Jaffe C L, McMahon-Pratt D
Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.
J Parasitol. 1988 Aug;74(4):548-61.
The membrane glycoconjugates of 8 different species of Leishmania were compared by lectin blotting. Five different lectins with various sugar specificities were examined: concanavalin A, Lens culinaris, Ricinus communis, soybean agglutinin, and peanut agglutinin. Concanavalin A and Lens culinaris reacted with every Leishmania tested. The patterns observed for these 2 lectins, as well as the various species of parasites, were different. However, a common 41,000-52,000 and a 160,000-185,000 Mr component was present in almost all the parasite isolates examined. Ricinus communis only recognized a nondiscrete galactose-containing glycoconjugate similar to Leishmania-excreted factor. Soybean and peanut agglutinins reacted with a few low molecular weight parasite components. Soybean agglutinin reacted with all the Leishmania species tested, whereas peanut lectin only recognized 3 isolates. The latter lectin bound to discrete components migrating with the dye front and with Mr's of 35,000 and 52,000. Increased glycosylation was noted on avirulent L. major promastigotes and was associated with the appearance of several new peanut agglutinin-binding glycoproteins.
通过凝集素印迹法比较了8种不同利什曼原虫的膜糖缀合物。检测了5种具有不同糖特异性的凝集素：伴刀豆球蛋白A、菜豆凝集素、蓖麻凝集素、大豆凝集素和花生凝集素。伴刀豆球蛋白A和菜豆凝集素与所测试的每种利什曼原虫都发生反应。观察到这2种凝集素以及各种寄生虫的模式各不相同。然而，在几乎所有检测的寄生虫分离株中都存在一个共同的41,000 - 52,000和一个160,000 - 185,000相对分子质量的组分。蓖麻凝集素仅识别一种类似于利什曼原虫分泌因子的非离散含半乳糖糖缀合物。大豆凝集素和花生凝集素与一些低分子量的寄生虫组分发生反应。大豆凝集素与所有测试的利什曼原虫物种都发生反应，而花生凝集素仅识别3个分离株。后一种凝集素与在染料前沿迁移且相对分子质量为35,000和52,000的离散组分结合。无毒力的硕大利什曼原虫前鞭毛体上观察到糖基化增加，并且与几种新的花生凝集素结合糖蛋白的出现有关。
