Nose M, Wigzell H
Proc Natl Acad Sci U S A. 1983 Nov;80(21):6632-6. doi: 10.1073/pnas.80.21.6632.
We have prepared monoclonal hapten-specific mouse IgG2b antibodies depleted of asparagine-linked carbohydrate chains by treating the hybridoma cells with tunicamycin. The carbohydrate-deficient antibodies behaved in an identical manner to the normal antibodies with regard to fine antigen-binding reactivity (a Fab fragment feature) and protein A binding capacity [a feature requiring integrity at the CH2 and CH3 domain-interaction regions in the constant region of the heavy chain (CH)]. However, they lost the ability to activate complement, to bind to Fc receptors on macrophages, and to induce antibody-dependent cellular cytotoxicity. Furthermore, antigen-antibody complexes produced from such carbohydrate-deficient antibodies failed to be eliminated rapidly from the circulation. We conclude that removal of carbohydrate chains from IgG molecules may have a profound and highly select impact on the biological activity to these antibodies.
我们通过用衣霉素处理杂交瘤细胞，制备了去除了天冬酰胺连接的糖链的单克隆半抗原特异性小鼠IgG2b抗体。就精细抗原结合反应性（Fab片段特征）和蛋白A结合能力而言，缺乏碳水化合物的抗体与正常抗体表现相同[蛋白A结合能力是重链恒定区（CH）中CH2和CH3结构域相互作用区域完整性所需的特征]。然而，它们失去了激活补体、与巨噬细胞上的Fc受体结合以及诱导抗体依赖性细胞毒性的能力。此外，由这种缺乏碳水化合物的抗体产生的抗原-抗体复合物未能迅速从循环中清除。我们得出结论，从IgG分子中去除糖链可能对这些抗体的生物学活性产生深远且高度选择性的影响。
