathy and Public Health." Journal of the Hellenic Veterinary Medical Society 49, no. 3 (January 31, 2018): 171. http://dx.doi.org/10.12681/jhvms.15768.
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Bovine Spongiform Encephalopathy (BSE) is a transmissible degenerative disease of the central nervous system. It belongs to a group of diseases which affect man and various kinds of animals and they have a similar histopathological appearance. The harmful agent of BSE and all the others spongiform encephalopathies have not been totally clarified. Today according to the predominant opinion this agent is consisted mainly or/and only of an abnormal protein, which is called prion. In various observations the harmful agent appears like proteinaceous cylinders which are consisted of aggregations or polymerized forms of the agent and it is called prion-protein (PrP). It has been proved that there are two isoforms of PrP. The first of them, called PrPc, is produced from many cells of man and animals and consists a cellular structural element. The second, called PrPs t, due to its specific properties, it is considered to be pathological and responsible for the spongiform encephalopathies. The replication of PrPsc seems to take place in the lysosomes of central nervous system cells, dendritic, and other reticular cells of the lymphatic organs through transformation of PrPc into PrPsc. It appears BSE caused by feeding meat and bone meals to cattle which were originated from scrapie infected sheep. Refering to the pathogenesis originating from experimental data it seems that initially the PrF* enters the body by food and afterwards is settled in various lymphoid organs where the first replication takes place. It is believed that BSE is transmitted through the nerves to the CNS, where it creates the characteristic lesions of vacuolar degeneration of the neurons and finally the spongiosis. Then the clinical signs are expressed. The nervous signs characterised by behavioural alterations of the animals and kinetic abnormalities. The diagnosis of the disease is made by the observation of the histopathological lesions, the detection of Scrapie Associated Fibrils-SAF by EM, the immunohistochemical detection of prpsc i n histological samples or by electrophoresis (Western blotting test). BSE was proved to be transmissible to other animals and there is a possibility that it could be done to man through the food chain. According to the above in these years, from the appearance of the disease until now, have been taken bans from Great Britain as well as from E.U. for the eradication of the disease and the protection of the public health. These instructions should be followed by the authorities and additionally the consumers ought to be informed for the possible danger of various animal products.
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Orge, Leonor, Carla Lima, Carla Machado, Paula Tavares, Paula Mendonça, Paulo Carvalho, João Silva, et al. "Neuropathology of Animal Prion Diseases." Biomolecules 11, no. 3 (March 21, 2021): 466. http://dx.doi.org/10.3390/biom11030466.
Full textAbstract:
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 profile). Although the pathways for neurodegeneration as well as the involvement of brain inflammation in these diseases are not well understood, the spongiform changes, neuronal loss, gliosis and accumulation of PrPSc are the characteristic neuropathological lesions. Scrapie affecting small ruminants was the first identified TSE and has been considered the archetype of prion diseases, though atypical and new animal prion diseases continue to emerge highlighting the importance to investigate the lesion profile in naturally affected animals. In this report, we review the neuropathology and the neuroinflammation of animal prion diseases in natural hosts from scrapie, going through the zoonotic bovine spongiform encephalopathy (BSE), the chronic wasting disease (CWD) to the newly identified camel prion disease (CPD).
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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 (October 3, 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 overexpressing ovine, murine, hamster, or human prion protein. Using this newly developed cell system, the activity of three generic compounds known to cure prion-infected cell lines was evaluated. We show that the antiprion activity observed in neuronal cultures is species or strain dependent and recapitulates to some extent the activity reported in vivo in rodent models. Therefore, infected primary neuronal cultures may be a relevant system in which to investigate the efficacy and mode of action of antiprion drugs, including toward human transmissible spongiform encephalopathy agents.
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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 (November 4, 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. Consequently, we hypothesized that reduced levels of SOD2 may accelerate prion disease progression and play a critical role in the formation of spongiform change. Using SOD2 heterozygous knock-out and litter mate wild-type controls, we examined neuronal long-term potentiation, disease duration, pathology, and degree of spongiform change in mice infected with three strains of mouse adapted scrapie. No influence of the reduced SOD2 expression was observed in any parameter measured for any strain. We conclude that changes relating to SOD2 during prion disease are most likely secondary to the disease processes causing toxicity and do not influence the development of spongiform pathology.
