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首页> 外文OA文献 >Vesicular stomatitis virus antigenic octapeptide N52-59 is anchored into the groove of the H-2Kb molecule by the side chains of three amino acids and the main-chain atoms of the amino terminus.
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Vesicular stomatitis virus antigenic octapeptide N52-59 is anchored into the groove of the H-2Kb molecule by the side chains of three amino acids and the main-chain atoms of the amino terminus.

机译：水泡性口腔炎病毒抗原八肽N52-59通过三个氨基酸的侧链和氨基末端的主链原子锚定在H-2Kb分子的凹槽中。

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摘要

This study describes an analysis of the interaction of individual amino acid residues of the vesicular stomatitis virus (VSV) nucleocapsid antigenic octapeptide (N52-59; Arg-Gly-Tyr-Val-Tyr-Gln-Gly-Leu) with the H-2Kb molecule and T-cell receptors (TCRs). Tyr-3, Tyr-5, and Leu-8 were the positions in the peptide found to be H-2Kb contact residues by analyzing single alanine-substituted peptides in a competition assay with a Kb-restricted antigenic nonapeptide of Sendai virus. Arg-1, Gly-2, Val-4, Gln-6, and Gly-7 of the peptide were identified as putative TCR contact residues by testing the peptide analogs for their capacity to sensitize targets for VSV-specific cytolytic T-lymphocyte clones. The octamer N52-59 was the optimal length of the peptide required for binding to Kb. This peptide length requirement and the finding of an irregular interspersing of major histocompatibility complex and TCR contact residues are most consistent with the conclusion that the peptide is in an extended conformation in the antigen binding groove. Furthermore, data on binding of truncated peptides show that, although the Arg-1 side chain has been assigned as a TCR contact residue, the main-chain atoms of the N-terminal amino group are most likely involved in interacting with the major histocompatibility complex molecule. A panel of H-2Kb point mutants was constructed to explore the effect of altered amino acid residues on the binding of N52-59. Mutants with amino acid substitutions along the floor of the groove all bound the VSV peptide but modulated its interaction with Kb, apparently causing subtle changes in the spatial arrangement of some specific TCR contact residues in the peptide.
机译：这项研究描述了水疱性口腔炎病毒（VSV）核衣壳抗原八肽（N52-59; Arg-Gly-Tyr-Val-Tyr-Gln-Gly-Leu）与H-2Kb相互作用的分析分子和T细胞受体（TCR）。 Tyr-3，Tyr-5和Leu-8是在与仙台病毒的Kb限制性抗原九肽竞争分析中通过分析单个丙氨酸取代的肽而发现的肽，它们为H-2Kb接触残基。通过测试肽类似物对VSV特异性溶细胞性T淋巴细胞克隆的靶标敏感的能力，可将该肽的Arg-1，Gly-2，Val-4，Gln-6和Gly-7鉴定为推定的TCR接触残基。 。八聚体N52-59是与Kb结合所需的最佳肽段长度。该肽长度要求以及发现主要组织相容性复合物和TCR接触残基的不规则散布与该肽在抗原结合沟中处于延长构象的结论最一致。此外，有关截短肽结合的数据显示，尽管已将Arg-1侧链指定为TCR接触残基，但N末端氨基的主链原子最有可能与主要组织相容性复合物相互作用分子。构建了一组H-2Kb点突变体，以研究氨基酸残基改变对N52-59结合的影响。沿着凹槽底部具有氨基酸取代的突变体均结合了VSV肽，但调节了其与Kb的相互作用，显然导致了该肽中某些特定TCR接触残基的空间排列发生了细微变化。

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