Sekimata M, Hiraiwa M, Andrien M, Dupont E, Karaki S, Yamamoto J, Kano K, Takiguchi M
Department of Immunology, University of Tokyo, Japan.
J Immunol. 1990 Apr 15;144(8):3228-33.
A novel HLA-B5 CREG gene, HLA-B SNA was cloned and the primary structure was determined. The sequence data showed that HLA-B SNA was identical to HLA-B51 except the alpha 1 domain in which one amino acid substitution at residue 74 and 5 amino acid substitutions associated with the Bw4/Bw6 epitopes were observed between these Ag. The comparison with other HLA-B locus genes suggested that HLA-B SNA evolved from HLA-B51 by gene exchange or recombination at the exon 2 between HLA-B51 and B8. A total of 10 of 14 HLA-B51-specific CTL clones showed significantly weak or no recognition of HLA-B SNA Ag. They also gave the same degree of a lysis of Hmy2CIR cells expressing the HLA-B35/51 chimeric Ag composed of the alpha 1 domain of HLA-B35 and other domains of HLA-B51 as that of Hmy2CIR cells expressing the HLA-B SNA Ag. These results demonstrated that amino acid substitutions within positions 77-83 associated with the HLA-Bw4/Bw6 epitopes have an influence on recognition of the HLA-B SNA antigen by HLA-B51-specific CTL.
克隆了一个新的HLA - B5 CREG基因HLA - B SNA,并确定了其一级结构。序列数据显示,HLA - B SNA与HLA - B51相同,只是在α1结构域中,这两种抗原之间在第74位氨基酸处有一个氨基酸替换,并且在与Bw4 / Bw6表位相关的位置有5个氨基酸替换。与其他HLA - B基因座基因的比较表明,HLA - B SNA是通过HLA - B51和B8之间外显子2的基因交换或重组从HLA - B51进化而来。14个HLA - B51特异性CTL克隆中有10个对HLA - B SNA抗原的识别明显较弱或无识别。它们对表达由HLA - B35的α1结构域和HLA - B51的其他结构域组成的HLA - B35 / 51嵌合抗原的Hmy2CIR细胞的裂解程度,与对表达HLA - B SNA抗原的Hmy2CIR细胞的裂解程度相同。这些结果表明,与HLA - Bw4 / Bw6表位相关的77 - 83位氨基酸替换对HLA - B51特异性CTL识别HLA - B SNA抗原有影响。