NDLI: Digestion and transportation of bovine spongiform encephalopathy-derived prion protein in the sheep intestine.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dagleish, Mark P. Hamilton, Scott González, Lorenzo Eaton, Samantha L. Steele, Philip Finlayson, Jeanie Sisó, Sílvia Pang, Yvonne Sales, Jill Chianini, Francesca Jeffrey, Martin
Description	Country affiliation: United kingdom Author Affiliation: Dagleish MP ( Moredun Research Institute, Pentlands Science Park, Bush Loan, Penicuik, Midlothian EH26 0PZ, UK.)
Abstract	Bovine spongiform encephalopathy (BSE) is acquired orally and the mechanisms involved in the absorption and transportation of infectivity across the gut wall are therefore critical. Isolated gut loops were created in lambs, massaged to remove intestinal contents (flushed) or left non-flushed, inoculated with cattle BSE homogenate and excised at different time-points. Gut loops were examined by immunohistochemistry (IHC) for disease-associated prion protein (PrP(d)), and the contents were analysed by Western blotting (WB) to determine the degradation rate of protease-resistant PrP (PrP(res)). The contents of scrapie-inoculated gut loops from a previous experiment were analysed by WB, and these in vivo digestion results were compared with those of an in vitro experiment on the same transmissible spongiform encephalopathy homogenates. BSE-inoculum-derived PrP(d) was detected by IHC in the gut lumen between 15 min and 3.5 h. It was found in the intestinal lymphatic system from 30 min onwards and was present at the highest frequency at 120 min post-inoculation. In vivo degradation of PrP(res) in the BSE inoculum had a significantly (P=0.006) different pattern compared with scrapie-derived PrP(res), with the BSE PrP(res) degrading more rapidly. However, the overall amount of degradation became similar by 120 min post-challenge. The results of the in vitro digestion experiments showed a similar pattern, although the magnitude of PrP(res) degradation was less than in the in vivo environment where absorption could also take place. BSE-derived PrP(res) is less protease resistant than scrapie PrP over a short time-course and the disappearance of detectable PrP(res) from the gut lumen results from both absorption and digestion by intestinal contents.
File Format	HTM / HTML
ISSN	00221317
Issue Number	Pt 12
Volume Number	91
e-ISSN	14652099
Journal	Journal of General Virology
Language	English
Publisher	Microbiology Society
Publisher Date	2010-12-01
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Immunohistochemistry Research Support, Non-u.s. Gov't Intestines Discipline Virology Transmission Sheep Diseases Metabolism Blotting, Western Journal Article Protein Transport Pathology Animals Cattle Prions Sheep Encephalopathy, Bovine Spongiform
Content Type	Text
Resource Type	Article
Subject	Virology

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