Antibodies to synthetic peptides corresponding to variable-region first-framework segments of T cell receptor. Detection of T cell products and cross-reactions with classical immunoglobulins.
Antibodies to synthetic peptides corresponding to variable-region first-framework segments of T cell receptor. Detection of T cell products and cross-reactions with classical immunoglobulins.
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对应于 T 细胞受体可变区第一框架片段的合成肽的抗体。
DOI：
10.1007/bf02919072
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发表时间：
1989
影响因子：
4.4
通讯作者：
Marchalonis,JJ
中科院分区：
文献类型：
--
作者：
Ross,CR;Hubbard,RA;Schluter,SF;Diamanduros,A;Wang,AC;Marchalonis,JJ
最近在基因水平上的研究表明，T细胞表达四种类型的T细胞受体的重排基因，这些T细胞受体在连接区和可变区的框架1（Fr1）和3段中与经典免疫球蛋白高度同源。基于基因序列中的同源性，可以得出基因产物将显示氨基酸序列和蛋白质折叠中的相似性，从而预期T细胞受体的可变区和经典免疫球蛋白之间的抗原决定簇中的交叉反应性。我们已经合成了与T细胞受体α、β和γ链的Fr1残基的预测蛋白质序列相对应的肽，并在兔中产生了针对这些合成肽的抗体。抗血清和亲和纯化的抗肽抗体的使用表明，可以提出高滴度的抗体是具体的个别Fr1肽。观察到T细胞受体Fr1肽段与免疫球蛋白轻链之间的交叉反应。此外，一些针对经典多克隆免疫球蛋白或亲和纯化的免疫球蛋白样T细胞受体的兔抗血清被发现对T细胞受体β和γ链的Fr1肽表现出结合活性。尽管T细胞受体和免疫球蛋白轻链的Fr1之间存在真实的序列同源性，但其同源性是中等的，并且抗原交叉反应必须反映存在的氨基酸的构型和类型。抗肽抗体的发展为表征各种T细胞来源的T细胞受体提供了希望，也为鉴定与重排免疫球蛋白相关的分子提供了新的手段。
Recent studies at the gene level have shown that T cells express rearranged genes for four types of T cell receptors that are strongly homologous to classical immunoglobulins in the joining region and in the framework 1 (Fr1) and 3 segments of the variable region. Based upon the homologies in gene sequence, it follows that the gene products would show similarities in amino acid sequence and in the folding of the proteins so that cross-reactivities in antigenic determinants would be expected between variable regions of the T cell receptors and classical immunoglobulins. We have synthesized peptides corresponding to predicted protein sequences of the Fr1 residues of T cell receptor α, β- and γ-chains and have produced antibodies in rabbits against these synthetic peptides. Use of antisera and affinity-purified antipeptide antibodies indicated that high-titer antibodies could be raised that were specific for individual Fr1 peptides. Cross-reactions among Fr1 peptides ofT cell receptors and immunoglobulin light chains were observed. In addition, some rabbit antisera raised against classical polyclonal immunoglobulins or affinity-purified immunoglobulin-like T cell receptors were found to exhibit binding activity against Fr1 peptides of T cell receptor β- and γ-chains. The sequence homology, although real among the Fr1 of T cell receptors and immunoglobulin light chains, is moderate and the antigenic cross-reaction must reflect the configuration and types of amino acids present. The development of antipeptide antibodies holds promise for the characterization of T cell receptors of various T cell sources and also offers a new means for the identification of molecules related to rearranging immunoglobulins.