Schumacher T N, De Bruijn M L, Vernie L N, Kast W M, Melief C J, Neefjes J J, Ploegh H L
Department of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam.
Nature. 1991 Apr 25;350(6320):703-6. doi: 10.1038/350703a0.
Synthetic peptides have been used to sensitize target cells and thereby screen for epitopes recognized by T cells. Most epitopes of cytotoxic T lymphocytes can be mimicked by synthetic peptides of 12-15 amino acids. Although in specific cases, truncations of peptides improves sensitization of target cells, no optimum length for binding to major histocompatibility complex (MHC) class I molecules has been defined. We have now analysed synthetic peptide captured by empty MHC class I molecules of the mutant cell line RMA-S. We found that class I molecules preferentially bound short peptides (nine amino acids) and selectively bound these peptides even when they were a minor component in a mixture of longer peptides. These results may help to explain the difference in size restriction of T-cell epitopes between experiments with synthetic peptides and those with naturally processed peptides.
合成肽已被用于使靶细胞致敏，从而筛选出被T细胞识别的表位。细胞毒性T淋巴细胞的大多数表位可被12 - 15个氨基酸的合成肽模拟。尽管在特定情况下，肽的截短可提高靶细胞的致敏性，但尚未确定与主要组织相容性复合体（MHC）I类分子结合的最佳长度。我们现在分析了突变细胞系RMA - S的空MHC I类分子捕获的合成肽。我们发现I类分子优先结合短肽（九个氨基酸），并且即使它们是较长肽混合物中的次要成分，也能选择性地结合这些肽。这些结果可能有助于解释在合成肽实验和天然加工肽实验之间T细胞表位大小限制的差异。
