Prusiner S B, Füzi M, Scott M, Serban D, Serban H, Taraboulos A, Gabriel J M, Wells G A, Wilesmith J W, Bradley R
Department of Neurology, Biochemistry and Biophysics, and Pathology, University of California, San Francisco 94143-0518.
J Infect Dis. 1993 Mar;167(3):602-13. doi: 10.1093/infdis/167.3.602.
Bovine spongiform encephalopathy (BSE) is a transmissible neurodegenerative disease. Six brain regions from 11 cattle were examined for the presence of the abnormal isoform of the prion protein (PrPBSE). The highest concentrations of PrPBSE were found in the brain stem, where the greatest degree of spongiform change was observed. Molecular cloning of the bovine PrP gene showed that it encodes a protein of 256 or 264 amino acids with five or six Gly:Pro-rich octarepeats, respectively, in contrast to all other mammalian PrP genes, which encode only five octarepeats. The bovine PrP gene is single copy, and the entire open-reading frame lies within a single exon. Since the transmission of prions across species seems to be restricted by differences in PrP sequence, the high degree of homology between sheep and bovine PrP (98%) correlates with the proposed cause of BSE.
牛海绵状脑病（BSE）是一种可传播的神经退行性疾病。对11头牛的六个脑区进行了检查，以确定是否存在朊病毒蛋白异常异构体（PrPBSE）。在脑干中发现了最高浓度的PrPBSE，在那里观察到了最大程度的海绵状变化。牛PrP基因的分子克隆表明，它编码一种由256或264个氨基酸组成的蛋白质，分别具有五个或六个富含Gly:Pro的八肽重复序列，这与所有其他仅编码五个八肽重复序列的哺乳动物PrP基因形成对比。牛PrP基因是单拷贝的，整个开放阅读框位于一个外显子内。由于朊病毒跨物种传播似乎受到PrP序列差异的限制，绵羊和牛PrP之间的高度同源性（98%）与BSE的推测病因相关。
