Data Sheet 1_IgG N-glycosylation in autoimmune diseases.pdf

It carries a single conserved glycosylation site, Asparagine 297, in its Fc domain. This N-glycan is critical for the ability of the antibody to activate immune cells via binding to, and cross-linking Fc receptors in order to elicit functional responses.

First documented in the context of rheumatoid arthritis (RA), the IgG N-glycan may undergo changes that are correlated to host health. We present a narrative in-depth comparison of changes incurred by IgG N-glycans in autoimmune diseases; RA, systemic lupus erythematosus, multiple sclerosis, type I diabetes, primary biliary cholangitis and inflammatory bowel disease (Crohn’s disease and ulcerative colitis). Based on a systematic literature search, we identify common traits and features that are specific for any one autoimmune disease.