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Complex genetic regulation of IgG glycosylation (106.1)
Author(s) -
Lauc Gordan
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.106.1
Subject(s) - glycosylation , glycan , antibody , fragment crystallizable region , immunoglobulin g , gene , biology , immune system , effector , immunoglobulin superfamily , n linked glycosylation , epitope , immunology , genetics , glycoprotein
Immunoglobulin G (IgG) is one of the key effectors of the immune system. Elaborate genetic mechanisms generate genes for variable regions of immunoglobulins, which can recognize virtually all foreign epitopes. Physiological mechanisms that regulate effector functions of IgG are even more complex, and glycosylation apparently plays a key role in them. Glycans attached to the conserved N‐glycosylation site of IgG heavy chains significantly alter structure of the IgG Fc region and direct IgG to different receptors. Slight modifications in structure of the attached IgG glycan can activate or block antibody‐dependent cellular cytotoxicity, or convert IgG from pro‐inflammatory into an anti‐inflammatory agent. By performing genome wide association study (GWAS) on over 10,000 individuals we identified a complex network of genes that associate with IgG glycosylation. The vast majority of these genes were previously not linked with glycosylation, but were found to be important in different inflammatory and autoimmune diseases. Affected IgG glycans are altered in these diseases, indicating that changes in IgG glycosylation could contribute to the development and course of many diseases.