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The term Multiple exogenous antigens and endogenous immune receptors does not refer to a single molecular entity but rather describes the broad pharmacological profile of polyclonal antibody therapies, such as Intravenous Immunoglobulin (IVIG). These therapies contain a diverse repertoire of IgG antibodies derived from thousands of healthy donors, allowing them to target a vast array of exogenous antigens including viral, bacterial, and fungal proteins. By binding these antigens, the therapy provides passive immunity and neutralizes circulating pathogens and toxins. Simultaneously, these therapies interact with various endogenous immune receptors to exert immunomodulatory effects. Key interactions include the saturation of the neonatal Fc receptor (FcRn), which accelerates the degradation of pathogenic autoantibodies, and the binding to inhibitory Fc gamma receptors (FcγRIIB), which helps suppress overactive immune responses in autoimmune conditions. Because this designation encompasses hundreds of distinct molecular targets across different biological systems, it is considered a multi-target therapeutic category rather than a specific canonical receptor or enzyme.
The mechanism involves the neutralization of various exogenous pathogens (viruses, bacteria, toxins) through direct binding, alongside the modulation of endogenous immune receptors such as Fc receptors (FcγR) and neonatal Fc receptors (FcRn) to regulate inflammation and autoantibody clearance.
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