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.