Historically, antibodies have been divided into two functionally independent domains, the variable (V) region for antigen binding and the constant (C) region for mediating effector functions. However, this classical view of antibody function has been severely challenged by a large and growing number of studies, which reveal long-range conformational interactions and allosteric links between the V and C regions. This review comprehensively summarizes the existing studies on antibody allostery, including allosteric conformational changes induced by covalent modifications or noncovalent ligand binding. In addition, we discuss how intramolecular allosteric signals are transmitted from the V to C regions and vice versa. This review argues that there is sufficient evidence to revisit the structure-function relationship of antibodies. These advances in antibody allostery will provide a blueprint for regulating antibody functions in a simple and highly predictable manner. More focus on antibody allostery will definitely benefit antibody engineering and vaccine design in the field of biotechnology.

中文翻译：

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抗体特性的非经典观点：可变区和恒定区之间的变构效应


从历史上看，抗体分为两个功能独立的结构域，用于抗原结合的可变 （V） 区和用于介导效应子功能的恒定 （C） 区。然而，这种关于抗体功能的经典观点受到了大量且不断增长的研究的严重挑战，这些研究揭示了 V 区和 C 区之间的长程构象相互作用和变构连接。本文全面总结了现有的抗体变构研究，包括共价修饰或非共价配体结合诱导的变构构象变化。此外，我们还讨论了分子内变构信号如何从 V 区传递到 C 区，反之亦然。本综述认为，有足够的证据重新审视抗体的结构-功能关系。抗体变构的这些进展将为以简单且高度可预测的方式调节抗体功能提供蓝图。更多地关注抗体变构肯定会有利于生物技术领域的抗体工程和疫苗设计。