Monoclonal antibodies specific for the M- and N-forms of human glycophorin A.
Four mouse monoclonal antibodies directed against the red cell membrane protein glycophorin A have been isolated and characterized. They are produced by hybridomas derived from SP2/0 myeloma cells and spleen cells from Biozzi mice immunized with a mixture of human erythrocytes from homozygous blood group M and N individuals. These antibodies recognize and bind to purified glycophorin A and to glycophorin on the red cell surface. All are of the IgGl, kappa light chain subclass and bind to determinants presented on the 39 amino acid, trypsin-sensitive, N-terminal peptide of glycophorin A. Three display differential specificities for the two allelic forms of glycophorin A; two are exquisitely specific for the M-form and one preferentially binds the N-form. Treatment of red cells with neuraminidase, which removes N-acetylneuraminic acid from glycophorin A, abolishes the binding of these three antibodies. The binding of the N-specific antibody is also sensitive to modification of the amino-terminal residue of the antigen. The fourth antibody binds equally well to both the M- and N-forms as well as to neuraminidase-treated red cells; thus it recognizes a public, N-acetylneuraminic acid independent glycophorin A determinant.
D000372:Agglutination Tests; D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000276:immunology*; D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D002460:Cell Line; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology; D006021:Glycophorins / Q000276:immunology*; D006801:Humans; D008951:MNSs Blood-Group System / Q000276:immunology*; D051379:Mice; D009439:Neuraminidase; D012794:Sialic Acids / Q000276:immunology; D012795:Sialoglycoproteins / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D006021:Glycophorins; D008951:MNSs Blood-Group System; D012794:Sialic Acids; D012795:Sialoglycoproteins; D009439:Neuraminidase