de Araújo-Jorge T C, de Souza W
Z Parasitenkd. 1986;72(2):153-71. doi: 10.1007/BF00931143.
The effect of incubation with lectins of the macrophages or two evolutive stages of Trypanosoma cruzi (noninfective epimastigotes and infective trypomastigotes) on the ingestion of the parasites by mouse peritoneal macrophages was studied. Lectins which bind to residues of mannose (Lens culinaris, LCA), N-acetyl-D-glucosamine or N-acetylneuraminic acid (Triticum vulgaris, WGA), beta-D-galactose (Ricinus communis, RCA), N-acetyl-D-galactosamine (Phaseolus vulgaris, PHA; Dolichos biflorus, DBA; and Wistaria floribunda, WFA), fucose (Lotus tetragonolobus, LTA), and N-acetylneuraminic acid (Limulus polyphemus, LPA) were used. By lectin blockage we concluded that, alpha-D-mannose-like, beta-D-galactose and N-acetyl-D-galactosamine (PHA, reagent) residues, located on the macrophage's surface are required for both epi- and trypomastigote uptake, while N-acetylneuraminic acid and fucose residues, impede trypomastigote ingestion but do not interfere with epimastigote interiorization. Macrophages' N-acetyl-D-glucosamine residues are required for epimastigote uptake. On the other hand, from the T. cruzi surface, mannose residues prevent ingestion of epi- and trypomastigotes. Galactose residues participate in endocytosis of trypomastigotes, but hinder epimastigote interiorization. Exposed N-acetyl-D-glucosamine residues are required for uptake of the two evolutive forms. N-acetylneuraminic acid residues on the trypomastigote membrane prevent their endocytosis by macrophages. These results together with those reported previously showing the effect of monosaccharides on the T. cruzi-macrophage interaction, indicate that (a) sugar residues located on the parasite and on macrophage surface play some role in the process of recognition of T. cruzi, (b) different macrophage carbohydrate-containing receptors are involved in the recognition of epimastigotes and trypomastigotes forms of T. cruzi, (c) N-acetylneuraminic acid residues located on the surface of trypomastigotes or macrophages impede the interaction of the parasite with these host cells, and suggest that (d) sugar-binding proteins located on the macrophage surface participate in the recognition of beta-D-galactose and N-acetyl-D-galactosamine residues located on the surface of trypomastigotes and exposed after blockage or splitting off of N-acetylneuraminic acid residues. Some lectins which bind to macrophages and block the ingestion of parasites did not interfere with their adhesion.
研究了用凝集素与巨噬细胞或克氏锥虫的两个进化阶段（非感染性前鞭毛体和感染性锥鞭毛体）共同孵育对小鼠腹腔巨噬细胞摄取这些寄生虫的影响。使用了与甘露糖残基结合的凝集素（小扁豆凝集素，LCA）、N-乙酰-D-葡糖胺或N-乙酰神经氨酸（小麦胚芽凝集素，WGA）、β-D-半乳糖（蓖麻凝集素，RCA）、N-乙酰-D-半乳糖胺（菜豆凝集素，PHA；双花扁豆凝集素，DBA；和紫藤凝集素，WFA）、岩藻糖（四角豆凝集素，LTA）以及N-乙酰神经氨酸（鲎试剂，LPA）。通过凝集素阻断，我们得出结论，巨噬细胞表面的α-D-甘露糖样、β-D-半乳糖和N-乙酰-D-半乳糖胺（PHA，试剂）残基对于前鞭毛体和锥鞭毛体的摄取都是必需的，而N-乙酰神经氨酸和岩藻糖残基会阻碍锥鞭毛体的摄取，但不干扰前鞭毛体的内化。巨噬细胞的N-乙酰-D-葡糖胺残基是前鞭毛体摄取所必需的。另一方面，在克氏锥虫表面，甘露糖残基会阻止前鞭毛体和锥鞭毛体的摄取。半乳糖残基参与锥鞭毛体的内吞作用，但会阻碍前鞭毛体的内化。两种进化形式的摄取都需要暴露的N-乙酰-D-葡糖胺残基。锥鞭毛体膜上的N-乙酰神经氨酸残基会阻止巨噬细胞对它们的内吞作用。这些结果与先前报道的单糖对克氏锥虫-巨噬细胞相互作用的影响一起表明，（a）位于寄生虫和巨噬细胞表面的糖残基在克氏锥虫的识别过程中起一定作用，（b）不同的含碳水化合物的巨噬细胞受体参与克氏锥虫前鞭毛体和锥鞭毛体形式的识别，（c）位于锥鞭毛体或巨噬细胞表面的N-乙酰神经氨酸残基会阻碍寄生虫与这些宿主细胞的相互作用，并表明（d）位于巨噬细胞表面的糖结合蛋白参与识别位于锥鞭毛体表面且在N-乙酰神经氨酸残基被阻断或分离后暴露的β-D-半乳糖和N-乙酰-D-半乳糖胺残基。一些与巨噬细胞结合并阻断寄生虫摄取的凝集素不会干扰它们的黏附。
