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  • Title: High polymeric IgA content facilitates recognition of microbial polysaccharide-natural serum antibody immune complexes by immobilized human galectin-1.
    Author: Paul A, Antony M, Mathai J, Appukuttan PS.
    Journal: Immunol Lett; 2011 Apr 30; 136(1):55-60. PubMed ID: 21147166.
    Abstract:
    Dextran-binding immunoglobulin (DIg) and anti-β-glucan antibody (ABG) are naturally occurring human serum antibodies specific to α- and β-glucoside epitopes respectively of polysaccharide antigens and heavily enriched in IgA. ABG and DIg are shown here to have much more of their IgA in polymeric form than does serum IgA in general. Cell wall β-glucans and glycoproteins of the widely consumed yeast (Saccharomyces cerevisiae) offered several hundred fold better ligands for ABG than did small β-glucosides. Candida albicans cell wall antigen (CCA), a commonly encountered polysaccharide-rich fungal antigen was recognized by normal human serum anti-carbohydrate antibodies to precipitate maximally at a definite stoichiometry typical of immune complexes (IC). IC formed in serum in vitro on addition of CCA contained a significantly higher percentage of IgA than did either naturally occurring IC or serum. Polymeric IgA was far better ligand than monomeric IgA for both anti-IgA antibody and the most widely expressed human tissue lectin galectin-1 which recognizes O-linked oligosaccharides characteristic of IgA, in contrast to N-linked oligosaccharides present in all immunoglobulins. Moreover, desialylation by neuraminidase, an enzyme released into circulation during many microbial infections and diabetes, increased lectin-binding activity of polymeric IgA much more than that of monomeric IgA. Human galectin-1 immobilized in active form in vitro sugar-specifically captured IgA and IgA-containing IC formed by CCA in serum but not IgG. Results suggest that while high IgA content especially in polymeric form may render polysaccharide IC more susceptible to tissue uptake, desialylation of IgA in IC could enhance the process.
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