Structural analysis of the oligosaccharides of DR1 and DQw1 molecules.
The major glycopeptide fractions of the alpha- and beta-chains of HLA-DR1 and DQw1 molecules were isolated on columns of immobilized concanavalin A (Con A), Lens culinaris (Lens), Ricinus communis agglutinin Type I (RCA), and leuko-phytohemagglutinin. Oligosaccharides were prepared from these fractions by enzymatic digestion with Endoglycosidases H or F and were analyzed on Bio-Gel P-6. The glycopeptides tightly bound to Con A (ConA III) were mostly associated with alpha-chains and were resolved as a single oligosaccharide peak (Kd = 0.72) on Bio-Gel P-6 after Endo H digestion. Man-5 is the minimal polymannosyl structure which can be deduced for the ConA III fractions of either DQw1 or DR1 oligosaccharides. The major component of the glycopeptides of the alpha-chains of either DR1 or DQw1 molecules which were weakly bound to Con A (ConA II fraction) did not interact with RCA before or after mild acid hydrolysis or neuraminidase treatment. This component represents a biantennary complex with neither terminal galactose nor sialic acid residues with a minimal structure terminating in N-acetyl glucosamine on the Mannose alpha 1----6 arm, referred to as GnM. The ConA II fractions, which constitute 10% of the total glycopeptides of beta-chains, are associated primarily with fucosylated, sialylated biantennary oligosaccharides not seen on the alpha-chains. The ConA I unbound fractions of either alpha- or beta-chains were mostly bound to RCA after mild acid hydrolysis, suggesting that the minimal structure was a sialylated triantennary structure. The major component associated with the beta-chains was bound to Lens such that a more definite structural assignment can be made, i.e., a triantennary structure with the Mannose on the alpha 1----6 arm substituted at C-2 and C-6. The oligosaccharides of alpha- and beta-chains were resolved as broad peaks on Bio-Gel P-6, suggesting that a mixture of tri- and tetraantennary structures with variable degrees of sialylation and galactosylation were present. The structural differences reported here between oligosaccharides of alpha- and beta-chains of DQw1 and of the two subsets of DR1 molecules could be responsible in part for the differential recognition properties expected of human class II molecules encoded by distinct loci.
D000180:Acrylic Resins; D002236:Carbohydrate Conformation; D002846:Chromatography, Affinity; D003208:Concanavalin A; D006020:Glycopeptides / Q000378:metabolism; D006683:HLA-DQ Antigens; D015798:HLA-DR1 Antigen; D006596:Hexosaminidases; D000949:Histocompatibility Antigens Class II; D006801:Humans; D037102:Lectins / Q000378:metabolism; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D009439:Neuraminidase; D009844:Oligosaccharides / Q000302:isolation & purification / Q000378:metabolism; D010835:Phytohemagglutinins; D037121:Plant Lectins; D012794:Sialic Acids
D000180:Acrylic Resins; D006020:Glycopeptides; D006683:HLA-DQ Antigens; D015798:HLA-DR1 Antigen; D000949:Histocompatibility Antigens Class II; D037102:Lectins; D009844:Oligosaccharides; D010835:Phytohemagglutinins; D037121:Plant Lectins; C017707:Ricinus communis agglutinin-1; D012794:Sialic Acids; D003208:Concanavalin A; C046089:Bio-Gel P-4; D006596:Hexosaminidases; D009439:Neuraminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase