PMC:7228307 / 1587-2551 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7228307","sourcedb":"PMC","sourceid":"7228307","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7228307","text":"cused glycan or protein engineering of the Fc to increase affinity and/or tailor specificity for selective engagement of individual activating FcγRs or the inhibitory FcγRIIb or alternatively, for the ablation of FcγR interaction altogether. This review touches on recent aspects of FcγR and IgG immunobiology and its relationship with the present and future actions of therapeutic mAbs.\n\nFragment crystallizable (Fc) receptors for immunoglobulin (Ig)G activate and modulate a powerful network of inflammatory, host‐protective effector functions that are central to effective and balanced immune responses. These responses are also harnessed—or avoided—by therapeutic monoclonal antibodies. The use and manipulation of IgG2, IgG4 as well as IgG1 for optimized activating or inhibitory FcγR effector functions will underpin the development of potent \"next‐gen\" antibody therapeutics.\n\nIntroduction\nThe regulatory approval of the first therapeutic monoclonal 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