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Antigenic changes produced by complex formation between thrombin and antithrombin-III.

F C McDuffie, J M Peterson, G Clark

    Journal of Immunology (Baltimore, Md. : 1950)
    |July 1, 1981
    PubMed
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    Antibodies generated against human thrombin and antithrombin-III recognize neoantigens formed upon complexation. These neoantigens arise from interactions between immunogens and host proteins, indicating cross-reactivity.

    Area of Science:

    • Biochemistry
    • Immunology
    • Protein Chemistry

    Background:

    • Thrombin and antithrombin-III are key proteins in the coagulation cascade.
    • Understanding antibody interactions with these proteins is crucial for diagnostics and therapeutics.

    Purpose of the Study:

    • To investigate the immune response to human thrombin and antithrombin-III.
    • To characterize the neoantigens formed during complexation of these proteins.

    Main Methods:

    • Immunization of goats and mules with human thrombin and antithrombin-III.
    • Antiserum characterization using precipitation assays and radioimmunoassay.
    • Analysis of protein-protein interactions in complex formation.

    Main Results:

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    • Antiserum to human thrombin showed weak reactivity to prothrombin but higher affinity for thrombin-antithrombin-III complexes.
    • Antiserum to antithrombin-III detected neoantigens in complexes with thrombin and clotting factor Xa.
    • Neoantigen formation was observed with host thrombin and human antithrombin-III, suggesting host-protein interactions.

    Conclusions:

    • Neoantigens are formed due to interactions between immunogens (thrombin or antithrombin) and host proteins (antithrombin-III or thrombin).
    • Antibodies generated are not entirely specific, cross-reacting with free proteins to some extent.