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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 understood. M cells, dendritic cells and possibly enteroendocrine cells are important in the movement of infectious prions across the GI epithelium. From there, PrPscpropagation requires B lymphocytes, dendritic cells and follicular dendritic cells of Peyer’s patches. The early accumulation of the disease-causing agent in the plexuses of the enteric nervous system supports the contention that the autonomic nervous system is important in disease transmission. This is further supported by the presence of PrPscin the ganglia of the parasympathetic and sympathetic nerves that innervate the GI tract. Additionally, the lymphoreticular system has been implicated as the route of transmission from the gut to the brain. Although normal cellular prion protein is found in the enteric nervous system, its role has not been characterized. Further research is required to understand how the cellular components of the gut wall interact to propagate and transmit infectious prions to develop potential therapies that may prevent the progression of transmissible spongiform encephalopathies.
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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 sites like the gastrointestinal tract[2,3]. The process by which prions invade the brain is termed neuroinvasion[4]. We and others have speculated that, depending on the amount of infectious agent injected, the injection site, and the strain of prions employed, neuroinvasion can occur either directly via peripheral nerves or first through the lymphoreticular system and then via peripheral nerves[5].
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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.
Full textAbstract:
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 linked to infectious episodes related to the use of prion-contaminated medicines, medical devices, or meat products as in the variant Creutzfeldt-Jakob disease (CJD). Clinical signs occur months or years after infection, and during this silent periodPrPTSE, the only reliable marker of infection, is not easily measurable in blood or other accessible tissues or body fluids causing public health concerns. To overcome the limit ofPrPTSEdetection, several highly sensitive assays have been developed, but attempts to apply these techniques to blood of infected hosts have been unsuccessful or not yet validated. An update on the latest advances for the detection of misfolded prion protein in body fluids is provided.
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MOON, HARLEY W. "Bovine Spongiform Encephalopathy: Hypothetical Risk of Emergence as a Zoonotic Foodborne Epidemic." Journal of Food Protection 59, no. 10 (October 1, 1996): 1106–11. http://dx.doi.org/10.4315/0362-028x-59.10.1106.
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Bovine spongiform encephalopathy (BSE) is a fatal neurological disease of cattle, recognized in Great Britain in 1986. Cases in other countries have been attributed to imports from Great Britain. The disease has not occurred in the U.S. BSE is one of a group of diseases (other examples are scrapie of sheep and Creutzfeld-Jacob disease of humans) referred to as prion diseases or transmissible spongiform encephalopathies. Under some circumstances prion diseases can be transmitted by injection or by feeding infected (abnormal prion protein-containing) tissue to susceptible hosts. BSE was disseminated by feeding meat and bone meal containing BSE agent which was not completely inactivated by rendering. BSE is hypothesized to have emerged from scrapie via recycling of rendered by-products in cattle. There is also evidence of spontaneous feed-borne transmission of BSE to wild ruminants in zoological parks and to domestic cats. It has been hypothesized that foodborne transmission of BSE to humans has occurred or could occur. This hypothesis can neither be definitively refuted nor supported. However, it seems unlikely. In spite of hundreds of years of human exposure to scrapie, there is no evidence of transmission of scrapie to humans. Even if BSE is ultimately found to be somehow transmissible to humans, the risk of foodborne transmission appears to be low for several reasons: (i) The oral route is several orders of magnitude less sensitive than the parenteral route for transmission of prion diseases; (ii) the BSE agent is only detectable in brain, spinal cord, and intestine of infected cattle, tissues infrequently used for human food; and (iii) Great Britain (where the disease occurs) destroys and bans the use of all tissues from BSE-infected cattle as well as the brains, spinal cords, and intestinal tracts from clinically normal cattle.
