Journal
EXPERIMENTAL DERMATOLOGY
Volume 22, Issue 8, Pages 511-514Publisher
WILEY
DOI: 10.1111/exd.12171
Keywords
autoimmunity; B-Lymphocytes; glycosylation; IgG; self-tolerance
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Funding
- Swedish Research Council [2013-57x-20240]
- Foundation of Ake Wiberg
- Foundation of Alfred Osterlund
- Foundation of Petrus and Augusta Hedlund
- Foundation of Clas Groschinsky
- Foundation of Torsten och Ragnar Soderberg
- Swedish Society for Medicine
- Royal Physiografic Society in Lund
- King Gustaf V's 80 years fund
- Medical Faculty at Lund University
- Swedish governmental funding for clinical research (ALF)
- Hansa Medical AB
- German Research Foundation
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IgG antibodies have one conserved N-glycosylation site at Asn 297 in each of their constant heavy chain regions. These Fc glycans influence the overall structure and pro- or anti-inflammatory effector functions of IgG antibodies. The biantennary core glycan structure, consisting of four N-acetyl-glucosamine (GlcNAc) and three mannose residues, can be further decorated with fucose, a bisecting GlcNAc and terminal galactose or galactose plus sialic acid. Non-galactosylated (agalactosylated; G0) IgG antibodies have long been associated with pro-inflammatory effector functions in autoimmune patients with rheumatoid arthritis (RA). In contrast, it has been shown that sialylated IgGs are responsible for anti-inflammatory effects of intravenous immunoglobulin (IVIG; purified IgG from pooled human plasma), which is administered at high doses (2g/kg) for the systemic treatment of autoimmune patients. It has become increasingly evident that pro-inflammatory immune responses, such as autoimmune reactions, primarily induce antigen-specific G0 IgGs, whereas tolerance induces immunosuppressive galactosylated and sialylated IgGs. Under physiological conditions, differentially glycosylated IgGs mediate their pro- or anti-inflammatory effector functions obviously as immune complexes (IC) in an antigen-specific manner. Therefore, antigen-specific galactosylated and sialylated IgGs may be a promising therapeutic tool for re-establishing tolerance against defined (self-) antigens in autoimmune or allergic patients. Here, we summarize these findings and outline our viewpoint on the development and function of differentially glycosylated antigen-specific IgG antibodies.
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