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Fc gamma receptors (FcγRs) are a family of cell surface receptors on immune cells (including macrophages, monocytes, neutrophils, natural killer cells, and dendritic cells) that specifically bind the Fc region of IgG antibodies[1][2][3][4][5][6]. Upon binding IgG immune complexes, FcγRs mediate a broad array of immune effector functions, including pathogen phagocytosis, antigen uptake and presentation, antibody-dependent cellular cytotoxicity, and immunomodulation[1][2][3][4]. Signal transduction occurs through immunoreceptor tyrosine-based activation motifs (ITAMs) or inhibitory motifs (ITIMs) within their cytoplasmic domains or associated adaptor proteins[1][4]. These receptors bridge innate and adaptive immunity and are key in the clinical action of therapeutic antibodies—their subtypes and affinities influence efficacy and safety profiles in infectious disease, cancer, and autoimmunity[1][2][3][4][5]. Persistent or dysregulated FcγR activation can contribute to pathogenic inflammation and autoimmune disease, or promote disease enhancement in viral infections such as dengue[3][5].
Fc-mediated engagement of immune cells (phagocytosis, ADCC, antigen presentation); Modulation of immune responses via activating (ITAM-containing) and inhibitory (ITIM-containing) signaling
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