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Blood, 16 April 2009, Vol. 113, No. 16, pp. 3716-3725. Prepublished online as a Blood First Edition Paper on November 18, 2008; DOI 10.1182/blood-2008-09-179754. This Article Full Text (PDF) Supplemental Table and Figures All Versions of this Article: blood-2008-09-179754v1 113/16/3716    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Bruhns, P. Articles by Daeron, M. Search for Related Content PubMed PubMed Citation Articles by Bruhns, P. Articles by Daeron, M. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted September 18, 2008 Accepted November 4, 2008 Specificity and affinity of human Fc receptors and their polymorphic variants for human IgG subclasses Pierre Bruhns*, Bruno Iannascoli, Patrick England, David A Mancardi, Nadine Fernandez, Sylvie Jorieux, and Marc Daeron Departement d'Immunologie, Unite d'Allergologie Moleculaire et Cellulaire, Institut Pasteur, Paris, France INSERM, U760, Paris, France CNRS, URA 2185, Paris, France Laboratoire Francais du fractionnement et des Biotechnologies, Les Ulis, France Laboratoire Francais du fractionnement et des Biotechnologies, Lille, France * Corresponding author; email: bruhns{at}pasteur.fr. Distinct genes encode six human receptors for IgG (hFcRs), three of which have two or three polymorphic variants. The specificity and affinity of individual hFcRs for the four human IgG subclasses is unknown. This information is critical for antibody-based immunotherapy which has been increasingly used in the clinics. We investigated the binding of polyclonal and monoclonal IgG1, IgG2, IgG3 and IgG4 to FcRI, FcRIIA, IIB and IIC, FcRIIIA and IIIB and all known polymorphic variants. Wt and low-fucosylated IgG1 anti-CD20 and anti-RhD mAbs were also examined. We found: 1) that IgG1 and IgG3 bind to all hFcRs; 2) that IgG2 bind not only to FcRIIAH131, but also, with a lower affinity, to FcRIIAR131 and FcRIIIAV158; 3) that IgG4 bind to FcRI, FcRIIA, IIB and IIC and FcRIIIAV158; 4) that the inhibitory receptor FcRIIB has a lower affinity for IgG1, IgG2 and IgG3 than all other hFcRs. We also identified parameters which determine the specificity and affinity of hFcRs for IgG subclasses. These results document how hFcR specificity and affinity may account for the biological activities of antibodies. They therefore highlight the role of specific hFcRs in the therapeutic and pathogenic effects of antibodies in disease. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. Lazarou, J. A. G. Patino, R. M. Jennings, R. S. McIntosh, J. Shi, S. Howell, E. Cullen, T. Jones, J. R. Adame-Gallegos, J. A. Chappel, et al. Inhibition of Erythrocyte Invasion and Plasmodium falciparum Merozoite Surface Protein 1 Processing by Human Immunoglobulin G1 (IgG1) and IgG3 Antibodies Infect. Immun., December 1, 2009; 77(12): 5659 - 5667. [Abstract] [Full Text] [PDF] D. Hudrisier, B. Clemenceau, S. Balor, S. Daubeuf, E. Magdeleine, M. Daeron, P. Bruhns, and H. Vie Ligand Binding but Undetected Functional Response of FcR after Their Capture by T Cells via Trogocytosis J. Immunol., November 15, 2009; 183(10): 6102 - 6113. [Abstract] [Full Text] [PDF] L. G. Perez, M. R. Costa, C. A. Todd, B. F. Haynes, and D. C. Montefiori Utilization of Immunoglobulin G Fc Receptors by Human Immunodeficiency Virus Type 1: a Specific Role for Antibodies against the Membrane-Proximal External Region of gp41 J. Virol., August 1, 2009; 83(15): 7397 - 7410. [Abstract] [Full Text] [PDF]

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