Abstract
It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector functions, thereby possibly having a role in IgG modulation of allergic response. This is the first study investigating patients’ IgG glycosylation profile in allergic diseases. Subclass specific IgG glycosylation profile was analyzed in two cohorts of allergen sensitized and non-sensitized 3- to 11-year-old children (conducted at University of Aberdeen, UK and Children’s Hospital Srebrnjak, Zagreb, Croatia) with 893 subjects in total. IgG was isolated from serum/plasma by affinity chromatography on Protein G. IgG tryptic glycopeptides were analyzed by liquid chromatography electrospray ionization mass spectrometry. In the Zagreb cohort IgG glycome composition changed with age across all IgG subclasses. In both cohorts, IgG glycome composition did not differ in allergen sensitized subjects, nor children sensitized to individual allergens, single allergen mean wheal diameter or positive wheal sum values. In the Zagreb study the results were also replicated for high total serum IgE and in children with self-reported manifest allergic disease. In conclusion, our findings demonstrate no association between serum IgG glycome composition and allergic diseases in children.
Highlights
It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions
No association was found between IgG glycosylation pattern and sensitization to any single allergen, single allergen mean wheal diameter or positive wheal sum values (Supplemental Tables 1 and 2)
We report here the first study comparing the immunoglobulin glycosylation profiles of normal subjects with subjects suffering from allergic diseases
Summary
It is speculated that immunoglobulin G (IgG) plays a regulatory role in allergic reactions. The glycans on the Fc region are known to affect IgG effector functions, thereby possibly having a role in IgG modulation of allergic response. This is the first study investigating patients’ IgG glycosylation profile in allergic diseases. Glycans and glycan binding molecules play a major role in immune system regulation[18] as do IgG glycans They are of key importance for structural stabilization of the Fc region as well as for the IgG effector functions, affecting IgG binding affinity for FcγRs and other receptors[19,20,21,22,23]. Variation in IgG Fc N-glycan are known to affect the activity of therapeutic antibodies and intravenous immunoglobulin preparations[25,26]
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