Fc gamma receptors: glycobiology and therapeutic prospects

Jerrard M Hayes,1 Mark R Wormald,2 Pauline M Rudd,3 Gavin P Davey1 1School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College, Dublin, Ireland; 2Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, Oxford, UK; 3NIBRT Glycoscience Group,...

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Autores principales:	Hayes JM, Wormald MR, Rudd PM, Davey GP
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2016
Materias:	Glycosylation IgG Fc gamma receptor therapeutic monoclonal antibody Pathology RB1-214 Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/b4d1d567fa39453a82270b36ecab4b9f
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spelling	oai:doaj.org-article:b4d1d567fa39453a82270b36ecab4b9f2021-12-02T00:12:38ZFc gamma receptors: glycobiology and therapeutic prospects1178-7031https://doaj.org/article/b4d1d567fa39453a82270b36ecab4b9f2016-11-01T00:00:00Zhttps://www.dovepress.com/fc-gamma-receptors-glycobiology-and-therapeutic-prospects-peer-reviewed-article-JIRhttps://doaj.org/toc/1178-7031Jerrard M Hayes,1 Mark R Wormald,2 Pauline M Rudd,3 Gavin P Davey1 1School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College, Dublin, Ireland; 2Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, Oxford, UK; 3NIBRT Glycoscience Group, National Institute for Bioprocessing, Research and Training, Dublin, Ireland Abstract: Therapeutic antibodies hold great promise for the treatment of cancer and autoimmune diseases, and developments in antibody–drug conjugates and bispecific antibodies continue to enhance treatment options for patients. Immunoglobulin (Ig) G antibodies are proteins with complex modifications, which have a significant impact on their function. The most important of these modifications is glycosylation, the addition of conserved glycans to the antibody Fc region, which is critical for its interaction with the immune system and induction of effector activities such as antibody-dependent cell cytotoxicity, complement activation and phagocytosis. Communication of IgG antibodies with the immune system is controlled and mediated by Fc gamma receptors (FcγRs), membrane-bound proteins, which relay the information sensed and gathered by antibodies to the immune system. These receptors are also glycoproteins and provide a link between the innate and adaptive immune systems. Recent information suggests that this receptor glycan modification is also important for the interaction with antibodies and downstream immune response. In this study, the current knowledge on FcγR glycosylation is discussed, and some insight into its role and influence on the interaction properties with IgG, particularly in the context of biotherapeutics, is provided. For the purpose of this study, other Fc receptors such as FcαR, FcεR or FcRn are not discussed extensively, as IgG-based antibodies are currently the only therapeutic antibody-based products on the market. In addition, FcγRs as therapeutics and therapeutic targets are discussed, and insight into and comment on the therapeutic aspects of receptor glycosylation are provided. Keywords: glycosylation, IgG, Fc gamma receptor, therapeutic monoclonal antibodyHayes JMWormald MRRudd PMDavey GPDove Medical PressarticleGlycosylationIgGFc gamma receptortherapeutic monoclonal antibodyPathologyRB1-214Therapeutics. PharmacologyRM1-950ENJournal of Inflammation Research, Vol Volume 9, Pp 209-219 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Glycosylation IgG Fc gamma receptor therapeutic monoclonal antibody Pathology RB1-214 Therapeutics. Pharmacology RM1-950
spellingShingle	Glycosylation IgG Fc gamma receptor therapeutic monoclonal antibody Pathology RB1-214 Therapeutics. Pharmacology RM1-950 Hayes JM Wormald MR Rudd PM Davey GP Fc gamma receptors: glycobiology and therapeutic prospects
description	Jerrard M Hayes,1 Mark R Wormald,2 Pauline M Rudd,3 Gavin P Davey1 1School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College, Dublin, Ireland; 2Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, Oxford, UK; 3NIBRT Glycoscience Group, National Institute for Bioprocessing, Research and Training, Dublin, Ireland Abstract: Therapeutic antibodies hold great promise for the treatment of cancer and autoimmune diseases, and developments in antibody–drug conjugates and bispecific antibodies continue to enhance treatment options for patients. Immunoglobulin (Ig) G antibodies are proteins with complex modifications, which have a significant impact on their function. The most important of these modifications is glycosylation, the addition of conserved glycans to the antibody Fc region, which is critical for its interaction with the immune system and induction of effector activities such as antibody-dependent cell cytotoxicity, complement activation and phagocytosis. Communication of IgG antibodies with the immune system is controlled and mediated by Fc gamma receptors (FcγRs), membrane-bound proteins, which relay the information sensed and gathered by antibodies to the immune system. These receptors are also glycoproteins and provide a link between the innate and adaptive immune systems. Recent information suggests that this receptor glycan modification is also important for the interaction with antibodies and downstream immune response. In this study, the current knowledge on FcγR glycosylation is discussed, and some insight into its role and influence on the interaction properties with IgG, particularly in the context of biotherapeutics, is provided. For the purpose of this study, other Fc receptors such as FcαR, FcεR or FcRn are not discussed extensively, as IgG-based antibodies are currently the only therapeutic antibody-based products on the market. In addition, FcγRs as therapeutics and therapeutic targets are discussed, and insight into and comment on the therapeutic aspects of receptor glycosylation are provided. Keywords: glycosylation, IgG, Fc gamma receptor, therapeutic monoclonal antibody
format	article
author	Hayes JM Wormald MR Rudd PM Davey GP
author_facet	Hayes JM Wormald MR Rudd PM Davey GP
author_sort	Hayes JM
title	Fc gamma receptors: glycobiology and therapeutic prospects
title_short	Fc gamma receptors: glycobiology and therapeutic prospects
title_full	Fc gamma receptors: glycobiology and therapeutic prospects
title_fullStr	Fc gamma receptors: glycobiology and therapeutic prospects
title_full_unstemmed	Fc gamma receptors: glycobiology and therapeutic prospects
title_sort	fc gamma receptors: glycobiology and therapeutic prospects
publisher	Dove Medical Press
publishDate	2016
url	https://doaj.org/article/b4d1d567fa39453a82270b36ecab4b9f
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Fc gamma receptors: glycobiology and therapeutic prospects

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