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    Interaction of human, rat, and mouse immunoglobulin A (IgA) with staphylococcal superantigen-like 7 (SSL7) decoy protein and leukocyte IgA receptor

    Access Status
    Open access via publisher
    Authors
    Wines, B.
    Ramsland, Paul
    Trist, H.
    Gardam, S.
    Brink, R.
    Fraser, J.
    Hogarth, P.
    Date
    2011
    Type
    Journal Article
    
    Metadata
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    Citation
    Wines, B. and Ramsland, P. and Trist, H. and Gardam, S. and Brink, R. and Fraser, J. and Hogarth, P. 2011. Interaction of human, rat, and mouse immunoglobulin A (IgA) with staphylococcal superantigen-like 7 (SSL7) decoy protein and leukocyte IgA receptor. Journal of Biological Chemistry. 286 (38): pp. 33118-33124.
    Source Title
    Journal of Biological Chemistry
    DOI
    10.1074/jbc.M111.272252
    ISSN
    0021-9258
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/45571
    Collection
    • Curtin Research Publications
    Abstract

    Host survival depends on an effective immune system and pathogen survival on the effectiveness of immune evasion mechanisms. Staphylococcus aureus utilizes a number of molecules to modulate host immunity, including the SSL family of which SSL7 binds IgA and inhibits Fca receptor I (FcaRI)-mediated function. Other Gram-positive bacterial pathogens produce IgA binding proteins, which, similar to SSL7, also bind the Fc at the CH2/CH3 interface (the junction between constant domains 2 and 3 of the heavy chain). The opposing activities of the host FcaRI-IgA receptor ligand pair and the pathogen decoy proteins select for host and pathogen variants, which exert stronger protection or evasion, respectively. Curiously, mouse but not rat IgA contains a putative N-linked glycosylation site in the center of this host receptor and pathogen-binding site. Here, we demonstrate that this site is glycosylated and that the effect of amino acid changes and glycosylation of the CH2/CH3 interface inhibits interaction with the pathogen IgA binding protein SSL7, while maintaining binding of pIgR, essential to the biosynthesis and transport of SIgA. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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