Endo T, Obata F, Ishikawa N, Kojima H, Kashiwagi N
Department of Transplantation Immunology, Kitasato University School of Medicine, Sagamihara, Japan.
Hum Immunol. 1987 Nov;20(3):209-17. doi: 10.1016/0198-8859(87)90104-2.
The molecular localization of a novel human class II specificity, DQ "Wa," was investigated. A monoclonal antibody, HU46, which has previously been shown to react with DR4, Dw15 and DRw8, Dw8 B cells that type as DQ "blank," was used for the isolation and structural characterization of class II molecules bearing the DQ "Wa" determinant. The partial N-terminal sequence analysis of class II molecules bearing the DQ "Wa" determinant, purified from two B-cell lines, EBV-Wa (DR4, Dw15, DQ "blank") and GI (DRw8, Dw8, DQ "blank"), shows that the alpha and beta chain sequences are homologous to HLA-DQ. Within the limits of our analysis, the alpha and beta chains from both cell lines are identical. Both beta chains possess a phenylalanine residue at position 9 that differs from the tyrosine residue present at this position in beta chains of DQ alleles. These studies indicate that a novel human class II specificity, DQ "Wa," resides on a new allelic form of DQ molecules found in DR4, Dw15 and DRw8, Dw8 cells that are DQ "blank."
对一种新型人类Ⅱ类特异性分子DQ“Wa”的分子定位进行了研究。一种单克隆抗体HU46,先前已证明它能与DR4、Dw15以及DRw8、Dw8且Ⅱ类分子分型为DQ“空白”的B细胞发生反应,该抗体被用于分离和鉴定带有DQ“Wa”决定簇的Ⅱ类分子的结构特征。从两个B细胞系EBV-Wa(DR4、Dw15、DQ“空白”)和GI(DRw8、Dw8、DQ“空白”)中纯化出带有DQ“Wa”决定簇的Ⅱ类分子,并对其进行部分N端序列分析,结果显示α链和β链序列与HLA-DQ具有同源性。在我们的分析范围内,两个细胞系的α链和β链是相同的。两条β链在第9位都有一个苯丙氨酸残基,这与DQ等位基因β链中该位置的酪氨酸残基不同。这些研究表明,一种新型人类Ⅱ类特异性分子DQ“Wa”存在于在DR4、Dw15以及DRw8、Dw8且Ⅱ类分子分型为DQ“空白”的细胞中发现的DQ分子的一种新等位基因形式上。