ArticleBMC veterinary research2013
Stability properties of PrP(Sc) from cattle with experimental transmissible spongiform encephalopathies: use of a rapid whole homogenate, protease-free assay.
Article in BMC veterinary research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Use of Agriculturally Important Animals as Models in Biomedical Research.Advances in experimental medicine and biology · 2022Review
- Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases.Viruses · 2021Review
- Novel Strain of the Chronic Wasting Disease Agent Isolated From Experimentally Inoculated Elk With LL132 Prion Protein.Scientific reports · 2020Article
- Role of donor genotype in RT-QuIC seeding activity of chronic wasting disease prions using human and bank vole substrates.PloS one · 2020Article
- Pathologic and biochemical characterization of PrPBMC veterinary research · 2018Article
- Article
- A Comparison of Classical and H-Type Bovine Spongiform Encephalopathy Associated with E211K Prion Protein Polymorphism in Wild-Type and EK211 Cattle Following Intracranial Inoculation.Frontiers in veterinary science · 2016Article
- Changes in retinal function and morphology are early clinical signs of disease in cattle with bovine spongiform encephalopathy.PloS one · 2015Article
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Authors and funding
6 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTransmissible Spongiform Encephalopathies (TSEs), including scrapie in sheep, chronic wasting disease (CWD) in cervids, transmissible mink encephalopathy (TME), and bovine spongiform encephalopathy (BSE), are fatal diseases of the nervous system associated with accumulation of misfolded prion protein (PrP(Sc)). Different strains of TSEs exist, associated with different PrP(Sc) conformations that can be probed by the stability assay, in which PrP(Sc) is treated with increasing concentrations of the denaturant guanidine hydrochloride (GdnHCl).
resultsHere, we provide the first comprehensive application of a rapid, protease-free version of the GdnHCl stability assay to brain tissue from cattle experimentally infected with various TSE isolates. Consistent with previous findings from a single Japanese isolate, the L-type isolates of BSE are not distinguishable from classical BSE in this assay. In contrast, H-type isolates of BSE, including our unique isolate of E211K BSE, exhibit higher stability than classical BSE, suggesting that its increased protection against protease digestion at the BSE N-terminus is associated with a higher stability in GdnHCl. While the difference in stability in our version of the assay is likely not large enough for effective use in a diagnostic laboratory setting, the use of alternative experimental conditions may enhance this effect. TSEs from other natural host species that have been passaged in cattle, including CWD and TME, were not distinguishable from classical BSE, while isolates of cattle passaged scrapie exhibited a slight increase in stability as compared to classical BSE.
conclusionsThese results suggest that the core of PrP(Sc), as probed in this assay, has similar stability properties among cattle-passaged TSE isolates and that the conformational differences that lead to changes in the proteinase K cleavage site do not cause large changes in the stability of PrP(Sc) from TSE-affected cattle. However, the stability differences observed here will provide a basis of comparison for new isolates of atypical BSE observed in the future and in other geographic locations, especially in the case of H-type BSE.
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