Matsui K, Boniface J J, Reay P A, Schild H, Fazekas de St Groth B, Davis M M
Howard Hughes Medical Institute, Stanford, CA.
Science. 1991 Dec 20;254(5039):1788-91. doi: 10.1126/science.1763329.
The interaction of antigen-specific T cell receptors (TCRs) with their ligands, peptides bound to molecules of the major histocompatibility complex (MHC), is central to most immune responses, yet little is known about its chemical characteristics. The binding to T cells of a labeled monoclonal antibody to the TCR was inhibited by soluble class II MHC heterodimers complexed to different peptides. Inhibition was both peptide- and TCR-specific and of low affinity, with a KD = 4 x 10(-5) to 6 x 10(-5) M, orders of magnitude weaker than comparable antibody-antigen interactions. This finding is consistent with the scanning nature of T cell recognition and suggests that antigen-independent adhesion precedes TCR engagement.
抗原特异性T细胞受体（TCRs）与其配体（即与主要组织相容性复合体（MHC）分子结合的肽段）之间的相互作用是大多数免疫反应的核心，但对其化学特性却知之甚少。与不同肽段复合的可溶性II类MHC异二聚体可抑制标记的抗TCR单克隆抗体与T细胞的结合。抑制作用具有肽段特异性和TCR特异性，且亲和力较低，解离常数（KD）为4×10⁻⁵至6×10⁻⁵ M，比类似的抗体 - 抗原相互作用弱几个数量级。这一发现与T细胞识别的扫描性质一致，并表明在TCR参与之前存在抗原非依赖性黏附。
