Structural heterogeneity in HLA-B70, a high-frequency antigen of black populations.

Structural heterogeneity in HLA-B70, a high-frequency antigen of black populations.
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DOI:
10.1111/j.1399-0039.1993.tb02196.x
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发表时间:
1993-11
期刊:
影响因子:
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通讯作者:
J. Domena;A. Little;A. Madrigal;W. Hildebrand;L. Johnston-Dow;E. D. du Toit;W. Bias;P. Parham
J. Domena;A. Little;A. Madrigal;W. Hildebrand;L. Johnston-Dow;E. D. du Toit;W. Bias;P. Parham
中科院分区:
医学4区
文献类型:
--
作者:
J. Domena;A. Little;A. Madrigal;W. Hildebrand;L. Johnston-Dow;E. D. du Toit;W. Bias;P. Parham

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尽管B70抗原在非洲和美国黑人群体中表现出8-23%的等位基因频率,但其仍然定义不清。对来自6个细胞系的编码B70抗原的cDNA进行克隆和测序,鉴定出一组三个密切相关的等位基因:B*1503、B*1509和B*1510,它们形成B15家族的一个亚组。这些等位基因的序列,特别是B*1503的序列,与HLA-B共有序列的序列接近,这与其血清学定义的困难一致。三个等位基因的产物对应于三种经免疫学检测的B70抗原变体,并且可以与B70抗原的B71和B72亚特异性进行一些关联。第四个等位基因,B*7901,先前由Choo等(J. Immunol.147:174-180,1991)描述,其血清学分型不是B70,与B*1510的区别在于单核苷酸取代。同种抗体对肽结合残基的单一差异的敏感性表明结合肽在HLA-B70同种抗原特异性中的作用。由四个等位基因编码的重链在抗原识别位点的四个肽结合残基处不同,其进化修饰可以用等位基因间重组事件来解释。
Although the B70 antigen exhibits allele frequencies of 8-23% in African and American black populations, it remains poorly defined. Cloning and sequencing of cDNA encoding B70 antigens from six cell lines has identified a group of three closely related alleles: B*1503, B*1509 and B*1510, that form a subgroup of the B15 family. The sequences of these alleles and, in particular, B*1503, are close to that of the HLA-B consensus consistent with the difficulty in their serological definition. The products of the three alleles correspond to three electrophoretically detected variants of the B70 antigen and some correlation with the B71 and B72 subspecificities of the B70 antigen can be made. A fourth allele, B*7901, previously described by Choo et al. (J. Immunol. 147: 174-180, 1991) that was not serologically typed as B70, differs by a single nucleotide substitution from B*1510. The sensitivity of alloantibodies to single differences in peptide binding residues suggest a role for bound peptides in the HLA-B70 alloantigenic specificities. The heavy chains encoded by the four alleles differ at four peptide binding residues of the antigen recognition site, the evolutionary modification of which can be explained in terms of interallelic recombination events.