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Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Immunol+Cell+Biol 2020 ; 98 (4): 287-304 Nephropedia Template TP
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Harnessing the immune system via FcgammaR function in immune therapy: a pathway to next-gen mAbs #MMPMID32157732
Chenoweth AM; Wines BD; Anania JC; Mark Hogarth P
Immunol Cell Biol 2020[Apr]; 98 (4): 287-304 PMID32157732show ga
The human fragment crystallizable (Fc)gamma receptor (R) interacts with antigen-complexed immunoglobulin (Ig)G ligands to both activate and modulate a powerful network of inflammatory host-protective effector functions that are key to the normal physiology of immune resistance to pathogens. More than 100 therapeutic monoclonal antibodies (mAbs) are approved or in late stage clinical trials, many of which harness the potent FcgammaR-mediated effector systems to varying degrees. This is most evident for antibodies targeting cancer cells inducing antibody-dependent killing or phagocytosis but is also true to some degree for the mAbs that neutralize or remove small macromolecules such as cytokines or other Igs. The use of mAb therapeutics has also revealed a "scaffolding" role for FcgammaR which, in different contexts, may either underpin the therapeutic mAb action such as immune agonism or trigger catastrophic adverse effects. The still unmet therapeutic need in many cancers, inflammatory diseases or emerging infections such as severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) requires increased effort on the development of improved and novel mAbs. A more mature appreciation of the immunobiology of individual FcgammaR function and the complexity of the relationships between FcgammaRs and antibodies is fueling efforts to develop more potent "next-gen" therapeutic antibodies. Such development strategies now include focused glycan or protein engineering of the Fc to increase affinity and/or tailor specificity for selective engagement of individual activating FcgammaRs or the inhibitory FcgammaRIIb or alternatively, for the ablation of FcgammaR interaction altogether. This review touches on recent aspects of FcgammaR and IgG immunobiology and its relationship with the present and future actions of therapeutic mAbs.