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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.

Original publication

DOI

10.1016/j.bbagen.2016.04.016

Type

Journal article

Journal

Biochim Biophys Acta

Publication Date

08/2016

Volume

1860

Pages

1655 - 1668

Keywords

Antibody, Effector function, Glycan, Glycosylation, Structure, Therapeutic antibodies, Glycosylation, Humans, Immunoglobulin Fc Fragments, Immunoglobulin G, Polysaccharides, Protein Engineering