Use of antibodies to characterize a 220-kilodalton surface protein from Entamoeba histolytica.
Antibodies were prepared against a 220-kilodalton (kDa) protein partially purified by Sepharose 4B chromatography of Entamoeba histolytica strain HM38:IMSS homogenates, and the protein was found to have lectin properties. The antibodies specifically recognized this protein in trophozoite homogenates. Immunologically related molecules with the same molecular weight were identified by polyclonal antibodies in strains HM1:IMSS, Entamoeba invadens, and Entamoeba histolytica Laredo. Six monoclonal antibodies recognized only the 220-kDa protein present in strains HM38 and HM1, a result indicating the presence of similar epitopes in the proteins from virulent strains isolated from humans. All the antibodies against the 220-kDa protein have the following properties: (1) they bind to the plasma membrane of live or fixed trophozoites, (2) they partially inhibit the adhesion of trophozoites to erythrocytes and cultured cells, and (3) they inhibit erythrophagocytosis.
D000268:Adhesiveness; D000818:Animals; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D002478:Cells, Cultured; D004748:Entamoeba histolytica / Q000276:immunology / Q000378:metabolism* / Q000502:physiology; D004912:Erythrocytes / Q000502:physiology; D005455:Fluorescent Antibody Technique; D006801:Humans; D037102:Lectins; D008565:Membrane Proteins / Q000032:analysis* / Q000276:immunology; D008970:Molecular Weight; D010587:Phagocytosis
D000911:Antibodies, Monoclonal; D037102:Lectins; D008565:Membrane Proteins