title: Surface properties related to concanavalin A-induced agglutination. A comparative study of several Entamoeba strains.
abstract: Pathogenic strains of Entamoeba histolytica are more easily agglutinated with concanavalin A (Con A) than strains isolated from human asymptomatic carriers. All three pathogenic strains studied here were found to agglutinate with low concentrations of Con A in contrast to various nonpathogenic axenic strains of amebas, characterized by their ability to grow at room temperature. Our present observations suggest that the extreme susceptibility of pathogenic strains of E. histolytica to agglutinate with Con A is related to their higher capacity for lectin binding and to their lack of detectable repulsive charges at the cell surface. The amount of fluorescein-tagged Con A bound to the surface was much higher in pathogenic strains. Only nonpathogenic strains showed a detectable negative surface charge as studied both by means of cell microelectrophoresis and by labeling cells with cationized ferritin at 0 degrees C. The mobility of surface Con A receptors estimated as the percentage of caps was comparable in all strains. Results of one strain cultured in axenic and monoxenic conditions suggested that bacteria can modify the behaviour of E. histolytica trophozoites by altering surface properties of the amebas.
mesh_terms: D000372:Agglutination Tests; D000818:Animals; D003208:Concanavalin A / Q000494:pharmacology*; D004586:Electrophoresis / Q000379:methods; D004747:Entamoeba / Q000187:drug effects / Q000378:metabolism / Q000472:pathogenicity*; D005293:Ferritins / Q000378:metabolism; D033862:Iron-Binding Proteins; D011956:Receptors, Cell Surface / Q000378:metabolism; D011952:Receptors, Concanavalin A / Q000378:metabolism; D013499:Surface Properties
chemical_list: D033862:Iron-Binding Proteins; D011956:Receptors, Cell Surface; D011952:Receptors, Concanavalin A; C027293:ferritin receptor; D003208:Concanavalin A; D005293:Ferritins