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This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Koene, H. R. Articles by de Haas, M. Search for Related Content PubMed PubMed Citation Articles by Koene, H. R. Articles by de Haas, M. Related Collections Immunobiology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  FcRIIIa-158V/F Polymorphism Influences the Binding of IgG by Natural Killer Cell FcRIIIa, Independently of the FcRIIIa-48L/R/H Phenotype Harry R. Koene, Marion Kleijer, Johan Algra, Dirk Roos, Albert E.G.Kr. von dem Borne, and Masja de Haas From the Central Laboratory of the Netherlands Red Cross Blood Transfusion Service and Laboratory for Experimental and Clinical Immunology, University of Amsterdam, Amsterdam; and Academic Medical Centre, Amsterdam, The Netherlands. We analyzed a genetic polymorphism of Fc receptor IIIa (CD16) that is present on position 158 (Phe or Val) in the membrane-proximal, IgG-binding domain. With a polymerase chain reaction-based allele-specific restriction analysis assay we genotyped 87 donors and found gene frequencies of 0.57 and 0.43 for FcRIIIA-158F and -158V, respectively. A clear linkage was observed between the FcRIIIA-158F and -48L genotypes on the one hand and the FcRIIIA-158V and -48H or -48R genotypes on the other hand (2 test; P < .001). To determine the functional consequences of this FcRIIIa-158V/F polymorphism, we performed IgG binding experiments with natural killer (NK) cells from genotyped donors. All donors were also typed for the recently described triallelic FcRIIIa-48L/R/H polymorphism. NK cells were treated with lactic acid to remove cell-associated IgG. FcRIIIaNK158F bound significantly less IgG1, IgG3, and IgG4 than did FcRIIIaNK-158V, irrespective of the FcRIIIa-48 phenotype. Moreover, freshly isolated NK cells from FcRIIIa-158VV individuals carried significantly more cytophilic IgG than did NK cells from FcRIIIa-158FF individuals. In addition, CD16 monoclonal antibody (MoAb) MEM154 bound more strongly to FcRIIIa-158V, compared with -158F, again independently of the FcRIIIa-48 phenotype. The binding of MoAb B73.1 was not influenced by the FcRIIIa-158V/F polymorphism, but proved to depend solely on the amino acid present at position 48 of FcRIIIa. In conclusion, the previously reported differences in IgG binding among the three FcRIIIa-48L/R/H isoforms are a consequence of the linked, biallelic FcRIIIa-158V/F polymorphism at amino-acid position 158. Blood, Vol. 90 No. 3 (August 1), 1997: pp. 1109-1114 © 1997 by The American Society of Hematology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: G. Cartron, L. Zhao-Yang, M. Baudard, T. Kanouni, V. Rouille, P. Quittet, B. Klein, and J.-F. Rossi Granulocyte-Macrophage Colony-Stimulating Factor Potentiates Rituximab in Patients With Relapsed Follicular Lymphoma: Results of a Phase II Study J. Clin. Oncol., June 1, 2008; 26(16): 2725 - 2731. [Abstract] [Full Text] [PDF] A. Musolino, N. Naldi, B. Bortesi, D. Pezzuolo, M. Capelletti, G. Missale, D. Laccabue, A. Zerbini, R. Camisa, G. Bisagni, et al. 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