HLA-B*3501-peptide interactions: role of anchor residues of peptides in their binding to HLA-B*3501 molecules.
HLA-B*3501-peptide interactions: role of anchor residues of peptides in their binding to HLA-B*3501 molecules.
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HLA-B*3501-肽相互作用：肽锚定残基在与 HLA-B*3501 分子结合中的作用。
DOI：
10.1093/intimm/6.2.255
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发表时间：
1994
影响因子：
4.4
通讯作者：
Takiguchi,M
中科院分区：
文献类型：
--
作者：
Takamiya,Y;Schönbach,C;Nokihara,K;Yamaguchi,M;Ferrone,S;Kano,K;Egawa,K;Takiguchi,M
从培养的人B淋巴细胞表达的HLA-B * 3501分子中分离到两个与HLA-B * 3501结合的自身肽LPFDFTPQY（37 F）和LPGPKFLQY（28 H）。这两个序列与先前报道的HLA-B*3501结合肽的基序一致，所述基序在位置2携带脯氨酸，在位置9携带酪氨酸作为锚残基。这些肽与HLA-B *3501分子的直接结合通过用HLA-B *3501基因转染的RMA-S细胞（RMA-S-B*3501）的流式细胞术分析来定量。37 F和28 H肽均有效地结合HLA-B*3501分子。在HLA-B*3501结合肽的第2位和/或第9位氨基酸的取代显著降低了它们与HLA-B*3501分子的结合。这些结果表明，两个锚残基，位置2的脯氨酸和位置9的酪氨酸在肽与HLA-B*3501分子的结合中是关键的。在肽37 F的第8位插入多达4个甘氨酸残基并不影响其与HLA-B*3501分子的结合亲和力。这些结果表明，只要锚残基是保守的，长肽可以有效地结合HLA I类分子。
Two HLA-B*3501 binding self-peptldes, LPFDFTPQY (37F) and LPGPKFLQY (28H), were Isolated from HLA-B*3501 molecules expressed by cultured human B lymphold cells. Both sequences were consistent with previously reported motifs of HLA-B*3501 binding peptides which carry prollne at position 2 and tyroslne at position 9 as anchor residues. Direct binding of these peptides to HLA-B*3501 molecules was quantitated by flow cytometry analysis of RMA-S cells transfected with the HLA-B*3501 gene (RMA-S-B*3501). Both 37F and 28H peptides bound effectively to HLA-B*3501 molecules. Substitution of amlno acids at position 2 and/or 9 of HLA-B*3501 binding peptides markedly reduced their binding to HLA-B*3501 molecules. These results indicate that two anchor residues, prollne at position 2 and tyroslne at position 9 are critical in binding of peptides to HLA-B*3501 molecules. Insertion of up to four glycine residues at position 8 of the peptide 37F did not affect Its binding affinity to HLA-B*3501 molecules. These results indicate that long peptides can effectively bind to HLA class I molecules provided that anchor residues are conserved.