Journal
SCIENTIFIC REPORTS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-018-22199-8
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Funding
- grant of 'Research on Regulatory Science of Pharmaceuticals and Medical Devices' from AMED (Japan agency for medical research and development)
- JSPS KAKENHI [15K06962, 25249115]
- [16K18973]
- Grants-in-Aid for Scientific Research [15K06962, 25249115, 16H02420] Funding Source: KAKEN
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The N-glycan moiety of IgG-Fc has a significant impact on multifaceted properties of antibodies such as in their effector function, structure, and stability. Numerous studies have been devoted to understanding its biological effect since the exact composition of the Fc N-glycan modulates the magnitude of effector functions such as the antibody-dependent cell mediated cytotoxicity (ADCC), and the complement-dependent cytotoxicity (CDC). To date, systematic analyses of the properties and influence of glycan variants have been of great interest. Understanding the principles on how N-glycosylation modulates those properties is important for the molecular design, manufacturing, process optimization, and quality control of therapeutic antibodies. In this study, we have separated a model therapeutic antibody into three fractions according to the composition of the N-glycan by using a novel Fc gamma RIIIa chromatography column. Notably, Fc galactosylation was a major factor influencing the affinity of IgG-Fc to the Fc gamma RIIIa immobilized on the column. Each antibody fraction was employed for structural, biological, and physicochemical analysis, illustrating the mechanism by which galactose modulates the affinity to Fc gamma RIIIa. In addition, we discuss the benefits of the Fc gamma RIIIa chromatography column to assess the heterogeneity of the N-glycan.
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