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Impact of Glycosylation on Effector Functions of Therapeutic IgG†
INSERM UMRS 872, Paris, F-75006 France
Cordeliers Research Center, Université Pierre & Marie Curie, UMRS 872, Paris, F-75006, France
Université Paris-Descartes, UMRS 872, Paris, F-75006 France
Laboratoire français du Fractionnement et des Biotechnologies (LFB), Les Ulis, France
† Paper published on Special Issue “Monoclonal Antibody”, edited by Jagadeesh Bayry.
* Author to whom correspondence should be addressed.
Received: 15 December 2009; in revised form: 30 December 2009 / Accepted: 8 January 2010 / Published: 12 January 2010
Abstract: Human IgG has only one conserved glycosylation site located in the Cγ2 domain of the Fc region that accounts for the presence of two sugar moieties per IgG. These IgG sugar cores play a critical role in a number of IgG effector functions. In the present review, we describe the main characteristics of IgG Fc glycosylation and some abnormalities of serum IgG glycosylation. We also discuss how glycosylation impacts on monoclonal antibodies (mAbs) and IVIg effector functions and how these molecules can be engineered. Several therapeutic antibodies have now been engineered to be no- or low-fucose antibodies and are currently tested in clinical trials. They exhibit an increased binding to activating FcγRIIIA and trigger a strong antibody-dependent cell cytotoxicity (ADCC) as compared to their highly-fucosylated counterparts. They represent a new generation of therapeutic antibodies that are likely to show a better clinical efficacy in patients, notably in cancer patients where cytotoxic antibodies are needed.
Keywords: antibody; Fc receptor; glycosylation; IgG
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Cite This Article
MDPI and ACS Style
Abès, R.; Teillaud, J.-L. Impact of Glycosylation on Effector Functions of Therapeutic IgG. Pharmaceuticals 2010, 3, 146-157.
Abès R, Teillaud J-L. Impact of Glycosylation on Effector Functions of Therapeutic IgG. Pharmaceuticals. 2010; 3(1):146-157.
Abès, Riad; Teillaud, Jean-Luc. 2010. "Impact of Glycosylation on Effector Functions of Therapeutic IgG." Pharmaceuticals 3, no. 1: 146-157.