Gundlach B R, Wiesmüller K H, Junt T, Kienle S, Jung G, Walden P
Max Planck Institute for Biology, Section of Immunogenetics, Tubingen, Germany.
J Immunol. 1996 May 15;156(10):3645-51.
Random peptide libraries were employed to investigate the specificity of Ag recognition by H-3-specific, H-2K(b)-restricted CTL clones. The peptide libraries consist of octapeptides with one defined sequence position and mixtures of 19 amino acids (all proteinogenic amino acids except for cysteine) in the remaining seven sequence positions. The complete set of 152 peptide libraries includes all octapeptides possible with these amino acids. Responses of the CTL clones to these peptide libraries reveal patterns of preferred epitope amino acids. Depending on the CTL clone tested, varying numbers of different amino acids were identified for the different sequence positions indicating degeneracy of Ag recognition. Sequences for synthetic epitopes active at low pM concentrations could be deduced from these patterns. They confirm that TCRs of CTL clones do not exhibit specificity for unique ligand structures but rather can interact with sets of ligands. The sequences of peptides recognized by a single clone exhibit great sequence heterogeneity.
利用随机肽库研究H-3特异性、H-2K(b)限制的CTL克隆对Ag识别的特异性。肽库由一个确定序列位置的八肽和其余七个序列位置的19种氨基酸（除半胱氨酸外的所有蛋白ogenic氨基酸）混合物组成。152个肽库的完整集合包括这些氨基酸可能形成的所有八肽。CTL克隆对这些肽库的反应揭示了优先表位氨基酸的模式。根据所测试的CTL克隆，不同序列位置鉴定出不同数量的不同氨基酸，表明Ag识别具有简并性。可以从这些模式推导出在低pM浓度下具有活性的合成表位的序列。它们证实CTL克隆的TCR对独特的配体结构不具有特异性，而是可以与配体集合相互作用。单个克隆识别的肽序列表现出很大的序列异质性。
