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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Published inBiochimica et biophysica acta Vol. 1860; no. 8; pp. 1655 - 1668
Main Authors Le, Ngoc Phuong Lan, Bowden, Thomas A., Struwe, Weston B., Crispin, Max
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.08.2016
Elsevier Pub. Co
Subjects
antibodies
Antibody
autoimmunity
binding properties
blood serum
Effector function
engineering
Glycan
Glycosylation
Humans
Immunoglobulin Fc Fragments - genetics
Immunoglobulin Fc Fragments - metabolism
Immunoglobulin Fc Fragments - therapeutic use
immunoglobulin G
Immunoglobulin G - genetics
Immunoglobulin G - metabolism
Immunoglobulin G - therapeutic use
medicine
neoplasms
polysaccharides
Polysaccharides - genetics
Polysaccharides - metabolism
Protein Engineering - methods
receptors
Structure
Therapeutic antibodies
Glycosylation
Structure
Therapeutic antibodies
Antibody
Effector function
Glycan
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Abstract 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. •IgG glycosylation impacts antibody effector function.•Modulation of antibody glycosylation has therapeutic potential.•Antibody glycoforms exhibit anti- and pro-inflammatory properties.
AbstractList 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.
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. • IgG glycosylation impacts antibody effector function. • Modulation of antibody glycosylation has therapeutic potential. • Antibody glycoforms exhibit anti- and pro-inflammatory properties.
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. •IgG glycosylation impacts antibody effector function.•Modulation of antibody glycosylation has therapeutic potential.•Antibody glycoforms exhibit anti- and pro-inflammatory properties.
Author Crispin, Max
Le, Ngoc Phuong Lan
Struwe, Weston B.
Bowden, Thomas A.
AuthorAffiliation b Division of Structural Biology, University of Oxford, Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, United Kingdom
a Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
AuthorAffiliation_xml – name: b Division of Structural Biology, University of Oxford, Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, United Kingdom
– name: a Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
Author_xml – sequence: 1
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  fullname: Le, Ngoc Phuong Lan
  organization: Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
– sequence: 2
  givenname: Thomas A.
  surname: Bowden
  fullname: Bowden, Thomas A.
  organization: Division of Structural Biology, University of Oxford, Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, United Kingdom
– sequence: 3
  givenname: Weston B.
  surname: Struwe
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  organization: Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
– sequence: 4
  givenname: Max
  surname: Crispin
  fullname: Crispin, Max
  email: max.crispin@bioch.ox.ac.uk
  organization: Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
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RIG
TWZ
UHS
VH1
X7M
Y6R
YYP
ZE2
ZGI
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ISSN 0304-4165
0006-3002
IngestDate Thu Aug 21 14:13:59 EDT 2025
Thu Jul 10 21:12:10 EDT 2025
Fri Jul 11 05:08:07 EDT 2025
Mon Jul 21 06:03:53 EDT 2025
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Thu Apr 24 23:07:35 EDT 2025
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IsDoiOpenAccess true
IsOpenAccess true
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Issue 8
Keywords Glycosylation
Structure
Therapeutic antibodies
Antibody
Effector function
Glycan
Language English
License This is an open access article under the CC BY license.
Copyright © 2016 The Authors. Published by Elsevier B.V. All rights reserved.
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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  year: 2002
  ident: 10.1016/j.bbagen.2016.04.016_bb1345
  article-title: IRTAs: a new family of immunoglobulinlike receptors differentially expressed in B cells
  publication-title: Blood
  doi: 10.1182/blood.V99.8.2662
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Snippet Human serum IgG contains multiple glycoforms which exhibit a range of binding properties to effector molecules such as cellular Fc receptors. Emerging...
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SubjectTerms antibodies
Antibody
autoimmunity
binding properties
blood serum
Effector function
engineering
Glycan
Glycosylation
Humans
Immunoglobulin Fc Fragments - genetics
Immunoglobulin Fc Fragments - metabolism
Immunoglobulin Fc Fragments - therapeutic use
immunoglobulin G
Immunoglobulin G - genetics
Immunoglobulin G - metabolism
Immunoglobulin G - therapeutic use
medicine
neoplasms
polysaccharides
Polysaccharides - genetics
Polysaccharides - metabolism
Protein Engineering - methods
receptors
Structure
Therapeutic antibodies
Title Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies
URI https://dx.doi.org/10.1016/j.bbagen.2016.04.016
https://www.ncbi.nlm.nih.gov/pubmed/27105835
https://www.proquest.com/docview/1797257496
https://www.proquest.com/docview/1825430350
https://pubmed.ncbi.nlm.nih.gov/PMC4922387
Volume 1860
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