Piccardo P, Langeveld J P, Hill A F, Dlouhy S R, Young K, Giaccone G, Rossi G, Bugiani M, Bugiani O, Meloen R H, Collinge J, Tagliavini F, Ghetti B
Indiana University School of Medicine, Indianapolis, USA.
Am J Pathol. 1998 Jun;152(6):1415-20.
Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity (from strong immunopositivity to lack of reactivity) when challenged with PrP from diverse species. We have produced an antibody (anti-PrP95-108) raised against a synthetic peptide corresponding to residues 95 to 108 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (ie, cattle, sheep, hamsters, and mice). This is probably due to the fact that the epitope recognized by this antibody includes residues 100 to 108 of human PrP, a sequence that is also present in PrP of several other species. Thus, this reagent is valuable not only for the study of human prion diseases but also for analysis of the possible relationship between human and animal disorders.
针对朊病毒蛋白（PrP）的抗体对于人类和动物中与PrP相关的退行性疾病的神经病理学和生化特征研究至关重要。尽管PrP在进化上高度保守，但不同物种之间存在一些序列差异；因此，当用来自不同物种的PrP进行检测时，抗PrP抗体具有广泛的反应性（从强免疫阳性到无反应性）。我们制备了一种针对与人PrP第95至108位残基对应的合成肽产生的抗体（抗PrP95-108），并通过表位作图、Western免疫印迹分析和免疫组织化学对其进行了表征。该抗体不仅识别人类PrP异构体，还识别所有测试物种（即牛、羊、仓鼠和小鼠）的病理性PrP。这可能是因为该抗体识别的表位包括人类PrP的第100至108位残基，该序列也存在于其他几种物种的PrP中。因此，该试剂不仅对人类朊病毒疾病的研究有价值，而且对分析人类和动物疾病之间的可能关系也有价值。
