کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2438388 | 1107713 | 2010 | 11 صفحه PDF | دانلود رایگان |
SummaryScrapie is the transmissible spongiform encephalopathy (TSE) that naturally affects sheep and goats; these species are also susceptible to experimental infection with the bovine spongiform encephalopathy (BSE) agent. Discrimination between different strains of sheep scrapie and ovine BSE has been achieved by descriptive and quantitative profiling of deposits of the disease-associated prion protein (PrPd) in different areas of the brain, but this process is time-consuming and difficult to standardize between laboratories. The present paper describes an alternative PrPd profiling method that is less demanding and addresses these difficulties. It is based on the scoring of similar 14 PrPd types in 11 precisely defined areas of the telencephalon. When applied to 48 archived cases of experimental sheep BSE, SSBP/1, CH1641 and natural scrapie, it gave comparable results to the original profiling method, previously conducted on the same brains, and allowed differentiation between the different infectious sources. This new ‘short PrPd profiling’ method has the advantages of being less time-consuming and easier to standardize, so that it can be readily adopted by different laboratories to provide comparable results.
Journal: Journal of Comparative Pathology - Volume 142, Issue 4, May 2010, Pages 300–310