Falk K, Rötzschke O, Stevanović S, Gnau V, Sparbier K, Jung G, Rammensee H G, Walden P
Max-Planck-Institut für Biologie, Abteilung Immungenetik, Universität Tübingen, Germany.
Immunology. 1994 Jul;82(3):337-42.
A previously described nonapeptide sequence motif for antigens recognized by T cells in the context of the human major histocompatibility complex (MHC) molecule HLA-A2.1 was used to identify the natural epitope of influenza A virus matrix protein. We show here that the peptide with the sequence GILGFVFTL is the synthetic analogue of the natural epitope by demonstrating the presence of the corresponding peptide on MHC molecules of virus-infected cells. The role of the hydrophobic anchor amino acids in positions 2 and 9, which constitute the epitope motif, was investigated with synthetic variants of the epitope and cytotoxic T lymphocytes as indicator cells. The crucial role of the side chains of amino acids in those positions was evidence by their influence on the efficiency of T-cell stimulation.
一种先前描述的、用于在人类主要组织相容性复合体（MHC）分子HLA - A2.1背景下被T细胞识别的抗原的九肽序列基序，被用于鉴定甲型流感病毒基质蛋白的天然表位。我们在此表明，序列为GILGFVFTL的肽是天然表位的合成类似物，这是通过证明病毒感染细胞的MHC分子上存在相应肽来实现的。以表位的合成变体和细胞毒性T淋巴细胞作为指示细胞，研究了构成表位基序的第2位和第9位疏水锚定氨基酸的作用。这些位置氨基酸侧链的关键作用通过它们对T细胞刺激效率的影响得到了证实。
