Bendheim P E, Barry R A, DeArmond S J, Stites D P, Prusiner S B
Nature. 1984;310(5976):418-21. doi: 10.1038/310418a0.
Scrapie is a slow infection of the nervous system which progresses in the absence of any apparent immune response. The recent development of a large-scale purification protocol for scrapie prions made it possible to obtain substantial quantities of electrophoretically purified prion protein (PrP 27-30) and we report here on the successful production of a rabbit antiserum to PrP 27-30. The antiserum reacted with PrP 27-30 and several lower molecular weight proteins as shown by Western blots; it did not react with protein preparations from uninfected brains. Discrete structures in the subependymal region of scrapie-infected hamster brains were stained immunocytochemically. These same structures also stained with Congo red dye and showed green birefringence with polarized light, a characteristic of purified prion rods. This staining pattern suggests that they are amyloid plaques.
羊瘙痒症是一种神经系统的缓慢感染疾病，在没有任何明显免疫反应的情况下进展。最近开发的一种大规模纯化羊瘙痒症朊病毒的方案，使得获得大量经电泳纯化的朊病毒蛋白（PrP 27-30）成为可能，我们在此报告成功制备了针对PrP 27-30的兔抗血清。如免疫印迹所示，该抗血清与PrP 27-30及几种较低分子量的蛋白质发生反应；它不与未感染大脑的蛋白质制剂发生反应。羊瘙痒症感染的仓鼠脑室管膜下区域的离散结构经免疫细胞化学染色。这些相同的结构也用刚果红染料染色，并在偏振光下显示绿色双折射，这是纯化朊病毒杆的特征。这种染色模式表明它们是淀粉样斑块。
