scholarly journals Molecular Analysis of Cases of Italian Sheep Scrapie and Comparison with Cases of Bovine Spongiform Encephalopathy (BSE) and Experimental BSE in Sheep

2003 ◽  
Vol 41 (9) ◽  
pp. 4127-4133 ◽  
Author(s):  
R. Nonno ◽  
E. Esposito ◽  
G. Vaccari ◽  
M. Conte ◽  
S. Marcon ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Molecular Analysis ◽  
Spongiform Encephalopathy ◽  
Analysis Of Cases ◽  
Sheep Scrapie

scholarly journals Resistance of Domestic Cats to a US Sheep Scrapie Agent by Intracerebral Route

2002 ◽  
Vol 14 (5) ◽  
pp. 444-445 ◽  
Author(s):  
Amir N. Hamir ◽  
Wilber W. Clark ◽  
Diane L. Sutton ◽  
Janice M. Miller ◽  
Mick J. Stack ◽  
...  
Keyword(s):  
Western Blot ◽  
Bovine Spongiform Encephalopathy ◽  
Extended Period ◽  
Spongiform Encephalopathy ◽  
Neurologic Disease ◽  
Domestic Cats ◽  
Species Barrier ◽  
Scrapie Agent ◽  
Abnormal Form ◽  
Sheep Scrapie

Feline spongiform encephalopathy (FSE) is thought to have resulted from consumption of food contaminated with bovine spongiform encephalopathy and the latter is believed to result from the consumption of food contaminated with scrapie. However, no direct experimental documentation exists to indicate that the scrapie agent is capable of amplifying in cats, and, therefore, crossing the species barrier. During 1979, 6 cats ranging in age from 3.5 to 18 months were intracerebrally inoculated with sheep scrapie (inoculum G-639-PP) and were observed for an extended period. Inoculated cats did not develop neurologic disease, and microscopic lesions of spongiform encephalopathy were not evident. Immunohistochemistry and Western blot techniques failed to detect the abnormal form of prion protein (PrPres). These results indicate that the sheep scrapie agent (G-639-PP) used in this study was not capable of amplifying in cats and therefore was unable to cross the species barrier to produce FSE.

The neuropathologic phenotype of experimental ovine BSE is maintained after blood transfusion

Blood ◽  
2006 ◽  
Vol 108 (2) ◽  
pp. 745-748 ◽  
Author(s):  
Sílvia Sisó ◽  
Lorenzo González ◽  
Fiona Houston ◽  
Nora Hunter ◽  
Stuart Martin ◽  
...  
Keyword(s):  
Blood Transfusion ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Diseases ◽  
Spongiform Encephalopathy ◽  
Neurologic Disease ◽  
Infected Blood ◽  
Route Of Infection ◽  
Jakob Disease ◽  
Iatrogenic Transmission ◽  
Sheep Scrapie

Iatrogenic transmission by blood transfusion has been described in cases of human variant Creutzfeldt-Jakob disease (vCJD), experimental ovine bovine spongiform encephalopathy (BSE), and natural sheep scrapie, demonstrating that blood in these prion diseases is infectious. However, the possible effect of the transfusion, derived from differences in the inoculum (blood) and the route of infection (intravenous), on the pathologic phenotype of the disease in the recipients is not known. This study describes the neuropathologic phenotype of PrPd accumulation in sheep succumbing to neurologic disease after blood transfusion from donors experimentally infected with BSE; these were either clinically or subclinically affected at the time of donation. We demonstrate that blood can become infectious at early stages of ovine BSE infection and that the PrPd immunohistochemical phenotype is maintained after transfusion. This suggests that a change in the pathologic phenotype of vCJD would not be expected as a result of exposure to infected blood.

scholarly journals Three serial passages of bovine spongiform encephalopathy in sheep do not significantly affect discriminatory test results

2009 ◽  
Vol 90 (3) ◽  
pp. 764-768 ◽  
Author(s):  
Michael Stack ◽  
Lorenzo González ◽  
Martin Jeffrey ◽  
Stuart Martin ◽  
Colin Macaldowie ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Proteins ◽  
Oral Exposure ◽  
Spongiform Encephalopathy ◽  
Test Results ◽  
Western Immunoblotting ◽  
Jakob Disease ◽  
Disease Variant ◽  
The Uk ◽  
Sheep Scrapie

