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© The Rockefeller University Press, 0022-1007/1999/6/1715/ $5.00
The Journal of Experimental Medicine, Volume 189, Number 11, June 7, 1999 1715-1722

Articles

Immunoglobulin-binding Sites of Human Fc{alpha}RI (CD89) and Bovine Fc{gamma}2R Are Located in their Membrane-distal Extracellular Domains

H. Craig Morton*, Ger van Zandbergen{ddagger}, Cees van Kooten{ddagger}, Chris J. Howard§, Jan G. J. van de Winkel||, and Per Brandtzaeg*

From the * Laboratory of Immunohistochemistry and Immunopathology (LIIPAT), The National Hospital, University of Oslo, Rikshospitalet, N-0027 Oslo, Norway; the {ddagger} Department of Nephrology, Leiden University Medical Center, 2300 RC Leiden, The Netherlands; the § Division of Immunology and Pathology, The Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; and the || Department of Immunology and Medarex Europe, University Hospital Utrecht, 3584 CX Utrecht, The Netherlands

To localize the immunoglobulin (Ig)-binding regions of the human Fc{alpha} receptor (Fc{alpha}RI, CD89) and the bovine Fc{gamma}2 receptor (bFc{gamma}2R), chimeric receptors were generated by exchanging comparable regions between these two proteins. Fc{alpha}RI and bFc{gamma}2R are highly homologous and are more closely related to each other than to other human and bovine FcRs. Nevertheless, they are functionally distinct in that Fc{alpha}RI binds human IgA (hIgA) but not bovine IgG2 (bIgG2), whereas bFc{gamma}2R binds bIgG2 but not hIgA. Fc{alpha}RI and bFc{gamma}2R possess extracellular regions consisting of two Ig-like domains, a membrane-distal extracellular domain (EC1), a membrane-proximal EC domain (EC2), a transmembrane region, and a short cytoplasmic tail. Chimeras constructed by exchanging complete domains between these two receptors were transfected to COS-1 cells and assayed for their ability to bind hIgA- or bIgG2-coated beads. The results showed that the Ig-binding site of both Fc{alpha}RI and bFc{gamma}2R is located within EC1. Supporting this observation, monoclonal antibodies that blocked IgA binding to Fc{alpha}RI were found to recognize epitopes located in this domain. In terms of FcR–Ig interactions characterized thus far, this location is unique and surprising because it has been shown previously that leukocyte Fc{gamma}Rs and Fc{varepsilon}RI bind Ig via sites principally located in their EC2 domains.

Key Words: Fc receptor • CD89 • bovine Fc{gamma}2 receptor • immunoglobulin A • myeloid

Address correspondence to H. Craig Morton, LIIPAT, Rikshospitalet, N-0027, Oslo, Norway. Phone: 47-22-86-86-31; Fax: 47-22-11-22-61; E-mail: craig.morton{at}labmed.uio.no

Note added in proof. A recent report by Wines et al. (J. Immunol. 1999. 162:2146–2153) likewise identified the EC1 domain of Fc{alpha}RI to be responsible for ligand binding.

Abbreviations used: b, bovine; EC, extracellular; GAM, goat anti–mouse; GFP, green fluorescent protein; KIR, natural killer cell inhibitory receptor; TM/C, transmembrane/cytoplasmic.


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