《生命科学》 2017, 29(4): 319-330

IgG糖基化与疾病相关性研究进展

张　芳，许之珏，徐颖姣，邹　霞，张　延*

(上海交通大学系统生物医学研究院，系统生物医学教育部重点实验室，上海 200240)

摘　要：摘　要：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。

The glycosylation of immunoglobulin G and its alterations in diseases

ZHANG Fang， XU Zhi-Jue， XU Ying-Jiao， ZOU Xia， ZHANG Yan*

(Key Laboratory of Systems Biomedicine (Ministry of Education)， Shanghai Center for Systems Biomedicine， Shanghai Jiao Tong University， Shanghai 200240， China)

Abstract: Abstract: Immunoglobulin G (IgG) is the most important component of antibodies， and it is a glycoprotein. Glycosylation affects biological activities and biological functions through binding to Fc receptors or complement C1q. Systematic study of IgG glycosylation will deepen our understanding of IgG effector functions， and it has become a hotspot in cancer immunology as well as antibody drug discovery. Here， we focus on IgG glycosylation modification， effector functions of IgG glycans， the correlation between IgG glycosylation and various diseases， analytical methods of N-glycans and antibody glycoengineering. This review may help us to make further investigation into IgG glycosylation as well as its regulatory mechanism in various diseases， and improve the therapeutic effects of therapeutic antibody by modifying IgG glycosylation.