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.
Highlights
Antibodies, known as immunoglobulins (Ig), are naturally produced by plasma cells derived from B cells and play a key role in humoral immunity
This study indicates that Intravenous immunoglobulin (IVIg) can activate immunosuppressive pathways independently of B cells and CD22, it should not be misinterpreted as direct evidence against the ability of human CD22 to bind human sialylated immunoglobulin G (IgG) Fc (sFc)
The presence of oligosaccharides attached at a single site on the IgG Fc domain significantly influences antibody effector functions
Summary
Antibodies, known as immunoglobulins (Ig), are naturally produced by plasma cells derived from B cells and play a key role in humoral immunity. Human antibodies are classified into five isotypes (IgA, IgD, IgE, IgG and IgM) each with distinct structure and biological activity and the heavy chain within each class are designated α, δ, ε, γ and μ, respectively [1]. Among these five antibody isotypes, IgG has the longest serum half-life, is the most abundant (~ 75%) in circulation [2] and is the only isotype used in licensed recombinant monoclonal antibody therapeutics. We outline the current knowledge of structure-based IgG glycoform engineering
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