PEPTIDE BINDING TO EMPTY HLA-B27 MOLECULES OF VIABLE HUMAN-CELLS
PEPTIDE BINDING TO EMPTY HLA-B27 MOLECULES OF VIABLE HUMAN-CELLS
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DOI：
10.1038/351074a0
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发表时间：
1991-05-02
期刊：
影响因子：
64.8
通讯作者：
PARHAM, P
中科院分区：
文献类型：
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作者：
BENJAMIN, RJ;MADRIGAL, JA;PARHAM, P
通过多态性I类主要组织相容性复合物分子的抗原肽的细胞内结合产生由CD 8 + T细胞的受体识别的配体1。 先前描述的肽与I类分子结合的体外测定受到可及结合位点比例低或缺乏等位基因特异性的限制2-6。 在这里，我们描述了一个系统，其中人类I类分子HLA-B27结合相当数量的流感肽与精确的等位基因歧视。 结合需要活细胞，受γ-干扰素刺激，受布雷菲德菌素A抑制。 我们的结果与细胞表面存在相当稳定的“空”HLA-B27分子一致。 相比之下，对第二种流感肽的结合的分析表明，空的HLA-Aw 68分子相对较短。 我们推测HLA-B27可能在体内结合细胞外肽，这种特性可能是其与自身免疫性疾病相关的基础。
INTRACELLULAR binding of antigenic peptides by polymorphic class I major histocompatibility complex molecules creates the ligands recognized by receptors of CD8+ T cells 1. Previously described in vitro assays of peptide binding to class I molecules have been limited by either the low proportion of accessible binding sites or the lack of allelic specificity 2-6. Here we describe a system in which the human class I molecule HLA-B27 binds considerable amounts of an influenza peptide with precise allelic discrimination. Binding requires viable cells, is stimulated by gamma-interferon and is inhibited by brefeldin A. Our results are consistent with the presence of fairly stable 'empty' HLA-B27 molecules at the cell surface. By contrast, analysis of the binding of a second influenza peptide indicates that empty HLA-Aw68 molecules are relatively short-lived. We speculate that HLA-B27 might bind extracellular peptides in vivo and that this property could underlie its association with autoimmune disease.