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Impact of Glycosylation on Effector Functions of Therapeutic IgG †

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 o...

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Detalles Bibliográficos
Autores principales: Abès, Riad, Teillaud, Jean-Luc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3991024/
https://www.ncbi.nlm.nih.gov/pubmed/27713246
http://dx.doi.org/10.3390/ph3010146
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author Abès, Riad
Teillaud, Jean-Luc
author_facet Abès, Riad
Teillaud, Jean-Luc
author_sort Abès, Riad
collection PubMed
description 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.
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spelling pubmed-39910242014-04-18 Impact of Glycosylation on Effector Functions of Therapeutic IgG † Abès, Riad Teillaud, Jean-Luc Pharmaceuticals (Basel) Review 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. Molecular Diversity Preservation International 2010-01-12 /pmc/articles/PMC3991024/ /pubmed/27713246 http://dx.doi.org/10.3390/ph3010146 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Abès, Riad
Teillaud, Jean-Luc
Impact of Glycosylation on Effector Functions of Therapeutic IgG †
title Impact of Glycosylation on Effector Functions of Therapeutic IgG †
title_full Impact of Glycosylation on Effector Functions of Therapeutic IgG †
title_fullStr Impact of Glycosylation on Effector Functions of Therapeutic IgG †
title_full_unstemmed Impact of Glycosylation on Effector Functions of Therapeutic IgG †
title_short Impact of Glycosylation on Effector Functions of Therapeutic IgG †
title_sort impact of glycosylation on effector functions of therapeutic igg †
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3991024/
https://www.ncbi.nlm.nih.gov/pubmed/27713246
http://dx.doi.org/10.3390/ph3010146
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