Antibody Fc Glycosylation. IgG requires N-glycosylation at Asn297 in the CH2 domain of the Fc to adopt a functional conformation.
The structure-activity relationship of specific Fc-glycosylation characteristics on the pharmacokinetics and pharmacodynamics of mAbs is illustrated. An ensemble of pertinent references is also provided. The hypervariable complementarity determining region in the Fab domain can sometimes contain N-X-S/T sequons with N-glycans whose structure and role is less well understood than in the Fc domain. Different biopharmaceuticals such as hormones, blood-proteins, vaccines, growth factors, interferons and fusion proteins may each require distinct glycomic profiles for optimised function.