ArticleThe Journal of experimental medicine1999
Immunoglobulin-binding sites of human FcalphaRI (CD89) and bovine Fcgamma2R are located in their membrane-distal extracellular domains.
Article in The Journal of experimental medicine, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 66 citations in OpenAlex.
- Article
- Antagonizing FcαR1 (CD89) as treatment in IgA-mediated chronic inflammation and autoimmunity.Frontiers in immunology · 2023Article
- FcαRI binding at the IgA1 CProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The antibody loci of the domestic goat (Capra hircus).Immunogenetics · 2018Article
- Uptake of HLA Alloantigens via CD89 and CD206 Does Not Enhance Antigen Presentation by Indirect Allorecognition.Journal of immunology research · 2016Article
- The generation and evaluation of recombinant human IgA specific for Plasmodium falciparum merozoite surface protein 1-19 (PfMSP1 19).BMC biotechnology · 2011Article
- Characterization and ligand specificity of sheep IgG2 receptor.Immunogenetics · 2009Article
- Monocyte CD64 or CD89 targeting by surfactant protein D/anti-Fc receptor mediates bacterial uptake.Immunology · 2006Article
- Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques.Immunology · 2005Article
- Identification and characterization of macaque CD89 (immunoglobulin A Fc receptor).Immunology · 2004Article
- Article
- Limited role of charge matching in the interaction of human immunoglobulin A with the immunoglobulin A Fc receptor (Fc alpha RI) CD89.Immunology · 2003Article
- Immunoglobulin A-mediated protection against Bordetella pertussis infection.Infection and immunity · 2001Article
- The B-cell system of human mucosae and exocrine glands.Immunological reviews · 1999Review
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To localize the immunoglobulin (Ig)-binding regions of the human Fcalpha receptor (FcalphaRI, CD89) and the bovine Fcgamma2 receptor (bFcgamma2R), chimeric receptors were generated by exchanging comparable regions between these two proteins. FcalphaRI and bFcgamma2R 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 FcalphaRI binds human IgA (hIgA) but not bovine IgG2 (bIgG2), whereas bFcgamma2R binds bIgG2 but not hIgA. FcalphaRI and bFcgamma2R 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 FcalphaRI and bFcgamma2R is located within EC1. Supporting this observation, monoclonal antibodies that blocked IgA binding to FcalphaRI 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 FcgammaRs and FcepsilonRI bind Ig via sites principally located in their EC2 domains.
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