An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide
An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide
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DOI：
10.1002/eji.1830260210
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发表时间：
1996-02-01
影响因子：
5.4
通讯作者：
RowlandJones, S
中科院分区：
文献类型：
--
作者：
Dong, T;Boyd, D;RowlandJones, S
与HLA-B35相关的肽通常在肽的P2锚位置具有脯氨酸或偶尔具有丝氨酸残基。在C末端有一个酪氨酸基于这个基序，我们从HLA-B35呈递的A型流感病毒基质蛋白中鉴定了一个八聚体表位。已经使用在位置1处具有取代的该肽的类似物分析了MHC结合和T细胞受体接触的要求。2. 4. 7和8天然表位在肽的P2处含有丝氨酸残基。用脯氨酸（在B35相关肽的这个位置上的有利氨基酸）取代该残基显著增强了T2-B35细胞系中与HLA-B35的结合，但是该肽不被大多数CTL克隆识别，并且可以拮抗指示肽的识别。这表明P2锚位置的保守取代导致暴露于T细胞受体的肽-MHC表面的构象变化。
Peptides associated with HLA-B35 commonly have a proline or occasionally a serine residue in the P2 anchor position of the peptide. with a tyrosine at the C terminus. Based on this motif, we identified an octamer epitope from influenza A matrix protein which is presented by HLA-B35. The requirements for MHC binding and T cell receptor contact have been analyzed using analogs of this peptide with substitutions at positions 1. 2. 4. 7 and 8. The natural epitope contains a serine residue at P2 of the peptide. Substitution of this residue with proline (the favored amino acid in this position in B35-associated peptides) considerably enhances binding to HLA-B35 in thc T2-B35 cell line, but the peptide is not recognized by the majority of CTL clones and can antagonize recognition of the index peptide. This suggests that a conservative substitution at the P2 anchor position results in a conformational change in the peptide-MHC surface exposed to the T cell receptor.