Abstract
Multiple factors influence immunoglobulin G glycosylation, which in turn affect the glycoproteins’ function on eliciting an anti-inflammatory or pro-inflammatory response. It is prudent to underscore these processes when considering the use of immunoglobulin G N-glycan moieties as an indication of disease presence, progress, or response to therapeutics. It has been demonstrated that the altered expression of genes that encode enzymes involved in the biosynthesis of immunoglobulin G N-glycans, receptors, or complement factors may significantly modify immunoglobulin G effector response, which is important for regulating the immune system. The immunoglobulin G N-glycome is highly heterogenous; however, it is considered an interphenotype of disease (a link between genetic predisposition and environmental exposure) and so has the potential to be used as a dynamic biomarker from the perspective of predictive, preventive, and personalised medicine. Undoubtedly, a deeper understanding of how the multiple factors interact with each other to alter immunoglobulin G glycosylation is crucial. Herein we review the current literature on immunoglobulin G glycoprotein structure, immunoglobulin G Fc glycosylation, associated receptors, and complement factors, the downstream effector functions, and the factors associated with the heterogeneity of immunoglobulin G glycosylation.
Highlights
Immunoglobulin G (IgG) is an important effector glycoprotein linking the innate and adaptive branches of the immune system
Though this study contained participants from four populations (Orkney Islands in the UK, Vis and Korcula Islands in Croatia, Northern Sweden, and The Netherlands), one for validation (The Netherlands), there is still a considerable gap in knowledge regarding the association of specific loci and IgG glycosylation, and to what extent this can impact the final N-glycan moiety when compared with environmental factors
It is established that genetic and other factors influence IgG glycosylation, which in turn can affect whether the IgG glycoproteins will elicit an anti-inflammatory or pro-inflammatory response
Summary
Immunoglobulin G (IgG) is an important effector glycoprotein linking the innate and adaptive branches of the immune system. It has the ability to exert both anti-inflammatory and pro-inflammatory responses throughout the body, which are triggered by antigen recognition, and are dependent on its affinity for a number of different activating or inhibitory fragment crystallisable receptors (FcRs) and complement factors. This process mediates key effector functions, including pathogen clearance, antibody-dependent cell cytotoxicity (ADCC), and complement-initiated inflammation, all with both beneficial and detrimental effects depending on the premise of the IgG activity. Gar moieties, hereon known as N-glycans, affect the affinity of the Fc domain for a number of different FcRs, initiating different cellular events. This paper reviews the current literature on the IgG glycoprotein and its FcRs, as well as the factors associated with altered IgG glycosylation
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