[Glycosylation of antibodies and their pathogenic effect]

Immunoglobulin G (IgG) has covalently linked a sugar chain in the crystallizable fragment (Fc). This structure consists of double stranded glycosidic complexes with a high degree of heterogeneity that contribute to define the affinity to their specific receptors, and partly determine their biological activity. Recently was identified an anti-inflammatory mechanism mediated by IgG based on their different alternatives of Fc glycosylation and their interaction with the specific adhesion receptor of dendritic cells (DC-SIGN). This mechanism has clinical and therapeutic implications in autoimmune diseases. The objective of this review is to describe the biochemical structure of sugars associated to the Fc of IgG and its variants in relation to specific functions and pathogenicity, particularly in tuberculosis, in which may also have therapeutic implication.