ArticlePLoS pathogens2008
A C-terminal protease-resistant prion fragment distinguishes ovine "CH1641-like" scrapie from bovine classical and L-Type BSE in ovine transgenic mice.
Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- Conventional and State-of-the-Art Detection Methods of Bovine Spongiform Encephalopathy (BSE).International journal of molecular sciences · 2023Review
- Chronic wasting disease in Europe: new strains on the horizon.Acta veterinaria Scandinavica · 2021Review
- Host prion protein expression levels impact prion tropism for the spleen.PLoS pathogens · 2020Article
- Novel Type of Chronic Wasting Disease Detected in Moose (Alces alces), Norway.Emerging infectious diseases · 2018Article
- Interspecies transmission to bovinized transgenic mice uncovers new features of a CH1641-like scrapie isolate.Veterinary research · 2018Article
- New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.The American journal of pathology · 2016Article
- Stability of murine scrapie strain 87V after passage in sheep and comparison with the CH1641 ovine strain.The Journal of general virology · 2015Article
- Two alternative pathways for generating transmissible prion disease de novo.Acta neuropathologica communications · 2015Article
- The diversity and relationship of prion protein self-replicating states.Virus research · 2015Review
- Further characterisation of transmissible spongiform encephalopathy phenotypes after inoculation of cattle with two temporally separated sources of sheep scrapie from Great Britain.BMC research notes · 2015Article
- Phenotype shift from atypical scrapie to CH1641 following experimental transmission in sheep.PloS one · 2015Article
- Highly sensitive detection of small ruminant bovine spongiform encephalopathy within transmissible spongiform encephalopathy mixes by serial protein misfolding cyclic amplification.Journal of clinical microbiology · 2014Article
- Sheep prions with molecular properties intermediate between classical scrapie, BSE and CH1641-scrapie.Prion · 2014Article
- Prion protein-specific antibodies that detect multiple TSE agents with high sensitivity.PloS one · 2014Article
- Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles.The American journal of pathology · 2013Article
- Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.The Journal of biological chemistry · 2013Article
- Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.International journal of cell biology · 2013Review
- Differentiating ovine BSE from CH1641 scrapie by serial protein misfolding cyclic amplification.Molecular biotechnology · 2012Article
- A new mechanism for transmissible prion diseases.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Transmissibility of caprine scrapie in ovine transgenic mice.BMC veterinary research · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protease-resistant prion protein (PrP(res)) of a few natural scrapie isolates identified in sheep, reminiscent of the experimental isolate CH1641 derived from a British natural scrapie case, showed partial molecular similarities to ovine bovine spongiform encephalopathy (BSE). Recent discovery of an atypical form of BSE in cattle, L-type BSE or BASE, suggests that also this form of BSE might have been transmitted to sheep. We studied by Western blot the molecular features of PrP(res) in four "CH1641-like" natural scrapie isolates after transmission in an ovine transgenic model (TgOvPrP4), to see if "CH1641-like" isolates might be linked to L-type BSE. We found less diglycosylated PrP(res) than in classical BSE, but similar glycoform proportions and apparent molecular masses of the usual PrP(res) form (PrP(res) #1) to L-type BSE. However, the "CH1641-like" isolates differed from both L-type and classical BSE by an abundant, C-terminally cleaved PrP(res) product (PrP(res) #2) specifically recognised by a C-terminal antibody (SAF84). Differential immunoprecipitation of PrP(res) #1 and PrP(res) #2 resulted in enrichment in PrP(res) #2, and demonstrated the presence of mono- and diglycosylated PrP(res) products. PrP(res) #2 could not be obtained from several experimental scrapie sources (SSBP1, 79A, Chandler, C506M3) in TgOvPrP4 mice, but was identified in the 87V scrapie strain and, in lower and variable proportions, in 5 of 5 natural scrapie isolates with different molecular features to CH1641. PrP(res) #2 identification provides an additional method for the molecular discrimination of prion strains, and demonstrates differences between "CH1641-like" ovine scrapie and bovine L-type BSE transmitted in an ovine transgenic mouse model.
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