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Background The Fc region of IgG contains a single N-glycosylation site, which is known to be important for effecting immune activation through interaction with Fc receptors and complement molecules. Changes to the structure of these sugars can thus be very influential in determining the specific effector function of individual antibodies. Whereas therapeutic antibodies can be produced with particular effector functions in vitro, little is known regarding how glycosylation is regulated in primary B cells.

Antibody effector function is regulated by a combination of adaptive and innate signals