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首页> 外文期刊>Journal of Molecular Biology >Structural basis for the specific recognition of the major antigenic peptide from the Japanese cedar pollen allergen Cry j 1 by HLA-DP5
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Structural basis for the specific recognition of the major antigenic peptide from the Japanese cedar pollen allergen Cry j 1 by HLA-DP5

机译：HLA-DP5特异性识别日本雪松花粉过敏原Cry j 1中主要抗原肽的结构基础

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The major allergen, Cry j 1, was isolated from Japanese cedar Cryptomeria japonica (Cry j) pollen and was shown to react with immunoglobulin E antibodies in the sera from pollinosis patients. We previously reported that the frequency of HLA-DP5 was significantly higher in pollinosis patients and the immunodominant peptides from Cry j 1 bound to HLA-DP5 to activate Th2 cells. In the present study, we determined the crystal structure of the HLA-DP5 heterodimer in complex with a Cry j 1-derived nine-residue peptide, at 2.4 ? resolution. The peptide-binding groove recognizes the minimal peptide with 10 hydrogen bonds, including those between the negatively charged P1 pocket and the Lys side chain at the first position in the peptide sequence. We confirmed that HLA-DP5 exhibits the same Cry j 1-binding mode in solution, through pull-down experiments using structure-based mutations of Cry j 1. We also identified the characteristic residues of HLA-DP5 that are responsible for the distinct properties of the groove, by comparing the structure of HLA-DP5 and the previously reported structures of HLA-DP2 in complexes with pDRA of the self-antigen. The comparison revealed that the HLA-DP5·pCry j 1 complex forms several hydrogen bond/salt bridge networks between the receptor and the antigen that were not observed in the HLA-DP2·pDRA complex. Evolutionary considerations have led us to conclude that HLA-DP5 and HLA-DP2 represent two major groups of the HLA-DP family, in which the properties of the P1 and P4 pockets have evolved and acquired the present ranges of epitope peptide-binding specificities.
机译：主要过敏原Cry j 1是从日本雪松柳杉花粉（Cry j）花粉中分离出来的，显示与花粉病患者血清中的免疫球蛋白E抗体反应。我们以前曾报道，在花粉病患者中HLA-DP5的频率明显更高，并且Cry j 1的免疫优势肽与HLA-DP5结合以激活Th2细胞。在本研究中，我们确定了HLA-DP5异二聚体与Cry j 1衍生的九残基肽在2.4？解析度。肽结合槽识别具有10个氢键的最小肽，包括在肽序列第一个位置上带负电荷的P1口袋和Lys侧链之间的氢键。通过使用基于结构的Cry j 1突变的下拉实验，我们证实了HLA-DP5在溶液中表现出相同的Cry j 1结合模式。通过比较HLA-DP5的结构和先前报道的HLA-DP2与自身抗原的pDRA配合物的结构来确定凹槽的大小。比较表明，HLA-DP5·pCryj 1复合物在受体和抗原之间形成了几个氢键/盐桥网络，这在HLA-DP2·pDRA复合物中没有观察到。进化方面的考虑使我们得出结论，HLA-DP5和HLA-DP2代表HLA-DP家族的两个主要类别，其中P1和P4口袋的特性已经进化并获得了当前范围的表位肽结合特异性。

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