Atypical H-type bovine spongiform encephalopathy in a cow born after the reinforced feed ban on meat-and-bone meal in Europe.
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ABSTRACT:
SUBMITTER: Guldimann C
PROVIDER: S-EPMC3502978 | biostudies-literature | 2012 Dec
REPOSITORIES: biostudies-literature
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Atypical H-type bovine spongiform encephalopathy in a cow born after the reinforced feed ban on meat-and-bone meal in Europe.
Guldimann Claudia C Gsponer Michaela M Drögemüller Cord C Oevermann Anna A Seuberlich Torsten T
Journal of clinical microbiology 20121003 12
The significance of atypical bovine spongiform encephalopathies (BSE) in cattle for controlling the BSE epidemic is poorly understood. Here we report a case of atypical H-type BSE in a cow born after the implementation of the reinforced feed ban in Europe. This supports an etiology of H-type BSE unrelated to that of classical BSE. ...[more]
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Project description:BackgroundBovine spongiform encephalopathy (BSE) is an emerging zoonotic disease of cattle associated with pathological prion protein (PrPsc ) transmitted via meat and bone meal (MBM). Although Bangladesh did not experience a BSE outbreak but the country could not export animal products to developed countries as has not yet been declared BSE free country by OIE due to lack of scientific risk evaluation for BSE. The objectives were identification of hazard, release and exposure pathways of pathological prion protein through MBM and analysis of risk for the occurrence of BSE in Bangladesh.MethodsThe scientific data were reviewed, hazards were scheduled and surveys were conducted on livestock production system, import of MBM and its use to identify the hazards present in Bangladesh context. The analysis was done by the 'OIE Risk Analysis Framework 2006 and European Union (EU) Scientific Steering Committee (SSC) 2003'. From the historical reviews, import of MBM and its use was identified, as external hazards.ResultsThe analysis revealed that these hazards had negligible or moderate risk for the introduction of infectious PrPsc as Bangladeshi cattle are vegetarian cattle. No milk replacer was used and use of slaughtered waste in the animal feed industry is absent. Unconsumable bones are processed to produce bone chips, fertilizers and bone meal for poultry feeds. Scrapie was never prevalent in Bangladesh. Therefore, risk from the internal challenge was negligible in Bangladesh for the occurrence of classical BSE. These prevented the propagation of BSE infectivity and eliminated BSE infectivity from the system very fast, if that was present.ConclusionsIt was concluded that introduction of PrPsc into cattle population of Bangladesh through MBM was very negligible. Therefore, Bangladesh can be considered as BSE negligible risk country.
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Project description:The molecular events at the basis of prion diseases are characterized by the involvement of several genes which are differentially regulated during the onset and the progression of the infection. Gene expression profiling studies are a powerful tool for the development of preclinical diagnostic tests. Most of the studies performed up to date utilized tissues which are not suitable for a future perspective of a rapid analysis of the infected animals and patients. We used microarrays to identify the differentially regulated transcripts in blood of BSE-infected cattle in both the presymtomatic and the symptomatic stage of the infection. The identified genes may be used as a signature for prion diseases.
2016-04-19 | GSE69048 | GEO
Project description:The H-type of atypical bovine spongiform encephalopathy (H-BSE) was serially passaged in bovinized transgenic (TgBoPrP) mice. At the fourth passage, most challenged mice showed a typical H-BSE phenotype with incubation periods of 223 ± 7.8 days. However, a different phenotype of BSE prion with shorter incubation periods of 109 ± 4 days emerged in a minor subset of the inoculated mice. The latter showed distinct clinical signs, brain pathology, and abnormal prion protein profiles as compared to H-BSE and other known BSE strains in mice. This novel prion was transmitted intracerebrally to cattle, with incubation periods of 14.8 ± 1.5 months, with phenotypes that differed from those of other bovine prion strains. These data suggest that intraspecies transmission of H-BSE in cattle allows the emergence of a novel BSE strain. Therefore, the continuation of feed ban programs may be necessary to exclude the recycling of H-BSE prions, which appear to arise spontaneously, in livestock. Such measures should help to reduce the risks from both novel and known strains of BSE.
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Project description:Bovine spongiform encephalopathy (BSE) is a prion disease in cattle and is classified into the classical type (C-BSE) and two atypical BSEs, designated as high type (H-BSE) and low type (L-BSE). These classifications are based on the electrophoretic migration of the proteinase K-resistant core (PrPres) of the disease-associated form of the prion protein (PrPd). In a previous study, we succeeded in transmitting the H-BSE prion from cattle to TgHaNSE mice overexpressing normal hamster cellular PrP (PrPC). Further, Western blot analysis demonstrated that PrPres banding patterns of the H-BSE prion were indistinguishable from those of the C-BSE prion in TgHaNSE mice. In addition, similar PrPres glycoprofiles were detected among H-, C-, and L-BSE prions in TgHaNSE mice. Therefore, to better understand atypical BSE prions after interspecies transmission, H-BSE prion transmission from TgHaNSE mice to hamsters was investigated, and the characteristics of classical and atypical BSE prions among hamsters, wild-type mice, and mice overexpressing bovine PrPC (TgBoPrP) were compared in this study using biochemical and neuropathological methods. Identical PrPres banding patterns were confirmed between TgHaNSE mice and hamsters in the case of all three BSE prion strains. However, these PrPres banding patterns differed from those of TgBoPrP and wild-type mice infected with the H-BSE prion. In addition, glycoprofiles of TgHaNSE mice and hamsters infected with the L-BSE prion differed from those of TgBoPrP mice infected with the L-BSE prion. These data indicate that the PrPC amino acid sequences of new host species rather than other host environmental factors may affect some molecular aspects of atypical BSE prions. Although three BSE prion strains were distinguishable based on the neuropathological features in hamsters, interspecies transmission modified some molecular properties of atypical BSE prions, and these properties were indistinguishable from those of C-BSE prions in hamsters. Taken together, PrPres banding patterns and glycoprofiles are considered to be key factors for BSE strain typing. However, this study also revealed that interspecies transmission could sometimes influence these characteristics.
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