Interaction of human, rat, and mouse immunoglobulin A (IgA) with staphylococcal superantigen-like 7 (SSL7) decoy protein and leukocyte IgA receptor
dc.contributor.author | Wines, B. | |
dc.contributor.author | Ramsland, Paul | |
dc.contributor.author | Trist, H. | |
dc.contributor.author | Gardam, S. | |
dc.contributor.author | Brink, R. | |
dc.contributor.author | Fraser, J. | |
dc.contributor.author | Hogarth, P. | |
dc.date.accessioned | 2017-01-30T15:21:50Z | |
dc.date.available | 2017-01-30T15:21:50Z | |
dc.date.created | 2015-10-29T04:09:57Z | |
dc.date.issued | 2011 | |
dc.identifier.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. | |
dc.identifier.uri | http://hdl.handle.net/20.500.11937/45571 | |
dc.identifier.doi | 10.1074/jbc.M111.272252 | |
dc.description.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. | |
dc.title | Interaction of human, rat, and mouse immunoglobulin A (IgA) with staphylococcal superantigen-like 7 (SSL7) decoy protein and leukocyte IgA receptor | |
dc.type | Journal Article | |
dcterms.source.volume | 286 | |
dcterms.source.number | 38 | |
dcterms.source.startPage | 33118 | |
dcterms.source.endPage | 33124 | |
dcterms.source.issn | 0021-9258 | |
dcterms.source.title | Journal of Biological Chemistry | |
curtin.department | School of Biomedical Sciences | |
curtin.accessStatus | Open access via publisher |
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