Sitkovsky M V, Pasternack M S, Eisen H N
J Immunol. 1982 Oct;129(4):1372-6.
Several lectins were tested for the ability to interfere with the recognition or lysis of target cells by cytotoxic T lymphocytes (CTL). Of those tested, concanavalin A (Con A) had the greatest effect: at 0.25 to 10 micrograms/ml, it profoundly blocked antigen-specific lysis of target cells by cloned and uncloned CTL in various allo- and syngeneic systems. Separate pretreatment of CTL and target cells showed that the effect of Con A is exercised predominantly on CTL. Various experimental results ruled out several possible explanations for the inhibitory effect of Con A, such as: CTL-CTL self-killing by nonspecific, lectin-dependent cytotoxicity, impairment of lateral mobility of CTL surface components, and cell agglutination, preventing recycling of CTL among target cells. The findings suggest that subagglutinating concentrations of Con A block CTL activity by binding to and interfering with CTL surface structures that have relatively high affinity for Con A and are critically involved in recognition or lysis of target cells.
测试了几种凝集素干扰细胞毒性T淋巴细胞(CTL)对靶细胞识别或裂解的能力。在测试的凝集素中,伴刀豆球蛋白A(Con A)的效果最为显著:在0.25至10微克/毫升的浓度下,它能在各种同种异体和同基因系统中,显著阻断克隆的和未克隆的CTL对靶细胞的抗原特异性裂解。对CTL和靶细胞进行单独预处理表明,Con A的作用主要施加于CTL。各种实验结果排除了对Con A抑制作用的几种可能解释,例如:CTL通过非特异性、凝集素依赖性细胞毒性进行自我杀伤,CTL表面成分侧向流动性受损,以及细胞凝集,从而阻止CTL在靶细胞之间循环利用。研究结果表明,亚凝集浓度的Con A通过与对Con A具有相对高亲和力且在识别或裂解靶细胞中起关键作用的CTL表面结构结合并干扰,从而阻断CTL活性。