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Vaccari, Gabriele, Claudia D'Agostino, Romolo Nonno, Francesca Rosone, Michela Conte, Michele Angelo Di Bari, Barbara Chiappini, 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 (April 18, 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, which may have important implications for disease eradication strategies.
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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 (March 21, 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 rate. CJD usually appears in later life and has a high incubation period but become rapidly progressive once clinically symptoms begin. CJD exist in three major groups sporadic CJD (sCJD), Acquired CJD, and Genetic CJD. The sporadic form generally affects the late middle age or elderly persons (Mean age of 67 years). Most people with clinically diagnosed CJD die within a year. Other neurodegenerative illness like Alzheimer's disease involves the deposition of an aberrantly folded protein: although CJD is transmissible. There is no specific treatment for CJD except for supportive care. The arrangement of different clinicians and surveillance programs can maintain awareness of CJD to control the future incidence of its transmission.
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Martucci, Francesca, Pierluigi Acutis, Maria Mazza, Sabrina Nodari, Silvia Colussi, Cristiano Corona, Simone Barocci, 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 (April 1, 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) profile of the different prion strains, indicating universal affinity of two independent PrP regions for disease-associated PrP conformers regardless of species source and strain properties. Immunoprecipitation with motif-grafted antibodies increased the sensitivity of conventional detection methods based on centrifugation followed by WB, which was confirmed by assay of diluted samples using both methods. These reagents or derivative molecules may thus find broad applications in prion detection and research.
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Hamir, A. N., R. A. Kunkle, J. M. Miller, and J. A. Richt. "Second Passage of Sheep Scrapie and Transmissible Mink Encephalopathy (TME) Agents in Raccoons (Procyon lotor)." Veterinary Pathology 42, no. 6 (November 2005): 844–51. http://dx.doi.org/10.1354/vp.42-6-844.
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To determine the transmissibility and pathogenicity of sheep scrapie and transmissible mink encephalopathy (TME) agents derived from raccoons (first passage), raccoon kits were inoculated intracerebrally with either TME (one source) or scrapie (two sources—each in separate groups of raccoons). Two uninoculated raccoon kits served as controls. All animals in the TME-inoculated group developed clinical signs of neurologic dysfunction and were euthanatized between postinoculation month (PIM) 6 and 8. Raccoons in the two scrapie-inoculated groups manifested similar clinical signs of disease, but such signs were observed much later and the animals were euthanized between PIM 12 and 18. Necropsy revealed no gross lesions in any of the raccoons. Spongiform encephalopathy was observed by use of light microscopy, and the presence of protease-resistant prion protein (PrPres) was detected by use of immunohistochemical (IHC) and Western blot analytic techniques. Results of IHC analysis indicated a distinct pattern of anatomic distribution of PrPres in the TME- and scrapie-inoculated raccoons. These findings confirm that TME and sheep scrapie are experimentally transmissible to raccoons and that the incubation periods and IHC distribution for both agents are distinct. Therefore, it may be possible to use raccoons for differentiating unknown transmissible spongiform encephalopathy (TSE) agents. Further studies, with regard to the incubation period and the pattern of PrPres deposition by use of IHC analysis in bovine spongiform encephalopathy and for other isolates of scrapie, chronic wasting disease, and TME in raccoons are needed before the model can be further characterized for differentiation of TSE agents.
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Thomzig, Achim, Franco Cardone, Dominique Krüger, Maurizio Pocchiari, Paul Brown, and Michael Beekes. "Pathological prion protein in muscles of hamsters and mice infected with rodent-adapted BSE or vCJD." Journal of General Virology 87, no. 1 (January 1, 2006): 251–54. http://dx.doi.org/10.1099/vir.0.81277-0.
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Recently, pathological prion protein (PrPTSE) was detected in muscle from sheep infected with scrapie, the archetype of transmissible spongiform encephalopathies (TSEs). This finding has highlighted the question of whether mammalian muscle may potentially also provide a reservoir for TSE agents related to bovine spongiform encephalopathy (BSE) and variant Creutzfeldt–Jakob Disease (vCJD). Here, results are reported from studies in hamsters and mice that provide direct experimental evidence, for the first time, of BSE- and vCJD-associated PrPTSE deposition in muscles. Our findings emphasize the need for further assessment of possible public-health risks from TSE involvement of skeletal muscle.
