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

ABSTRACT: 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 an

SUBMITTER: Mimura Y 

PROVIDER: S-EPMC5777974 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature