Mottez E, Langlade-Demoyen P, Gournier H, Martinon F, Maryanski J, Kourilsky P, Abastado J P
Unité de Biologie Moléculaire du Gène, INSERM U277, Paris, France.
J Exp Med. 1995 Feb 1;181(2):493-502. doi: 10.1084/jem.181.2.493.
The major histocompatibility complex (MHC) class I molecules expressed at the cell surface are associated with a large number of different peptides so that the density of a given MHC-peptide complex is relatively low. Here we describe the properties of MHC class I molecules genetically attached to a single antigenic peptide. Cells expressing these fusion proteins are recognized by T cells specific for the particular MHC-peptide complex. Coculture of naive splenocytes with cells expressing these MHC-peptide fusion proteins and the B7.1 antigen allows the induction of primary cytotoxic T lymphocytes (CTL) in vitro. Injection of these cells into naive mice enhances the frequency of specific CTL precursors and protects against a subsequent challenge with a tumor or a virus bearing the antigenic peptide. Soluble MHC-peptide fusions were also produced in which all three components, that is, the heavy chain, beta 2-microglobulin and the peptide, have fused into a single-chain protein. The availability of MHC class I molecules bound to a single peptide provides valuable tools for the manipulation of CTL responses and the analysis of the selection processes in the thymus.
细胞表面表达的主要组织相容性复合体（MHC）I类分子与大量不同的肽相关联，因此特定MHC-肽复合物的密度相对较低。在此，我们描述了与单一抗原肽基因连接的MHC I类分子的特性。表达这些融合蛋白的细胞被针对特定MHC-肽复合物的T细胞识别。幼稚脾细胞与表达这些MHC-肽融合蛋白和B7.1抗原的细胞共培养可在体外诱导初级细胞毒性T淋巴细胞（CTL）。将这些细胞注射到幼稚小鼠体内可提高特异性CTL前体的频率，并能抵御随后携带抗原肽的肿瘤或病毒的攻击。还制备了可溶性MHC-肽融合体，其中重链、β2-微球蛋白和肽这三个组分都融合成了单链蛋白。与单一肽结合的MHC I类分子的可得性为操纵CTL反应和分析胸腺中的选择过程提供了有价值的工具。
