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免疫球蛋白G(IgG)是抗体的核心组成分子,是具有糖基化修饰的重要血清糖蛋白。糖基化修饰结构影响IgG与Fc受体或补体C1q结合,进而影响IgG的生物活性及生物学功能。IgG糖基化修饰的系统研究将拓展对其在免疫过程中效应功能的理解,是肿瘤免疫学及抗体药物开发领域的关注点。现从IgG糖基化修饰、IgG糖链的生物学功能及其与不同疾病的相关性、N-糖链分析方法和抗体糖基化工程四个方面进行综述,为进一步探究IgG糖基化与疾病调控机制以及通过改造IgG糖基化修饰进而改善治疗性抗体治疗效果等提供理论参考。
Immunoglobulin G (IgG) is a core component of antibodies and is an important serum glycoprotein with glycosylation. The glycosylation structure affects the binding of IgG to Fc receptors or complement C1q, which in turn affects the biological activity and biological function of IgG. Systematic studies on the glycosylation of IgG will broaden their understanding of the effector functions in the immune process and are of interest in the area of tumor immunology and antibody drug development. Now from the glycosylation of IgG, the biological function of IgG sugar chain and its relationship with different diseases, N-glycan analysis methods and antibody glycosylation engineering review from four aspects, in order to further explore the IgG glycosylation and Disease control mechanism and through the modification of IgG glycosylation modification and thus improve the therapeutic effect of therapeutic antibody provide theoretical reference.