IgG isotypes can differentially bind to Fcγ receptors and complement, making the selection of
which isotype to pursue for development of a particular therapeutic antibody important in …

Abstract The Fc variant of IgG2, designated as IgG2σ, was engineered with
V234A/G237A/P238S/H268A/V309L/A330S/P331S substitutions to eliminate affinity for Fcγ …

Engineering of fragment crystallizable (Fc) domains of therapeutic immunoglobulin (IgG)
antibodies to eliminate their immune effector functions while retaining other Fc …

Upper hinge is vulnerable to radical attacks that result in breakage of the heavy-light chain
linkage and cleavage of the hinge of an IgG1. To further explore mechanisms responsible …

Therapeutic monoclonal antibodies are among the most effective biotherapeutics to date. An
important aspect of antibodies is their ability to bind antigen while at the same time recruit …

Recombinant human IgG antibodies (hIgGs) completely devoid of binding to Fcγ receptors
(FcγRs) and complement protein C1q, and thus with abolished immune effector functions …

Highlights•The antibody Fc domain engages immune-activating, inhibitory, and homeostatic
Fc receptors.•Fc domains are largely unaltered in existing therapeutic antibodies, whether to …

The Fc region of an antibody mediates effector functions such as antibody-dependent cell-
mediated cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC), and plays a …

Immunoglobulin G (IgG) Fc receptors play a critical role in linking IgG antibody-mediated
immune responses with cellular effector functions. A high resolution map of the binding site …

The binding sites on human IgG1 for human Fcγ receptor (FcγR) I, FcγRIIa, FcγRIIb, FcγRIIIa
and neonatal FcR have been mapped. A common set of IgG1 residues is involved in binding …