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FcgammaRI (CD64) contributes substantially to severity of arthritis, hypersensitivity responses, and protection from bacterial infection.

Ioan-Facsinay A., de Kimpe S.J., Hellwig S.M.M., van Lent P.L., Hofhuis F.M.A., van Ojik H.H., Sedlik C., da Silveira S.A., Gerber J., de Jong Y.F., Roozendaal R., Aarden L.A., van den Berg W.B., Saito T., Mosser D., Amigorena S., Izui S., van Ommen G.-J.B., van Vugt M., van de Winkel J.G.J., Verbeek J.S.

The high-affinity receptor for IgG, FcgammaRI, shares its capacity to bind IgG2a immune complexes (IgG2a-IC) with the low-affinity receptor FcgammaRIII and complement factors, hampering the definition of its biological role. Moreover, in vivo, FcgammaRI is occupied by monomeric IgG2a, reducing its accessibility to newly formed IgG2a-IC. By using a variety of FcgammaR(-/-) mice, we demonstrate that in the absence of FcgammaRI, the IgG2a-IC-induced cellular processes of phagocytosis, cytokine release, cellular cytotoxicity, and antigen presentation are impaired. FcgammaRI(-/-) mice showed impaired hypersensitivity responses, strongly reduced cartilage destruction in an arthritis model, and impaired protection from a bacterial infection. We conclude that FcgammaRI contributes substantially to a variety of IgG2a-IC-dependent immune functions and immunopathological responses.

Immunity 16:391-402(2002) [PubMed] [Europe PMC]

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