During the 1980s, bovine spongiform encephalopathy (BSE)-contaminated meat and bonemeal were probably fed to sheep, raising concerns that BSE may have been transmitted to sheep in the UK. The human disease, variant Creutzfeldt–Jakob disease, arose during the BSE epidemic, and oral exposure of humans to BSE-infected tissues has been implicated in its aetiology. The concern is that sheep BSE could provide another source of BSE exposure to humans via sheep products. Two immunological techniques, Western immunoblotting (WB) and immunohistochemistry (IHC), have been developed to distinguish scrapie from cases of experimental sheep BSE by the characteristics of their respective abnormal, disease-associated prion proteins (PrPd). This study compares the WB and IHC characteristics of PrPd from brains of primary, secondary and tertiary experimental ovine BSE cases with those of cattle BSE and natural sheep scrapie. Discrimination between experimental sheep BSE and scrapie remained possible by both methods, regardless of the route of challenge.

scholarly journals Comparative Molecular Analysis of the Abnormal Prion Protein in Field Scrapie Cases and Experimental Bovine Spongiform Encephalopathy in Sheep by Use of Western Blotting and Immunohistochemical Methods

2004 ◽  
Vol 78 (7) ◽  
pp. 3654-3662 ◽  
Author(s):  
Stéphane Lezmi ◽  
Stuart Martin ◽  
Stéphanie Simon ◽  
Emmanuel Comoy ◽  
Anna Bencsik ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Western Blotting ◽  
Molecular Analysis ◽  
Infected Sheep ◽  
Enzyme Linked Immunosorbent Assay ◽  
Spongiform Encephalopathy ◽  
Protease Cleavage ◽  
Two Samples ◽  
Immunohistochemical Methods

ABSTRACT Since the appearance of bovine spongiform encephalopathy (BSE) in cattle and its linkage with the human variant of Creutzfeldt-Jakob disease, the possible spread of this agent to sheep flocks has been of concern as a potential new source of contamination. Molecular analysis of the protease cleavage of the abnormal prion protein (PrP), by Western blotting (PrPres) or by immunohistochemical methods (PrPd), has shown some potential to distinguish BSE and scrapie in sheep. Using a newly developed enzyme-linked immunosorbent assay, we identified 18 infected sheep in which PrPres showed an increased sensitivity to proteinase K digestion. When analyzed by Western blotting, two of them showed a low molecular mass of unglycosylated PrPres as found in BSE-infected sheep, in contrast to other naturally infected sheep. A decrease of the labeling by P4 monoclonal antibody, which recognizes an epitope close to the protease cleavage site, was also found by Western blotting in the former two samples, but this was less marked than in BSE-infected sheep. These two samples, and all of the other natural scrapie cases studied, were clearly distinguishable from those from sheep inoculated with the BSE agent from either French or British cattle by immunohistochemical analysis of PrPd labeling in the brain and lymphoid tissues. Final characterization of the strain involved in these samples will require analysis of the features of the disease following infection of mice, but our data already emphasize the need to use the different available methods to define the molecular properties of abnormal PrP and its possible similarities with the BSE agent.

scholarly journals Sheep-Passaged Bovine Spongiform Encephalopathy Agent Exhibits Altered Pathobiological Properties in Bovine-PrP Transgenic Mice

2006 ◽  
Vol 81 (2) ◽  
pp. 835-843 ◽  
Author(s):  
Juan Carlos Espinosa ◽  
Olivier Andréoletti ◽  
Joaquín Castilla ◽  
María Eugenia Herva ◽  
Mónica Morales ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Clinical Signs ◽  
Health Concern ◽  
Mouse Bioassay ◽  
Spongiform Encephalopathy ◽  
Species Barrier ◽  
Subsequent Passage ◽  
Sheep Scrapie ◽  
Cattle And Sheep ◽  
Transmission Barrier

ABSTRACT Sheep can be experimentally infected with bovine spongiform encephalopathy (BSE), and the ensuing disease is similar to scrapie in terms of pathogenesis and clinical signs. BSE infection in sheep is an animal and human health concern. In this study, the transmission in BoPrP-Tg110 mice of prions from BSE-infected sheep was examined and compared to the transmission of original cattle BSE in cattle and sheep scrapie prions. Our results indicate no transmission barrier for sheep BSE prions to infect BoPrP-Tg110 mice, but the course of the disease is accelerated compared to the effects of the original BSE isolate. The shortened incubation period of sheep BSE in the model was conserved in subsequent passage in BoPrP-Tg110 mice, indicating that it is not related to infectious titer differences. Biochemical signature, lesion profile, and PrPSc deposition pattern of both cattle and sheep BSE were similar. In contrast, all three sheep scrapie isolates tested showed an evident transmission barrier and further adaptation in subsequent passage. Taken together, those data indicate that BSE agent can be altered by crossing a species barrier, raising concerns about the virulence of this new prion towards other species, including humans. The BoPrP-Tg110 mouse bioassay should be considered as a valuable tool for discriminating scrapie and BSE in sheep.

