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A third immunoglobulin class in amphibians.

E Hsu, M F Flajnik, L Du Pasquier

    Journal of Immunology (Baltimore, Md. : 1950)
    |September 1, 1985
    PubMed
    Summary
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    Researchers discovered a new immunoglobulin class, IgX, in Xenopus laevis frogs. This novel IgX protein differs from other immunoglobulins and is consistently secreted by frog immune cells.

    Area of Science:

    • Immunology
    • Zoology
    • Biochemistry

    Background:

    • Immunoglobulins are crucial proteins in adaptive immunity.
    • Xenopus laevis, a South African frog, serves as a model organism in biological research.
    • Existing immunoglobulin classes in amphibians include IgM and IgY.

    Purpose of the Study:

    • To identify and characterize a novel immunoglobulin class in Xenopus laevis.
    • To differentiate this new immunoglobulin from known amphibian immunoglobulin types.
    • To investigate the secretion patterns of this novel immunoglobulin.

    Main Methods:

    • Immunoprecipitation using specific monoclonal antibodies.
    • Analysis of protein subunit composition (heavy and light chains).
    • Comparison of peptide maps with known immunoglobulin heavy chains (mu).

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  • Cell culture of spleen and intestinal mucosae to assess secretion.

    • Main Results:

    • A new immunoglobulin class, designated IgX, was identified in Xenopus laevis.
    • IgX is distinct from IgM and IgY, as shown by antibody-binding and peptide mapping.
    • IgX exists as a polymer composed of 80 kDa heavy chains and 25-29 kDa light chains.
    • IgX heavy chains contain asparagine-linked carbohydrates, similar to mu chains, but with distinct peptide maps.
    • IgX is consistently secreted by spleen and intestinal mucosae cells, despite variable serum concentrations.

    Conclusions:

    • Xenopus laevis possesses a unique immunoglobulin class, IgX, expanding the known diversity of vertebrate antibodies.
    • IgX represents a distinct evolutionary lineage of immunoglobulins.
    • The cellular sources of IgX secretion are identified, providing insights into its immune function in amphibians.