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Lambert, Zoe J., Justin J. Greenlee, Eric D. Cassmann, and M. Heather West Greenlee. "Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases." Viruses 13, no. 12 (December 7, 2021): 2453. http://dx.doi.org/10.3390/v13122453.
Full textAbstract:
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative protein misfolding diseases that invariably cause death. TSEs occur when the endogenous cellular prion protein (PrPC) misfolds to form the pathological prion protein (PrPSc), which templates further conversion of PrPC to PrPSc, accumulates, and initiates a cascade of pathologic processes in cells and tissues. Different strains of prion disease within a species are thought to arise from the differential misfolding of the prion protein and have different clinical phenotypes. Different strains of prion disease may also result in differential accumulation of PrPSc in brain regions and tissues of natural hosts. Here, we review differential accumulation that occurs in the retinal ganglion cells, cerebellar cortex and white matter, and plexuses of the enteric nervous system in cattle with bovine spongiform encephalopathy, sheep and goats with scrapie, cervids with chronic wasting disease, and humans with prion diseases. By characterizing TSEs in their natural host, we can better understand the pathogenesis of different prion strains. This information is valuable in the pursuit of evaluating and discovering potential biomarkers and therapeutics for prion diseases.
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Baker, Ridley, Wells, and Ironside. "Prion protein immunohistochemical staining in the brains of monkeys with transmissible spongiform encephalopathy." Neuropathology and Applied Neurobiology 24, no. 6 (November 1998): 476–86. http://dx.doi.org/10.1046/j.1365-2990.1998.00142.x.
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Salzano, Giulia, Gabriele Giachin, and Giuseppe Legname. "Structural Consequences of Copper Binding to the Prion Protein." Cells 8, no. 8 (July 25, 2019): 770. http://dx.doi.org/10.3390/cells8080770.
Full textAbstract:
Prion, or PrPSc, is the pathological isoform of the cellular prion protein (PrPC) and it is the etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and animal species. The most relevant function of PrPC is its ability to bind copper ions through its flexible N-terminal moiety. This review includes an overview of the structure and function of PrPC with a focus on its ability to bind copper ions. The state-of-the-art of the role of copper in both PrPC physiology and in prion pathogenesis is also discussed. Finally, we describe the structural consequences of copper binding to the PrPC structure.
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Leach, Scott P., M. D. Salman, and Dwayne Hamar. "Trace elements and prion diseases: a review of the interactions of copper, manganese and zinc with the prion protein." Animal Health Research Reviews 7, no. 1-2 (June 2006): 97–105. http://dx.doi.org/10.1017/s1466252307001181.
Full textAbstract:
Transmissible spongiform encephalopathies (TSEs) are a family of neurodegenerative diseases characterized by their long incubation periods, progressive neurological changes, and spongiform appearance in the brain. There is much evidence to show that TSEs are caused by an isoform of the normal cellular surface prion protein PrPC. The normal function of PrPC is still unknown, but it exhibits properties of a cupro-protein, capable of binding up to six copper ions. There are two differing views on copper's role in prion diseases. While one view looks at the PrPC copper-binding as the trigger for conversion to PrPSc, the opposing viewpoint sees a lack of PrPC copper-binding resulting in the conformational change into the disease causing isoform. Manganese and zinc have been shown to interact with PrPC as well and have been found in abnormal levels in prion diseases. This review addresses the interaction between select trace elements and the PrPC.
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Goldmann, Wilfred, Fiona Houston, Paula Stewart, Matteo Perucchini, James Foster, and Nora Hunter. "Ovine prion protein variant A136R154L168Q171 increases resistance to experimental challenge with bovine spongiform encephalopathy agent." Journal of General Virology 87, no. 12 (December 1, 2006): 3741–45. http://dx.doi.org/10.1099/vir.0.82083-0.
