MINIMUM LENGTH OF AN IDIOTYPIC PEPTIDE AND A MODEL FOR ITS BINDING TO A MAJOR HISTOCOMPATIBILITY COMPLEX CLASS-II MOLECULE
MINIMUM LENGTH OF AN IDIOTYPIC PEPTIDE AND A MODEL FOR ITS BINDING TO A MAJOR HISTOCOMPATIBILITY COMPLEX CLASS-II MOLECULE
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DOI：
10.1002/j.1460-2075.1989.tb03599.x
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发表时间：
1989-07-01
期刊：
影响因子：
11.4
通讯作者：
LAMBRIS, JD
中科院分区：
文献类型：
--
作者：
BOGEN, B;LAMBRIS, JD
我们已经确定了合成肽的最小长度，该合成肽可以激活对突变的自身抗原特异性的I-Ed限制性BALB/c T细胞克隆：同源的A2315免疫球蛋白轻链上的独特位。包含λ 2315序列的残基91 - 101的肽具有完全的刺激效力。令人惊讶的是，其中His97被删除的肽类似物几乎是完全活性的。截短的、缺失的或取代的肽类似物不能区分使用不同α/β的7个T细胞克隆。β的T细胞受体。在λ 2315轻链中的91 - 101区不形成两亲性螺旋，即使这样的螺旋已被认为对T细胞表位是重要的。此外，由Rothbard和Taylor提出的T细胞免疫原性肽共有的基序对于E2315独特型肽不是必需的。与其他七种I-Ed限制性肽的比较显示，这些肽通常带正电荷，并且具有围绕中心聚集的两个碱性氨基酸。基于II类分子多肽结合位点的模型，我们认为这些带正电荷的残基可能与E β d链的114位（Glu）和155位（Asp）的带负电荷的残基相互作用。
We have defined the minimum length of a synthetic peptide which can activate I-Ed-restricted BALB/c T cell clones specific for a mutated self-antigen: an idiotope on the syngeneic .lambda.2315 immunoglobulin light chain. A peptide comprising residues 91-101 of the .lambda.2315 sequence had full stimulatory potency. Surprisingly, a peptide analogue in which His97 was deleted was almost fully active. Truncated, deleted or substituted peptide analogues did not distinguish between seven T cell clones that use different .alpha./.beta. T cell receptors. The 91-101 region in the .lambda.2315 light chain does not form an amphipathic helix even though such a helix has been suggested to be important for T cell epitopes. Further, a motif proposed by Rothbard and Taylor as being common to T cell immunogenic peptides is not necessary for the .lambda.2315 idiotypic peptide. Comparison with seven other I-Ed-restricted peptides revealed that the peptides are generally positively charged and have two basic amino acids clustered around the center. On the basis of a model of the class II molecule poeptide binding site, we suggest that these positively charged residues may interact with the negatively charged residues at positions 114(Glu) and 155(Asp) of the E.beta.d chain.