Pierres A, Schmitt-Verhulst A M, Buferne M, Golstein P, Pierres M
Scand J Immunol. 1982 Jun;15(6):619-25. doi: 10.1111/j.1365-3083.1982.tb00691.x.
We have characterized a cytolytic T-cell clone, isolated from a A.TH anti-A.TL mixed lymphocyte culture, which recognized a private determinant of the I-Ak molecule. This specificity has been confirmed by inhibition of effector-target cell interaction by anti-I-Ak monoclonal antibody (mAb). Comparison of the inhibitory capacity of various mAb and the spatial arrangement of their epitopes (defined in previous studies by antibody-binding competition) indicated that the antigenic site recognized by this cytolytic T-cell clone was topologically related to one of the major polymorphic domains of the Ak molecule. This clone expressed the Thy-1.2+, Lyt-1.+, Lyt-1.2+low and I-As- cell surface phenotype. Testing of several rat mAb, screened for their ability to inhibit H-2K/D-specific cytolysis at the level of the effector cells, revealed that two anti-p94, 180 mAb but not various anti-Lyt-2 mAb inhibited the lytic function of this anti-I-Ak T-cell clone.
我们鉴定了一个细胞溶解型T细胞克隆，它从A.TH抗A.TL混合淋巴细胞培养物中分离得到，能识别I-Ak分子的一个私有决定簇。抗I-Ak单克隆抗体（mAb）对效应细胞与靶细胞相互作用的抑制作用证实了这种特异性。比较各种mAb的抑制能力及其表位的空间排列（先前研究通过抗体结合竞争确定）表明，该细胞溶解型T细胞克隆识别的抗原位点在拓扑结构上与Ak分子的一个主要多态结构域相关。该克隆表达Thy-1.2+、Lyt-1.+、Lyt-1.2+低表达和I-As-细胞表面表型。对几种大鼠mAb进行测试，筛选它们在效应细胞水平抑制H-2K/D特异性细胞溶解的能力，结果显示两种抗p94、180 mAb而非各种抗Lyt-2 mAb抑制了这个抗I-Ak T细胞克隆的溶解功能。
