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Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()

Human serum IgG contains multiple glycoforms which exhibit a range of binding properties to effector molecules such as cellular Fc receptors. Emerging knowledge of how the Fc glycans contribute to the antibody structure and effector functions has opened new avenues for the exploitation of defined an...

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Detalles Bibliográficos
Autores principales: Le, Ngoc Phuong Lan, Bowden, Thomas A., Struwe, Weston B., Crispin, Max
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Pub. Co 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4922387/
https://www.ncbi.nlm.nih.gov/pubmed/27105835
http://dx.doi.org/10.1016/j.bbagen.2016.04.016
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author Le, Ngoc Phuong Lan
Bowden, Thomas A.
Struwe, Weston B.
Crispin, Max
author_facet Le, Ngoc Phuong Lan
Bowden, Thomas A.
Struwe, Weston B.
Crispin, Max
author_sort Le, Ngoc Phuong Lan
collection PubMed
description Human serum IgG contains multiple glycoforms which exhibit a range of binding properties to effector molecules such as cellular Fc receptors. Emerging knowledge of how the Fc glycans contribute to the antibody structure and effector functions has opened new avenues for the exploitation of defined antibody glycoforms in the treatment of diseases. Here, we review the structure and activity of antibody glycoforms and highlight developments in antibody glycoengineering by both the manipulation of the cellular glycosylation machinery and by chemoenzymatic synthesis. We discuss wide ranging applications of antibody glycoengineering in the treatment of cancer, autoimmunity and inflammation. This article is part of a Special Issue entitled "Glycans in personalised medicine" Guest Editor: Professor Gordan Lauc.
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spelling pubmed-49223872016-08-01 Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies() Le, Ngoc Phuong Lan Bowden, Thomas A. Struwe, Weston B. Crispin, Max Biochim Biophys Acta Article Human serum IgG contains multiple glycoforms which exhibit a range of binding properties to effector molecules such as cellular Fc receptors. Emerging knowledge of how the Fc glycans contribute to the antibody structure and effector functions has opened new avenues for the exploitation of defined antibody glycoforms in the treatment of diseases. Here, we review the structure and activity of antibody glycoforms and highlight developments in antibody glycoengineering by both the manipulation of the cellular glycosylation machinery and by chemoenzymatic synthesis. We discuss wide ranging applications of antibody glycoengineering in the treatment of cancer, autoimmunity and inflammation. This article is part of a Special Issue entitled "Glycans in personalised medicine" Guest Editor: Professor Gordan Lauc. Elsevier Pub. Co 2016-08 /pmc/articles/PMC4922387/ /pubmed/27105835 http://dx.doi.org/10.1016/j.bbagen.2016.04.016 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Le, Ngoc Phuong Lan
Bowden, Thomas A.
Struwe, Weston B.
Crispin, Max
Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()
title Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()
title_full Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()
title_fullStr Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()
title_full_unstemmed Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()
title_short Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()
title_sort immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies()
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4922387/
https://www.ncbi.nlm.nih.gov/pubmed/27105835
http://dx.doi.org/10.1016/j.bbagen.2016.04.016
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