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Murine Fc gamma receptors (mFcγRs) are a group of cell surface proteins that recognize the Fc portion of IgG antibodies, bridging the adaptive and innate immune systems [1]. The family consists of activating receptors (FcγRI, FcγRIII, and FcγRIV) and one inhibitory receptor (FcγRIIB), which together maintain immune homeostasis [2]. These receptors are widely expressed on myeloid cells and certain lymphoid cells, where they trigger phagocytosis, degranulation, and antibody-dependent cellular cytotoxicity (ADCC) [3]. In therapeutic contexts, mFcγRs are pivotal for the activity of monoclonal antibodies used in cancer and autoimmune research, as they dictate the recruitment of effector cells to the target [4]. Preclinical studies often utilize mouse models to evaluate antibody-based drugs, but researchers must account for the distinct binding affinities of murine receptors compared to their human counterparts [5]. For instance, murine FcγRIV is a potent activator with no direct human ortholog, which can lead to discrepancies in drug efficacy and safety profiles during translation [2]. Targeting or modulating these receptors is a strategy for treating inflammatory diseases and enhancing the potency of anti-tumor antibodies [5].
Binding to the Fc region of IgG antibodies to modulate immune effector functions via immunoreceptor tyrosine-based activation motifs (ITAM) in activating receptors or inhibitory motifs (ITIM) in the inhibitory receptor.
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