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Generation and characterization of anti-idiotypic antibodies recognizing the interferon-alpha receptor: implications
1Department of Molecular Genetics and Microbiology, UMDNJ-Robert Wood Johnson Medical School, Piscataway 08854.
Monoclonal antibodies LI-1 and LI-8 against interferon-alpha A (IFN-alpha A) block IFN-alpha A activity and binding to its receptor, but they recognize distinct epitopes. Surprisingly, anti-idiotypic antibodies to both LI-1 and LI-8 have properties consistent with recognition of the receptor: anti-LI-1 and anti-LI-8 antibodies inhibit the binding of IFN-alpha A to its receptor. However, anti-LI-1 is an antagonist of IFN-alpha A, while anti-LI-8 is an agonist. Thus, at least some part of the epitopes on IFN-alpha A recognized by LI-1 and LI-8 are directly involved in receptor binding. Because these epitopes are spatially distinct, the implication is that the receptor binding site on IFN-alpha A must be extensive, or there are minimally two regions of IFN-alpha A involved in receptor interactions.
Monoclonal antibodies LI-1 and LI-8 against interferon-alpha A (IFN-alpha A) block IFN-alpha A activity and binding to its receptor, but they recognize distinct epitopes. Surprisingly, anti-idiotypic antibodies to both LI-1 and LI-8 have properties consistent with recognition of the receptor: anti-LI-1 and anti-LI-8 antibodies inhibit the binding of IFN-alpha A to its receptor. However, anti-LI-1 is an antagonist of IFN-alpha A, while anti-LI-8 is an agonist. Thus, at least some part of the epitopes on IFN-alpha A recognized by LI-1 and LI-8 are directly involved in receptor binding. Because these epitopes are spatially distinct, the implication is that the receptor binding site on IFN-alpha A must be extensive, or there are minimally two regions of IFN-alpha A involved in receptor interactions.