a c-terminal protease-resistant prion fragment distinguishes ovine “ch1641-like” scrapie from bovine classical and l-type bse in ovine transgenic micec端protease-resistant朊病毒片段区分绵羊的u201cch1641-likeu201d痒病牛古典和l型疯牛病在绵羊的转基因小鼠.pdfVIP

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a c-terminal protease-resistant prion fragment distinguishes ovine “ch1641-like” scrapie from bovine classical and l-type bse in ovine transgenic micec端protease-resistant朊病毒片段区分绵羊的u201cch1641-likeu201d痒病牛古典和l型疯牛病在绵羊的转基因小鼠.pdf

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a c-terminal protease-resistant prion fragment distinguishes ovine “ch1641-like” scrapie from bovine classical and l-type bse in ovine transgenic micec端protease-resistant朊病毒片段区分绵羊的u201cch1641-likeu201d痒病牛古典和l型疯牛病在绵羊的转基因小鼠

A C-Terminal Protease-Resistant Prion Fragment Distinguishes Ovine ‘‘CH1641-Like’’ Scrapie from Bovine Classical and L-Type BSE in Ovine Transgenic Mice ¨ ´ ´ Thierry Baron*, Anna Bencsik, Johann Vulin, Anne-Gaelle Biacabe, Eric Morignat, Jeremy Verchere, Dominique Betemps ´ ´ ´ Agence Franc¸aise de Securite Sanitaire des Aliments–Lyon, Unite ATNC, Lyon, France Abstract The protease-resistant prion protein (PrPres) 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 PrPres 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 PrPres than in classical BSE, but similar glycoform proportions and apparent molecular masses of the usual PrPres form (PrPres #1) to L-type BSE. However, the ‘‘CH1641-like’’ isolates differed from both L-type and classical BSE by an abundant, C-terminally cleaved PrPres product (PrPres #2) specifically recognised by a C-terminal antibody (SAF84). Differential immunoprecipitation of PrPres #1 and PrPres #2 resulted in enrichment in PrPres #2, and demonstrated the presence of mono- and diglycosylated PrPres products. PrPres