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杜氏利什曼原虫前鞭毛体的表面抗原

Surface antigens of Leishmania donovani promastigotes.

作者信息

Lepay D A, Nogueira N, Cohn Z

出版信息

J Exp Med. 1983 May 1;157(5):1562-72. doi: 10.1084/jem.157.5.1562.

Abstract

Surface antigen profiles of Leishmania donovani promastigote isolates have been studied. Surface patterns of Brazilian and African isolates display remarkable similarities and are extremely simple, consisting of three major peptides of 65,000, 25,000, and 23,000 mol wt. Surface iodination and biosynthetic labeling coupled to immunoprecipitation techniques revealed that a single major determinant of 65,000 mol wt is recognized in all strains by sera from kala-azar patients from both Brazil and Africa. This major determinant is not brought down by sera from normal individuals and shows no significant cross-reactivity with sera from Chagas' disease, leprosy, or syphilis patients. Binding to concanavalin A suggests a glycoprotein nature for this antigen. Sera from patients with cutaneous leishmaniasis (L. braziliensis) also recognized the same 65,000-mol wt determinant, although to a lesser extent. The possibility that this major surface antigen is shared, with minor differences, not only by L. donovani strains but between Leishmania species in general is suggested.

摘要

已对杜氏利什曼原虫前鞭毛体分离株的表面抗原谱进行了研究。巴西和非洲分离株的表面模式显示出显著的相似性,且极其简单,由分子量为65,000、25,000和23,000的三种主要肽组成。表面碘化和生物合成标记与免疫沉淀技术相结合表明,来自巴西和非洲黑热病患者的血清在所有菌株中均识别出一种分子量为65,000的单一主要决定簇。这种主要决定簇不会被正常个体的血清沉淀,并且与恰加斯病、麻风病或梅毒患者的血清无明显交叉反应。与伴刀豆球蛋白A的结合表明该抗原具有糖蛋白性质。皮肤利什曼病(巴西利什曼原虫)患者的血清也识别相同的分子量为65,000的决定簇,尽管程度较低。这表明这种主要表面抗原不仅在杜氏利什曼原虫菌株之间,而且在一般的利什曼原虫物种之间可能存在共享,只是存在微小差异。

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