Sykulev Y, Cohen R J, Eisen H N
Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, USA.
Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):11990-2. doi: 10.1073/pnas.92.26.11990.
An analysis of the initial antigen-recognition step in the destruction of target cells by CD8+ cytolytic T lymphocytes (CTLs) shows that a relationship in the form of the law of mass action can be used to describe interactions between antigen-specific receptors on T cells (TCRs) and their natural ligands on target cells (peptide-major histocompatibility protein complexes, termed pepMHC complexes), even though these reactants are confined to their respective cell membranes. For a designated level of lysis and receptor affinities below about 5 X 10(6) M-1, the product of the required number of pepMHC complexes per target cell ("epitope density") and TCR affinity for pepMHC complexes is constant; therefore, over this range TCR affinities can be predicted from epitope densities (or vice versa). At higher receptor affinities ("affinity ceiling") the epitope density required for half-maximal lysis reaches a lower limit of less than 10 complexes per target cell.
对CD8 + 细胞毒性T淋巴细胞(CTL)破坏靶细胞过程中初始抗原识别步骤的分析表明,尽管这些反应物局限于各自的细胞膜,但质量作用定律形式的关系可用于描述T细胞上的抗原特异性受体(TCR)与其靶细胞上的天然配体(肽 - 主要组织相容性蛋白复合物,称为肽 - MHC复合物)之间的相互作用。对于低于约5×10⁶ M⁻¹的指定裂解水平和受体亲和力,每个靶细胞所需的肽 - MHC复合物数量(“表位密度”)与TCR对肽 - MHC复合物的亲和力之积是恒定的;因此,在此范围内,TCR亲和力可从表位密度预测(反之亦然)。在较高的受体亲和力(“亲和力上限”)下,半最大裂解所需的表位密度达到下限,即每个靶细胞少于10个复合物。