Fc-gamma receptor and neonatal Fc receptor complex (FcR/FcRn)

The target "Immune cells via multiple surface receptors and Fc interactions" refers to the complex network of interactions between the Fc (fragment crystallizable) region of antibodies and various receptors, primarily Fc-gamma receptors (FcγRs) and the neonatal Fc receptor (FcRn), expressed on immune cells (Nimmerjahn & Ravetch, Nature Reviews Immunology, 2008). These interactions are central to the immune system's ability to bridge humoral and cellular immunity, mediating processes such as antibody-dependent cellular cytotoxicity (ADCC), phagocytosis, and the regulation of inflammatory signaling (Hogarth & Pietersz, Nature Reviews Drug Discovery, 2012). FcRn specifically regulates the homeostasis of IgG by protecting it from degradation, thereby extending its circulatory half-life (Roopenian & Akilesh, Nature Reviews Immunology, 2007). In clinical practice, this system is the primary target of intravenous immunoglobulin (IVIG) therapy, which acts by saturating these receptors to suppress autoimmune responses and neutralize pathogenic autoantibodies (Samuelsson et al., Science, 2001). Modern therapeutic strategies also include Fc-engineered monoclonal antibodies designed to enhance effector functions in oncology or FcRn-specific antagonists like efgartigimod that rapidly deplete autoantibodies in conditions like myasthenia gravis (Gable & Guptill, Frontiers in Neurology, 2022). Understanding these multi-receptor interactions is crucial for developing biologics with optimized safety and efficacy profiles (Saunders, Frontiers in Immunology, 2019).

Other names

Fc receptorsFc gamma receptorsFcRnNeonatal Fc receptorCD16CD32CD64Fc-gamma-R

Modulation of immune cell activity through binding of antibody Fc regions to surface receptors (FcγRs) and the neonatal Fc receptor (FcRn), leading to altered signaling, clearance of autoantibodies, or enhanced effector functions.