IgA in the horse: cloning of equine polymeric Ig receptor and J chain and characterization of recombinant forms of equine IgA

Melanie J. Lewis, B. Wagner, R. M. Irvine, Jennifer M. Woof (Lead / Corresponding author)

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    11 Citations (Scopus)
    112 Downloads (Pure)

    Abstract

    As in other mammals, immunoglobulin A (IgA) in the horse has a key role in immune defense. To better dissect equine IgA function, we isolated complementary DNA (cDNA) clones for equine J chain and polymeric Ig receptor (pIgR). When coexpressed with equine IgA, equine J chain promoted efficient IgA polymerization. A truncated version of equine pIgR, equivalent to secretory component, bound with nanomolar affinity to recombinant equine and human dimeric IgA but not with monomeric IgA from either species. Searches of the equine genome localized equine J chain and pIgR to chromosomes 3 and 5, respectively, with J chain and pIgR coding sequence distributed across 4 and 11 exons, respectively. Comparisons of transcriptional regulatory sequences suggest that horse and human pIgR expression is controlled through common regulatory mechanisms that are less conserved in rodents. These studies pave the way for full dissection of equine IgA function and open up possibilities for immune-based treatment of equine diseases.</p>
    Original languageEnglish
    Pages (from-to)610-621
    Number of pages12
    JournalMucosal Immunology
    Volume3
    Issue number6
    DOIs
    Publication statusPublished - Nov 2010

    Keywords

    • TRANSMEMBRANE SECRETORY COMPONENT
    • ANTIBODY ISOTYPE RESPONSES
    • IMMUNOGLOBULIN RECEPTOR
    • STRUCTURAL REQUIREMENTS
    • MUCOSAL IMMUNOLOGY
    • MOLECULAR-CLONING
    • X-RAY
    • GENE
    • EXPRESSION
    • CELLS

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