Journal
PROTEIN & CELL
Volume 9, Issue 1, Pages 47-62Publisher
HIGHER EDUCATION PRESS
DOI: 10.1007/s13238-017-0433-3
Keywords
chemoenzymatic glycoengineering; crystal structure; endoglycosidase; fucose; glycosylation; intravenous immunoglobulin; sialic acid; transglycosylation; ultra performance liquid chromatography
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Funding
- JSPS KAKENHI [23590578]
- Science Foundation Ireland Starting Investigator Research grant (SFI SIRG) [13/SIRG/2164]
- EU FP7 program HighGlycan grant [278535]
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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.
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