Sulfated oligosaccharides block antibodies to many Dictyostelium discoideum acid hydrolases.
The lysosomal hydrolases of the cellular slime mold, Dictyostelium discoideum, possess a common posttranslational modification which is extremely antigenic in rabbits and mice. Rabbit antisera and mouse monoclonal antibodies that recognize this determinant cross-react with a group of at least 40-50 highly negatively charged proteins which include most or all of the lysosomal enzymes. (Knecht, D. A., Dimond, R. L., Wheeler, S., and Loomis, W. F. (1984) J. Biol. Chem. 259, 10633-10640). The present study demonstrates that the determinant is found on certain N-linked oligosaccharides derived from one of these proteins. An esterified sulfate is absolutely required for antigenicity.
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D004023:Dictyostelium / Q000201:enzymology*; D000939:Epitopes / Q000032:analysis*; D006020:Glycopeptides / Q000276:immunology; D006867:Hydrolases / Q000276:immunology*; D007106:Immune Sera; D009844:Oligosaccharides / Q000494:pharmacology*
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes; D006020:Glycopeptides; D007106:Immune Sera; D009844:Oligosaccharides; D006867:Hydrolases