IgG-Fc N-glycosylation at Asn297 and IgA O-glycosylation in the hinge region in health and disease

Immunoglobulins (Igs) are the major molecules secreted by B lymphocytes during an adaptive immune response. They are glycoproteins with distinctive glycosylation patterns, resulting in wide variations in the number, type and location of their oligosaccharides in each isotype and subclass. The sugars play specific structural roles, maintaining and modulating effector functions of Igs. Aberrant glycosylation might contribute to disease pathogenesis. This review will focus on the glycosylation of IgG and IgA because they have been studied more extensively than other immunoglobulins. Rheumatoid arthritis and IgA nephritis are used to describe the association of glycosylation aberration and disease pathogenesis.