engleski

Fc-linked immunoglobulin G N-glycosylation in Fcγ receptor knock-out mice

Immunoglobulin G (IgG) is the most abundant immunoglobulin isotype in the blood and is involved in the pathogenesis and disease progression in various diseases. Glycosylation of the IgG Fc region is shown to vary in different physiological and pathological states. It can alter IgG’s effector functions by modulating its affinity for ligands, such as Fcγ receptors (FcγRs). The affinity of binding between IgG Fc regions and different FcγRs is dependent on the IgG subclass and the IgG Fc N- glycan composition. However, it is not known whether IgG glycosylation is affected by the available repertoire of FcγRs, and if Fc-linked N-glycome could compensate for modulation of IgG FcγR interaction. To explore this, we examined the subclass specific Fc IgG glycoprofiles of healthy male and female FcγR knock-out mice on C57BL/6 and BALB/c backgrounds. We observed slight changes in IgG Fc N-glycan profiles in different knock-outs, however, it seems that the strain background and sex have a stronger effect on N- glycosylation of IgG Fc regions than the FcγR repertoire.

Fcγ receptor ; IgG N-glycan profile ; immunoglobulin G ; N-glycosylation

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