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Receptors recognizing the Fc region of immunoglobulin (Ig) G (FcγR) have attracted much interest concerning the aetiology and pathogenesis of autoimmune diseases [1, 2]. In addition to the placental FcγR (FcγRn), which transfers maternal monomeric IgG to the fetus, three distinct classes of FcγR have been characterized: FcγRI (CD64), FcγRII (CD32) and FcγRIII (CD16). Human FcγRII is divided into subclasses A, B and C, and for FcγRIII subclasses A and B have been described [3]. Except for FcγRIIB, all FcγRs are activating, e.g. they initiate antibody-dependent cellular cytotoxicity, proinflammatory cytokine secretion and phagocytosis, ultimately resulting in immune complex clearance and antigen presentation by antigen-presenting cells [4, 5]. In contrast to FcγRII and FcγRIII, FcγRI is a high-affinity receptor with the ability to bind IgG monomers

Dan's use-case:

• What’s being collected is “Antigen-specific FcR Binding” with results in units of median fluorescence intensity
• FcR is a cell surface receptor that binds to the Fc (constant domain) of an IgG antibody
• The antigens are HA’s from a variety of influenza strains
• Antigens are bound to magnetic micro beads
• Subject serum is added and antigens are bound by antibodies specific for them
• Microbeads with an antibody-antigen complex are separated from microbeads with unbound antigens
• Various FcR’s are added and incubated with the antibody-antigen microbead complexes
• The mdFI of the resulting antigen-antibody-FcR microbead complex is assessed

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