Takahashi H, Takahashi R H, Hasegawa H, Horiuchi M, Shinagawa M, Yokoyama T, Kimura K, Haritani M, Kurata T, Nagashima K
Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
J Neurovirol. 1999 Jun;5(3):300-7. doi: 10.3109/13550289909015816.
To analyze the antigenicity of peptides derived from bovine prion protein (PrP) cDNA, we immunized rabbits with four synthetic peptides and compared the immunoreactivity of antibodies to PrPs from various species by immunoblotting and immunohistochemistry. Two of the antibodies reacted strongly with all PrPs. The other antibodies, raised against overlapping peptides close to two glycosylation sites, did not recognize PrPSc-mouse but did recognize PrPSc-sheep which contains two sugar residues and PrPCJD with or without a sugar residue. Our results suggest that these antibodies may have species-specificity for both glycosylation status and amino acid sequences of the protein. In conclusion, we identified two regions in bovine-PrP which appear suitable for raising antibodies that detect various kinds of PrPs, and one region (Ab103-121) which appears suitable for raising antibodies that detect several species of PrPs. These antibodies may be useful for diagnosing prion diseases and for researching their pathogenesis.
为分析源自牛朊蛋白（PrP）cDNA的肽段的抗原性，我们用四种合成肽免疫兔子，并通过免疫印迹和免疫组织化学比较了针对来自不同物种的PrP的抗体的免疫反应性。其中两种抗体与所有PrP都发生强烈反应。另外两种针对靠近两个糖基化位点的重叠肽产生的抗体，不识别PrPSc - 小鼠，但能识别含有两个糖残基的PrPSc - 绵羊以及有或无糖残基的PrPCJD。我们的结果表明，这些抗体可能对该蛋白的糖基化状态和氨基酸序列具有物种特异性。总之，我们在牛PrP中鉴定出两个似乎适合产生能检测各种PrP的抗体的区域，以及一个似乎适合产生能检测几种物种的PrP的抗体的区域（Ab103 - 121）。这些抗体可能有助于诊断朊病毒疾病及其发病机制的研究。
