Adhesion properties of Entamoeba histolytica.
Trophozoites of Entamoeba histolytica adhere to and phagocytize red blood cells and bacteria. Furthermore, in the initial step of the amoebic infectious process the parasite attaches to intestinal epithelial cells. A lectin (carbohydrate-binding protein) which apparently has a role in the attachment of the parasite to host cells was found in trophozoites of E. histolytica. When amoeba cells were disrupted by freeze-thawing, the lectin activity, as determined by haemagglutination of human erythrocytes, remained associated with the sedimented membrane fraction. This activity was pH dependent and heat and oxidation-sensitive, and was destroyed by proteolysis and on autoincubation. Moreover, the lectin activity was inhibited by a variety of N-acetylglucosamine-containing compounds such as chitin and chitin oligosaccharides, bacterial peptidoglycan, rabbit colonic mucus, bovine and human serum, an IgA fraction isolated from human colostrum, and IgG from sera of amoebiasis patients. These glycoconjugates also interfered with the adherence of intact radiolabelled amoeba trophozoites to human intestinal epithelial cells as well as their attachment to red blood cells. Although the lectin activity and the toxin-like activity previously found in E. histolytica seem to be two separate substances, they share a number of properties which suggest that they are related and may have a function in pathogenicity.
D000117:Acetylglucosamine / Q000494:pharmacology; D000268:Adhesiveness; D000373:Agglutinins / Q000032:analysis / Q000494:pharmacology; D000818:Animals; D002460:Cell Line; D004748:Entamoeba histolytica / Q000032:analysis / Q000472:pathogenicity / Q000502:physiology*; D006384:Hemagglutination; D006801:Humans; D037102:Lectins / Q000032:analysis / Q000494:pharmacology; D014118:Toxins, Biological / Q000494:pharmacology
D000373:Agglutinins; D037102:Lectins; D014118:Toxins, Biological; D000117:Acetylglucosamine