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首页> 外文期刊>Immunology: An Official Journal of the British Society for Immunology >Steric recognition of T-cell receptor contact residues is required to map mutant epitopes by immunoinformatical programmes
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Steric recognition of T-cell receptor contact residues is required to map mutant epitopes by immunoinformatical programmes

机译：要通过免疫信息学程序绘制突变表位，必须立体识别T细胞受体接触残基

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摘要

MHC class I-restricted CD8 T-lymphocyte epitopes comprise anchor motifs, T-cell receptor (TCR) contact residues and the peptide backbone. Serial variant epitopes with substitution of amino acids at either anchor motifs or TCR contact residues have been synthesized for specific interferon-γ responses to clarify the TCR recognition mechanism as well as to assess the epitope prediction capacity of immunoinformatical programmes. CD8 T lymphocytes recognise the steric configuration of functional groups at the TCR contact side chain with a parallel observation that peptide backbones of various epitopes adapt to the conserved conformation upon binding to the same MHC class I molecule. Variant epitopes with amino acid substitutions at the TCR contact site are not recognised by specific CD8 T lymphocytes without compromising their binding capacity to MHC class I molecules, which demonstrates two discrete antigen presentation events for the binding of peptides to MHC class I molecules and for TCR recognition. The predicted outcome of immunoinformatical programmes is not consistent with the results of epitope identification by laboratory experiments in the absence of information on the interaction with TCR contact residues. Immunoinformatical programmes based on the binding affinity to MHC class I molecules are not sufficient for the accurate prediction of CD8 T-lymphocyte epitopes. The predictive capacity is further improved to distinguish mutant epitopes from the non-mutated epitopes if the peptide-TCR interface is integrated into the computing simulation programme.
机译：MHC I类限制性CD8 T淋巴细胞表位包含锚基序，T细胞受体（TCR）接触残基和肽骨架。已经合成了在锚基序或TCR接触残基处具有氨基酸取代的连续变体表位，以用于特异性干扰素-γ应答，以阐明TCR识别机制以及评估免疫信息程序的表位预测能力。 CD8 T淋巴细胞在TCR接触侧链上识别官能团的空间构型，同时观察到各种表位的肽主链与相同的I类MHC分子结合后会适应保守的构象。在不损害其与MHC I类分子的结合能力的情况下，特异性CD8 T淋巴细胞无法识别在TCR接触位点具有氨基酸取代的变异抗原决定簇，这证明了肽与MHC I类分子和TCR结合的两个离散抗原呈递事件。承认。在没有有关与TCR接触残基相互作用的信息的情况下，免疫信息学计划的预测结果与实验室实验确定的抗原决定簇的结果不一致。基于与I类MHC分子的结合亲和力的免疫信息学程序不足以准确预测CD8 T淋巴细胞表位。如果将肽-TCR接口集成到计算仿真程序中，则进一步提高了预测能力，可将突变表位与非突变表位区分开。

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