Snary D, Barnstable C J, Bodmer W F, Crumpton M J
Eur J Immunol. 1977 Aug;7(8):580-5. doi: 10.1002/eji.1830070816.
The HLA-CW2 antigen of the B lymphoblastoid cell line BRI 8 is structurally homologous to the HLA-A and B antigens as judged by various criteria. Each antigen comprised a glycosylated polypeptide of 43 000 molecular weight that is noncovalently associated with beta2-microglobulin (beta2m). Some small differences in molecular parameters were, however, revealed. Thus, the deoxycholate-solubilized HLA-CW2 antigen sedimented at the same rate as the HLA-A antigens but at a slightly faster rate than the HLA-B antigens. This variation is apparently is apparently due to different amounts of bound deoxycholate. Also, whereas essentially all of the HLA-A and B antigens and about half of the HLA-CW2 antigen were adsorbed strongly by Lens culinaris lectin-Sepharose, the remaining HLA-CW2 antigen was bound much more weakly and did not require sugar for elution. This difference reflects some structural heterogeneity in the carbohydrate moiety of the HLA-CW2 antigen. The results of various studies suggest that the HLA-CW2 antigen is expressed to a lower extent than the HLA-A or B antigens and that essentially all of the beta2m of the BRI 8 plasma membrane is associated with the HLA-A, B and C alloantigenic polypeptides.
根据各种标准判断，B淋巴母细胞系BRI 8的HLA - CW2抗原在结构上与HLA - A和B抗原同源。每种抗原都包含一条分子量为43000的糖基化多肽，该多肽与β2 - 微球蛋白（β2m）非共价结合。然而，分子参数上显示出一些小差异。因此，脱氧胆酸盐溶解的HLA - CW2抗原沉降速率与HLA - A抗原相同，但比HLA - B抗原略快。这种差异显然是由于结合的脱氧胆酸盐量不同。此外，虽然基本上所有的HLA - A和B抗原以及大约一半的HLA - CW2抗原都被扁豆凝集素 - 琼脂糖强烈吸附，但其余的HLA - CW2抗原结合较弱，洗脱时不需要糖。这种差异反映了HLA - CW2抗原碳水化合物部分的一些结构异质性。各种研究结果表明，HLA - CW2抗原的表达程度低于HLA - A或B抗原，并且BRI 8质膜上基本上所有的β2m都与HLA - A、B和C同种异体抗原多肽相关。
