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 …

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

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 …

Engineering the antibody Fc region to enhance the cytotoxic activity of therapeutic
antibodies is currently an active area of investigation. The contribution of complement to the …

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

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 …

Monoclonal antibodies (mAbs) are one of the most widely used drug platforms for infectious
diseases or cancer therapeutics because they selectively target pathogens, infectious cells …

The contribution of Fc-mediated effector functions to the therapeutic efficacy of some
monoclonal antibodies has motivated efforts to enhance interactions with Fcγ receptors …

The use of antibody therapy for cancer has steadily increased in recent years and has
become standard treatment for numerous tumor types. It is now appreciated that the clinical …

The monospecific and bivalent characteristics of naturally occurring immunoglobulin G (IgG)
antibodies depend on homodimerization of the fragment crystallizable (Fc) regions of two …