Analysis of HLA-DR antigen glycosylation by serial lectin affinity chromatography.
The structure of the N-linked oligosaccharides of HLA-DR molecules from an HLA-DR homozygous B-lymphoblastoid cell line (CA) was characterized by serial lectin affinity analysis. Glycans lectin affinity profile were obtained for the HLA-DR complex and separated alpha- and beta-chains. Two structurally distinct glycosylation patterns were detected for the alpha-chain species, the alpha 1 with high-mannose- and complex-type oligosaccharides and alpha 2 with a complex-type one. In contrast, the beta-chain species contains only complex-type oligosaccharides. Further oligosaccharide heterogeneity is found for each alpha 1-, alpha 2- and beta-chain described. In contrast to murine and guinea-pig Ia antigens, no significant amount of glycopeptides with biantennary structure was found in HLA-DR.
D002460:Cell Line; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis; D006684:HLA-DR Antigens; D000949:Histocompatibility Antigens Class II / Q000032:analysis*; D037102:Lectins; D008358:Mannose / Q000032:analysis; D008970:Molecular Weight; D009844:Oligosaccharides / Q000032:analysis*; D013329:Structure-Activity Relationship
D006023:Glycoproteins; D006684:HLA-DR Antigens; D000949:Histocompatibility Antigens Class II; D037102:Lectins; D009844:Oligosaccharides; D008358:Mannose