Weber S, Traunecker A, Oliveri F, Gerhard W, Karjalainen K
Basel Institute for Immunology, Switzerland.
Nature. 1992 Apr 30;356(6372):793-6. doi: 10.1038/356793a0.
The T-cell receptor is necessary and sufficient for recognition of peptides presented by major histocompatibility complex molecules. Other adhesion molecules, like CD4 or CD8, play an auxiliary role in antigen recognition by T cells. Here we analyse T-cell receptor (TCR) binding using a soluble rather than a cell-bound receptor molecule. A TCR-immunoglobulin chimaera is constructed with the variable and the first constant regions of both the TCR alpha- and beta-chains linked to the immunoglobulin light-chain constant regions. This soluble TCR is expressed, assembled and secreted as an alpha beta heterodimer by a myeloma cell line transfected with the recombinant genes. Furthermore, the soluble TCR is biologically active: it specifically inhibits antigen-dependent activation of the relevant T-cell clones and thus discriminates between proper and irrelevant peptides presented by major histocompatibility complex molecules.
T细胞受体对于识别主要组织相容性复合体分子所呈递的肽段而言是必要且充分的。其他黏附分子，如CD4或CD8，在T细胞的抗原识别中起辅助作用。在此，我们使用可溶性而非细胞结合型受体分子来分析T细胞受体（TCR）的结合情况。构建一种TCR-免疫球蛋白嵌合体，其中TCRα链和β链的可变区及第一个恒定区与免疫球蛋白轻链恒定区相连。这种可溶性TCR由转染了重组基因的骨髓瘤细胞系表达、组装并分泌为αβ异二聚体。此外，可溶性TCR具有生物学活性：它能特异性抑制相关T细胞克隆的抗原依赖性激活，从而区分主要组织相容性复合体分子所呈递的合适与不合适的肽段。