Full textAbstract:
Susceptibility and incubation periods of transmissible spongiform encephalopathies, such as scrapie in sheep, are modulated by the PrP gene. The standard model of association between ovine PrP genetics and classical scrapie susceptibility is based on PrP genotypes with respect to codons 136, 154 and 171, e.g. alanine–arginine–glutamine (ARQ). It is demonstrated here that a proline to leucine substitution in codon 168 of the ovine PrP protein gene is associated with increased resistance to experimental bovine spongiform encephalopathy (BSE) inoculation. The ARL168Q PrP allele was found in heterozygous ARP168Q/ARL168Q sheep that have so far survived intravenous BSE challenge three times longer than BSE-challenged homozygous ARP168Q/ARP168Q sheep, which develop disease in around 700 days. In contrast, the L141F polymorphism does not appear to be associated with susceptibility to intravenous BSE challenge.
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Eiden, Martin, Alma Gedvilaite, Fabienne Leidel, Rainer G. Ulrich, and Martin H. Groschup. "Vaccination with Prion Peptide-Displaying Polyomavirus-Like Particles Prolongs Incubation Time in Scrapie-Infected Mice." Viruses 13, no. 5 (April 30, 2021): 811. http://dx.doi.org/10.3390/v13050811.
Full textAbstract:
Prion diseases like scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle or Creutzfeldt–Jakob disease (CJD) in humans are fatal neurodegenerative diseases characterized by the conformational conversion of the normal, mainly α-helical cellular prion protein (PrPC) into the abnormal β-sheet rich infectious isoform PrPSc. Various therapeutic or prophylactic approaches have been conducted, but no approved therapeutic treatment is available so far. Immunisation against prions is hampered by the self-tolerance to PrPC in mammalian species. One strategy to avoid this tolerance is presenting PrP variants in virus-like particles (VLPs). Therefore, we vaccinated C57/BL6 mice with nine prion peptide variants presented by hamster polyomavirus capsid protein VP1/VP2-derived VLPs. Mice were subsequently challenged intraperitoneally with the murine RML prion strain. Importantly, one group exhibited significantly increased mean survival time of 240 days post-inoculation compared with 202 days of the control group. These data show that immunisation with VLPs presenting PrP peptides may represent a promising strategy for an effective vaccination against transmissible spongiform encephalitis agents.
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Wilson, Rona, Chris Plinston, Nora Hunter, Cristina Casalone, Cristiano Corona, Fabrizio Tagliavini, Silvia Suardi, et al. "Chronic wasting disease and atypical forms of bovine spongiform encephalopathy and scrapie are not transmissible to mice expressing wild-type levels of human prion protein." Journal of General Virology 93, no. 7 (July 1, 2012): 1624–29. http://dx.doi.org/10.1099/vir.0.042507-0.
Full textAbstract:
The association between bovine spongiform encephalopathy (BSE) and variant Creutzfeldt–Jakob disease (vCJD) has demonstrated that cattle transmissible spongiform encephalopathies (TSEs) can pose a risk to human health and raises the possibility that other ruminant TSEs may be transmissible to humans. In recent years, several novel TSEs in sheep, cattle and deer have been described and the risk posed to humans by these agents is currently unknown. In this study, we inoculated two forms of atypical BSE (BASE and H-type BSE), a chronic wasting disease (CWD) isolate and seven isolates of atypical scrapie into gene-targeted transgenic (Tg) mice expressing the human prion protein (PrP). Upon challenge with these ruminant TSEs, gene-targeted Tg mice expressing human PrP did not show any signs of disease pathology. These data strongly suggest the presence of a substantial transmission barrier between these recently identified ruminant TSEs and humans.
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Bessen, Richard A., Gregory J. Raymond, and Byron Caughey. "In SituFormation of Protease-resistant Prion Protein in Transmissible Spongiform Encephalopathy-infected Brain Slices." Journal of Biological Chemistry 272, no. 24 (June 13, 1997): 15227–31. http://dx.doi.org/10.1074/jbc.272.24.15227.
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