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Science 20 January 1989:
Vol. 243. no. 4889, pp. 378 - 381
DOI: 10.1126/science.2911749
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Articles

Science, Vol 243, Issue 4889, 378-381
Copyright © 1989 by American Association for the Advancement of Science

articles

Isolation and expression of functional high-affinity Fc receptor complementary DNAs

JM Allen and B Seed

Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.

Human and murine mononuclear phagocytes express a high-affinity receptor for immunoglobulin G that plays a central role in macrophage antibody-dependent cellular cytotoxicity and clearance of immune complexes. The receptor (FcRI) may also be involved in CD4-independent infection of human macrophages by human immunodeficiency virus. This report describes the isolation of cDNA clones encoding the human FcRI by a ligand-mediated selection technique. Expression of the cDNAs in COS cells gave rise to immunoglobulin G binding of the expected affinity and subtype specificity. RNA blot analysis revealed expression of a 1.7-kilobase transcript in macrophages and in cells of the promonocytic cell line U937 induced with interferon-gamma. The extracellular region of FcRI consists of three immunoglobulin-like domains, two of which share homology with low-affinity receptor domains.


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