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Libraries of synthetic glycopeptides in the characterization of hte T cell response to tumor associated mucin antigens

机译：合成糖肽的文库在HTE T细胞对肿瘤相关粘蛋白抗原的表征中的表征

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It has been well established that T cell stimulation is mediated by the presentation of peptide antigens by the MHC molecules on the surface of the antigen presenting cells. The peptides are fragments of proteins or even glycoproteins. The design of the binding groove of the MHC molecule is such that it only binds to peptides in their more or less extended coformation by interaction with anchor residues often towards the terminal ends. Carbohydrates and lipids do not interact with the MHC molecules and they belong to the group of T cell independent antigens unable to elicit a T cel response. However, the elution and analysis of peptides bound to the MHC molecules has revealed that glycan residues remaining from glycoprotein degradation could be attached to peptides bound to the MHC molecules [1]. It is therefore important to investigate the immunogenicity of glycopeptides, in particular the changes observed in the mucin glycosylation pattern in the case of e.g. colon cancer cells due to down regulation of enzymes leading to aberrant glycosylation [2]. Nothing is known about the specificity of the T cell response to glycans attached to peptides binding to MHC. The E~k restricted self peptide, VITAFNEGLK, from CBA/J mouse hemoglobin (67-76) is known to bind well MHC class II molecules, but is unable to stimulate the CD4~+ T cells to proliferate [3]. Conversion of such a non-immunogenic peptide into an immunogen by glycosylation would indicate that the T cell specificity was due to direct contact between the glycan and the binding domain of the TCR. Furthermore, by modifying the glycan in this mdoel for T cell-glycan recognition it would be possible to study the detailed molecular interactions betwen the glycan and the TCR, which in turn could lead to knowledge about the requirements for the efficient design of cancer vaccines.
机译：已经很好地确定了T细胞刺激通过抗原呈现细胞表面上的MHC分子呈现肽抗原介绍。肽是蛋白质片段或甚至糖蛋白的片段。 MHC分子的粘合槽的设计是通过与通常朝向末端的锚定残留物的相互作用在其或多或少地延伸的凝结中仅与肽结合。碳水化合物和脂质不会与MHC分子相互作用，它们属于T细胞无关抗原组，不能引发T CEL反应。然而，与MHC分子结合的肽的洗脱和分析表明，剩余的糖蛋白降解含有糖蛋白残留物可以附着于与MHC分子结合的肽[1]。重要的是要调查糖肽的免疫原性，特别是在变化的粘蛋白糖基化模式中观察到的例如的情况下是很重要的由于抑制酶的调节导致异常糖基化的结肠癌细胞[2]。关于T细胞对肽与MHC结合的肽的蛋白的特异性是没有任何熟知的。已知来自CBA / J小鼠血红蛋白（67-76）的E〜K受限制的自肽，Vitafneglk用于结合MHC II类分子，但不能刺激CD4〜+ T细胞增殖[3]。通过糖基化将这种非免疫原性肽转化为免疫原性将表明T细胞特异性是由于聚糖与TCR的结合结构域之间的直接接触。此外，通过改变该MDOEL中的聚糖进行T细胞 - 聚糖识别，可以研究甘草和TCR之间的详细分子相互作用，这反过来可能导致关于癌症疫苗的有效设计要求的知识。

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