Characterization and distribution of multiple antigens on N-linked oligosaccharides of Dictyostelium discoideum proteins.
Monoclonal antibodies were prepared against a mixture of purified lysosomal enzymes from Dictyostelium discoideum. Three classes of antibodies were found which recognized distinct antigenic determinants on N-linked oligosaccharides of multiple proteins. The structure of the determinants was studied by competition assays using monosaccharides and oligosaccharide/glycopeptide fractions prepared from one Dictyostelium lysosomal enzyme or other sources. The results of these studies suggest that one class of antibody recognizes an epitope containing residues of Man-6-SO4, another recognizes a domain containing a modified GlcNAc, and the third class recognizes an undefined determinant that involves the oligosaccharide. The three determinants are found on multiple overlapping, but nonidentical sets of glycoproteins. The ability to produce monoclonal antibodies against unusual N-linked oligosaccharides offers a powerful tool which can be used to investigate the occurrence, structure, biosynthesis, and the biological roles of these highly immunogenic saccharides.
D000911:Antibodies, Monoclonal; D000946:Antigens, Fungal / Q000032:analysis*; D004023:Dictyostelium / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis; D005656:Fungal Proteins / Q000276:immunology*; D007120:Immunochemistry; D009844:Oligosaccharides / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000946:Antigens, Fungal; D000939:Epitopes; D005656:Fungal Proteins; D009844:Oligosaccharides