scholarly journals Molecular Analysis of the Abnormal Prion Protein during Coinfection of Mice by Bovine Spongiform Encephalopathy and a Scrapie Agent

2001 ◽  
Vol 75 (1) ◽  
pp. 107-114 ◽  
Author(s):  
Thierry G. M. Baron ◽  
Anne-Gaelle Biacabe
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Proteinase K ◽  
Spongiform Encephalopathy ◽  
Molecular Features ◽  
Electrophoretic Mobilities ◽  
Scrapie Agent ◽  
Scrapie Strain ◽  
Sheep Scrapie

ABSTRACT Molecular features of the proteinase K-resistant prion protein (PrP res) may discriminate among prion strains, and a specific signature could be found during infection by the infectious agent causing bovine spongiform encephalopathy (BSE). To investigate the molecular basis of BSE adaptation and selection, we established a model of coinfection of mice by both BSE and a sheep scrapie strain (C506M3). We now show that the PrP res features in these mice, characterized by glycoform ratios and electrophoretic mobilities, may be undistinguishable from those found in mice infected with scrapie only, including when mice were inoculated by both strains at the same time and by the same intracerebral inoculation route. Western blot analysis using different antibodies against sequences near the putative N-terminal end of PrP res also demonstrated differences in the main proteinase K cleavage sites between mice showing either the BSE or scrapie PrP res profile. These results, which may be linked to higher levels of PrP res associated with infection by scrapie, were similar following a challenge by a higher dose of the BSE agent during coinfection by both strains intracerebrally. Whereas PrP res extraction methods used allowed us to distinguish type 1 and type 2 PrP res, differing, like BSE and scrapie, by their electrophoretic mobilities, in the same brain region of some patients with Creutzfeldt-Jakob disease, analysis of in vitro mixtures of BSE and scrapie brain homogenates did not allow us to distinguish BSE and scrapie PrP res. These results suggest that the BSE agent, the origin of which remains unknown so far but which may have arisen from a sheep scrapie agent, may be hidden by a scrapie strain during attempts to identify it by molecular studies and following transmission of the disease in mice.

An epidemiologist’s view of bovine spongiform encephalopathy

1994 ◽  
Vol 343 (1306) ◽  
pp. 357-361 ◽  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Spongiform Encephalopathy ◽  
Meat And Bone Meal ◽  
Bone Meal ◽  
Original Source ◽  
Hydrocarbon Solvents ◽  
Epidemiological Features ◽  
Food Borne ◽  
Means Of Transmission ◽  
Sheep Scrapie

Bovine spongiform encephalopathy was first recognized in Great Britain in 1986 and was the result of infection with a scrapie-like agent surviving in m eat and bone meal used in feedstuffs. This effective exposure commenced in 1981-82 and was associated with a reduction in the use of hydrocarbon solvents in the manufacture of meat and bone meal. The epidemiological features are consistent with sheep scrapie as the original source, but the epidemic was amplified by the recycling of infected cattle tissue resulting in a marked increase in incidence from 1989. The food borne source was eliminated by legislation introduced in July 1988. The first effects of this became apparent during 1991 and these have become more obvious during 1993 with a reduction in the national incidence. Specific studies are still in progress to determine whether other means of transmission can occur, but none capable of maintaining the epidemic have been detected.

PRÍONS E DOENÇAS PRIÔNICAS: UMA REVISÃO

2020 ◽  
Vol 12 (2) ◽  
pp. 47-58
Author(s):  
Vinicio Berti
Keyword(s):  
Systematic Review ◽  
Bovine Spongiform Encephalopathy ◽  
Neurodegenerative Disorders ◽  
Spongiform Encephalopathy ◽  
General View ◽  
Chain Reaction ◽  
Wasting Disease ◽  
Jakob Disease ◽  
Altered Form ◽  
Sheep Scrapie

The name príon is given to an altered form of a protein present at the surface of neurons. Prions are remarkable for been able to induct their normal counterpart to assume the pathological configuration on a kind of chain reaction, with the possibility of trasmission between subjects and even through different species. Prions can cause a series of neurodegenerative disorders affecting humans (Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, kuru), and animals such cattle (bovine spongiform encephalopathy or “mad cow disease”), deer (chronic wasting disease) and sheep (scrapie). This article is a non-systematic review, obtained on PubMed, SciELO and Google Scholar databases, with the aim to give a general view about the nature of prions, followed by a brief discussion of the human diseases caused by prions.

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