Drijfhout J W, Brandt R M, D'Amaro J, Kast W M, Melief C J
Department of Immunohematology and Blood Bank, University Hospital Leiden, The Netherlands.
Hum Immunol. 1995 May;43(1):1-12. doi: 10.1016/0198-8859(94)00151-f.
Extensive sets of in total about 2000 synthetic peptides were investigated for their binding affinities to HLA-A0201. Comparisons of the amino acid compositions of binding to nonbinding sets of peptides provided new information concerning the rules for 9-, 10-, and 11-mer peptide binding at the amino acid level. Preferred primary anchors were shown to depend on peptide length, longer peptides being more demanding in this respect. A clear preference exists for certain amino acids at several nonanchor positions. In addition, the presence of particular amino acids at those positions almost completely precludes peptide binding. We found no evidence for preferred anchor pairs. From these results new and detailed HLA-A0201 peptide-binding motifs for 9-, 10-, and 11-mer peptide binding were deduced. The motifs are in accordance with earlier reports but include new findings, including C as a C-terminal anchor, the importance of D at positions 4 for binding, and the deleterious effect of R at position 5 (in 9-mers). The motifs are presented in such a way that they can be used to predict peptide binding to HLA-A*0201 by computer analysis (see accompanying paper [56]).
对总共约2000种合成肽的广泛集合进行了研究，以考察它们与HLA - A0201的结合亲和力。对结合和不结合肽集合的氨基酸组成进行比较，在氨基酸水平上提供了有关9肽、10肽和11肽结合规则的新信息。结果表明，优先一级锚定残基取决于肽的长度，在这方面较长的肽要求更高。在几个非锚定位置上，某些氨基酸存在明显偏好。此外，这些位置上特定氨基酸的存在几乎完全排除了肽的结合。我们没有发现优先锚定残基对的证据。从这些结果中推导得出了新的、详细的HLA - A0201肽结合基序，用于9肽、10肽和11肽的结合。这些基序与早期报告一致，但包括新的发现，包括C作为C末端锚定残基、第4位的D对结合的重要性以及第5位的R（在9肽中）的有害作用。这些基序以一种可通过计算机分析用于预测肽与HLA - A*0201结合的方式呈现（见随附论文[56]）。
