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Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety functionality and efficacy

机译：治疗性IgG抗体的糖基化工程：安全性功能性和功效方面的挑战

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摘要

Glycosylation of the Fc region of IgG has a profound impact on the safety and clinical efficacy of therapeutic antibodies. While the biantennary complex-type oligosaccharide attached to Asn297 of the Fc is essential for antibody effector functions, fucose and outer-arm sugars attached to the core heptasaccharide that generate structural heterogeneity (glycoforms) exhibit unique biological activities. Hence, efficient and quantitative glycan analysis techniques have been increasingly important for the development and quality control of therapeutic antibodies, and glycan profiles of the Fc are recognized as critical quality attributes. In the past decade our understanding of the influence of glycosylation on the structure/function of IgG-Fc has grown rapidly through X-ray crystallographic and nuclear magnetic resonance studies, which provides possibilities for the design of novel antibody therapeutics. Furthermore, the chemoenzymatic glycoengineering approach using endoglycosidase-based glycosynthases may facilitate the development of homogeneous IgG glycoforms with desirable functionality as next-generation therapeutic antibodies. Thus, the Fc glycans are fertile ground for the improvement of the safety, functionality, and efficacy of therapeutic IgG antibodies in the era of precision medicine.
机译：IgG Fc区的糖基化对治疗性抗体的安全性和临床疗效具有深远影响。虽然连接至Fc的Asn297的双天线复合型寡糖对于抗体效应子功能必不可少，但连接至核心七糖的岩藻糖和外臂糖却产生结构异质性（糖型）表现出独特的生物学活性。因此，有效的和定量的聚糖分析技术对于治疗性抗体的开发和质量控制已变得越来越重要，并且Fc的聚糖谱被认为是关键的质量属性。在过去的十年中，通过X射线晶体学和核磁共振研究，我们对糖基化对IgG-Fc的结构/功能的影响的了解迅速增长，这为设计新型抗体疗法提供了可能性。此外，使用基于内切糖苷酶的糖合酶的化学酶促糖工程方法可以促进具有理想功能的均质IgG糖型作为下一代治疗性抗体的开发。因此，Fc聚糖是在精密医学时代改善治疗性IgG抗体的安全性，功能性和功效的沃土。

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