Improving Antibody Therapeutics by Manipulating the Fc Domain: Immunological and Structural Considerations.

ABSTRACT: Interactions between the crystallizable fragment (Fc) domain of antibodies and a plethora of cellular Fc receptors (FcRs) or soluble proteins form a critical link between humoral and innate immunity. In particular, the immunoglobulin G Fc domain is critical for the clearance of target cells by processes that include (a) cytotoxicity, phagocytosis, or complement lysis; (b) modulation of inflammation; (c) antigen presentation; (d) antibody-mediated receptor clustering; and (e) cytokine release. More than 30 Fc-engineered antibodies aimed primarily at tailoring these effects for optimal therapeutic outcomes are in clinical evaluation or have already been approved. Nonetheless, our understanding of how FcR engagement impacts various immune cell phenotypes is

SUBMITTER: Delidakis G 

PROVIDER: S-EPMC9648538 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature