Abstract
Renewed interest in mucosal immunity occurred with the discovery by Tornasi and colleagues that both the quality and quantity of the immunoglobulins in the external secretions were different from those of serum. Secretory IgA contained an additional glycoprotein component, secretory component (SC), not generally present on serum IgA (1–2). More recently it was shown that in human and canine secretions, secretory component is also associated with IgM (3–4). The interaction of human SC with human immunoglobulins has been studied in considerable detail (5–11). Human SC binds with high affinity to polymeric IgM and IgA, but not to monomeric immunoglobulins (7,11). Binding of SC to pentameric IgM proceeds predominately through non-covalent bonds while binding to IgA dimer involves non-covalent association followed by formation of a disulfide bond linking SC to one of the monomeric subunits of the IgA dimer (7,10). Several reports in the literature indicated that SC can also bind to heterologous polymeric immunoglobulins (5,12).
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References
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Underdown, B.J., Socken, D.J. (1978). A Comparison of Secretory Component — Immunoglobulin Interactions Amongst Different Species. In: McGhee, J.R., Mestecky, J., Babb, J.L. (eds) Secretory Immunity and Infection. Advances in Experimental Medicine and Biology, vol 107. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3369-2_57
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DOI: https://doi.org/10.1007/978-1-4684-3369-2_57
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