Neel D, Giner M, Merlu B, Turmel P, Goussault Y, Charron D J
Mol Immunol. 1985 Sep;22(9):1053-9. doi: 10.1016/0161-5890(85)90108-7.
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.
通过系列凝集素亲和分析对来自HLA - DR纯合B淋巴母细胞系（CA）的HLA - DR分子的N - 连接寡糖结构进行了表征。获得了HLA - DR复合物以及分离的α链和β链的聚糖凝集素亲和图谱。在α链种类中检测到两种结构不同的糖基化模式，α1具有高甘露糖型和复合型寡糖，α2仅具有复合型寡糖。相比之下，β链种类仅包含复合型寡糖。对于所描述的每个α1、α2和β链，还发现了进一步的寡糖异质性。与小鼠和豚鼠的Ia抗原不同，在HLA - DR中未发现大量具有双触角结构的糖肽。
