Kobiler D, Mirelman D
J Infect Dis. 1981 Dec;144(6):539-46. doi: 10.1093/infdis/144.6.539.
The adhesion of radiolabeled trophozoites of Entamoeba histolytica to monolayers of a human intestinal epithelial cell line was found to be dependent on time, temperature, and concentration. Adherence seems to be mediated by a carbohydrate binding protein (lectin), which was previously found in trophozoites of E. histolytica. The adherence of the trophozoites was found to be pH-dependent and was inhibited by several N-acetyl-glucosamine-containing glycoconjugates, such as bacterial peptidoglycan, chitin, and IgA; similar results were obtained with the isolated lectin. Furthermore, the semipurified amoebic lectin and wheat germ agglutinin, which have similar sugar specificities, competed with the intact amoeba for receptor sites on the epithelial cells. In addition, both sera from patients with amoebiasis and an IgG fraction from these sera inhibited lectin activity and the adherence of the trophozoites.
研究发现,溶组织内阿米巴放射性标记滋养体与人肠上皮细胞系单层的黏附取决于时间、温度和浓度。黏附似乎是由一种碳水化合物结合蛋白(凝集素)介导的,该凝集素先前在溶组织内阿米巴滋养体中被发现。已发现滋养体的黏附依赖于pH值,并受到几种含N-乙酰葡糖胺的糖缀合物的抑制,如细菌肽聚糖、几丁质和IgA;分离出的凝集素也得到了类似结果。此外,具有相似糖特异性的半纯化阿米巴凝集素和麦胚凝集素,会与完整的阿米巴竞争上皮细胞上的受体位点。另外,阿米巴病患者的血清以及这些血清中的IgG组分均能抑制凝集素活性和滋养体的黏附。