Oesch B, Doherr M, Heim D, Fischer K, Egli S, Bolliger S, Biffiger K, Schaller O, Vandevelde M, Moser M
Prionics AG, University of Zürich, Switzerland.
Arch Virol Suppl. 2000(16):189-95. doi: 10.1007/978-3-7091-6308-5_18.
Disease-specific PrP (PrP(Sc)) is at least part of the infectious particle (prion) causing bovine spongiform encephalopathy (BSE) or scrapie in sheep. Digestion with protease allows a distinction between normal PrP (PrP(C)) and PrP(Sc) i.e. PrP(C) is completely digested while PrP(Sc) is cleaved at the N-terminus leading to a fragment of reduced molecular weight (PrP 27-30). Detection of this fragment by Western blotting has been described more than a decade ago for rodent PrP. We have now optimized the technique in order to allow rapid analysis of hundreds of samples per day. Here we report the application of this technique to the analysis of 3000 regularly slaughtered cattle from Swiss abattoirs. For comparison all the animals were subsequently examined by classical methods (i.e. histology and immunohistochemistry). All but one animal were negative for BSE by all methods. The Western blot positive animal was confirmed to be a BSE case and the carcass was removed from the food chain. We conclude that it is feasible to examine slaughtered cattle on a routine basis without causing delays to the meat processing industry.
疾病特异性朊蛋白（PrP(Sc)）至少是导致牛海绵状脑病（BSE）或绵羊瘙痒病的感染性颗粒（朊病毒）的一部分。用蛋白酶消化可区分正常朊蛋白（PrP(C)）和PrP(Sc)，即PrP(C)被完全消化，而PrP(Sc)在N端被切割，产生分子量降低的片段（PrP 27-30）。十多年前就已描述通过蛋白质印迹法检测该片段用于啮齿动物朊蛋白。我们现在对该技术进行了优化，以便每天能够快速分析数百个样本。在此我们报告该技术在分析来自瑞士屠宰场的3000头定期屠宰牛中的应用。为作比较，随后所有动物均通过经典方法（即组织学和免疫组织化学）进行检查。除一头动物外，所有动物经所有方法检测均为BSE阴性。蛋白质印迹法阳性的动物被确认为BSE病例，其 carcass 被从食物链中移除。我们得出结论，对屠宰牛进行常规检查且不延误肉类加工业是可行的。 （注：原文中“carcass”直接保留未翻译，可能是特定语境下的专业术语，此处可根据实际情况进一步准确翻译，比如“胴体”等。）
