Identification of terminal N-acetylglucosamine residues of highly branched asparagine-linked oligosaccharides as immunoreactive domains of a chicken heterophile antigenic determinant.
Chicken heterophile antigenic determinant (CHAD-1) has been previously found in medullary lymphocytes of the bursa and thymus as well as in some non-lymphoid cells by the immunoperoxidase method, using rabbit antiserum to a complete Freund's adjuvant (CFA) as the first antibody. In this work we demonstrated that absorption of anti-CFA serum with highly purified preparations of hen egg white glycoproteins (ovomucoid, ovoinhibitor, ovalbumin) or chicken orosomucoid completely blocked immunoperoxidase staining for CHAD-1. Treatment of these glycoproteins with beta-N-acetylglucosaminidase suppressed their capacity to inhibit this staining. Absorption of anti-CFA serum with asparagine-linked glycopeptides which have the mannose alpha 1,3 arm disubstituted by GlcNAc residues and which have another GlcNAc residue linked beta 1,4 to the beta-linked mannose of the core also inhibited staining for CHAD-1. These data indicated that highly branched asparagine-linked oligosaccharides with terminal GlcNAc residues beta-linked to mannose represent immunoreactive domains of CHAD-1.
D000042:Absorption; D000117:Acetylglucosamine / Q000276:immunology*; D000818:Animals; D001216:Asparagine / Q000276:immunology; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000032:analysis*; D005260:Female; D005620:Freund's Adjuvant; D005944:Glucosamine / Q000031:analogs & derivatives*; D006020:Glycopeptides; D007106:Immune Sera / Q000276:immunology; D007124:Immunoenzyme Techniques; D008297:Male; D009844:Oligosaccharides / Q000276:immunology*
D000939:Epitopes; D006020:Glycopeptides; D007106:Immune Sera; D009844:Oligosaccharides; D001216:Asparagine; D005620:Freund's Adjuvant; D005944:Glucosamine; D000117:Acetylglucosamine