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Biochim Biophys Acta. 2016 Aug;1860(8):1655-68. doi: 10.1016/j.bbagen.2016.04.016. Epub 2016 Apr 20.

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

Author information

1
Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
2
Division of Structural Biology, University of Oxford, Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX3 7BN, United Kingdom.
3
Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom. Electronic address: max.crispin@bioch.ox.ac.uk.

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.

KEYWORDS:

Antibody; Effector function; Glycan; Glycosylation; Structure; Therapeutic antibodies

PMID:
27105835
PMCID:
PMC4922387
DOI:
10.1016/j.bbagen.2016.04.016
[Indexed for MEDLINE]
Free PMC Article

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