Omer-Ali P, Magee A I, Kelly C, Simpson A J
J Immunol. 1986 Dec 1;137(11):3601-7.
A radioimmunoassay that makes use of whole schistosomula and 125I-labeled protein A has been used to characterize and to quantify the binding of antisera to the surface of 3 hr mechanically transformed schistosomula of Schistosoma mansoni. This technique facilitates the determination of epitopes on the schistosomula in addition to those detected by surface labeling and immunoprecipitation. By using this technique, it has been demonstrated that there is a much greater binding to the parasite surface of antibodies from chronically infected mice (CMS) than of antibodies from mice infected with highly irradiated cercariae (VMS), and CMS recognizes epitopes that VMS does not. Treatment of the surface of the schistosomula with trifluoromethanesulphonic acid and sodium metaperiodate has suggested that the discrepancy of the binding between the two sera is due to the recognition of a large number of additional epitopes by CMS, which are carbohydrate in nature. Some of the carbohydrate epitopes are expressed on the previously described surface glycoprotein antigens of Mr 200,000, 38,000, and 17,000.
一种利用完整的童虫和125I标记的蛋白A的放射免疫分析法,已被用于鉴定和定量抗血清与曼氏血吸虫3小时机械转化童虫表面的结合。除了通过表面标记和免疫沉淀检测到的表位外,该技术有助于确定童虫上的表位。通过使用该技术,已证明慢性感染小鼠(CMS)的抗体与寄生虫表面的结合比高度照射尾蚴感染小鼠(VMS)的抗体更强,并且CMS识别VMS不识别的表位。用三氟甲磺酸和偏高碘酸钠处理童虫表面表明,两种血清结合的差异是由于CMS识别了大量额外的表位,这些表位本质上是碳水化合物。一些碳水化合物表位在先前描述的分子量为200,000、38,000和17,000的表面糖蛋白抗原上表达。