Structural recognition and functional activation of FcγR by innate pentraxins
Jinghua Lu,
Lorraine L. Marnell,
Kristopher D. Marjon,
Carolyn Mold,
Terry W. Du Clos and
Peter D. Sun ()
Additional contact information
Jinghua Lu: Structural Immunology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, Maryland 20852, USA
Lorraine L. Marnell: University of New Mexico, Albuquerque, New Mexico 87131, USA
Kristopher D. Marjon: University of New Mexico, Albuquerque, New Mexico 87131, USA
Carolyn Mold: University of New Mexico, Albuquerque, New Mexico 87131, USA
Terry W. Du Clos: University of New Mexico, Albuquerque, New Mexico 87131, USA
Peter D. Sun: Structural Immunology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, Maryland 20852, USA
Nature, 2008, vol. 456, issue 7224, 989-992
Abstract:
Pentraxins involved in FcγR activation The classical pentraxins, serum amyloid P component (SAP) and C-reactive protein (CRP), are major acute phase reactants in mouse and man. As shown in this paper, pentraxins recognize various FcγRs, and SAP opsonization activates FcγR-mediated phagocytosis and cytokine secretion. The receptor binding sites for SAP and IgG overlap resulting in competition of IgG binding to FcγR as well as inhibition of immune complex-mediated phagocytosis by soluble pentraxins.
Date: 2008
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DOI: 10.1038/nature07468
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