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

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 …

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 …

All clinically approved antibodies are of the IgG isotype and mediate the clearance of target
cells via binding to Fcγ receptors and complement (C1q). Even though IgA can elicit …

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 …

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

Elimination of the binding of immunoglobulin Fc to Fc gamma receptors (FcγR) is highly
desirable for the avoidance of unwanted inflammatory responses to therapeutic antibodies …

Engineered crystallizable fragment (Fc) regions of antibody domains, which assume a
unique and unprecedented asymmetric structure within the homodimeric Fc polypeptide …

Abstract Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an
attractive approach for improving the efficacy of antibody therapeutics. However, the …