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Synthesis and characterization of anti-idiotypic anti-T₄ antibodies

Juge-Aubry CE, Liang H, Lang J, Barlow JW, Burger AG. Synthesis and characterization of anti-idiotypic anti-thyroxine antibodies. Eur J Endocrinol 1994;130:107–12. ISSN 0804–4643

We injected rabbits with purified monoclonal murine immunoglobulin (IgG1) or polyclonal anti-thyroxine antibodies (anti-T₄) and polyclonal anti-triiodothyroacetic acid (anti-Triac) antibodies to stimulate the production of anti-idiotypic antibodies. Purified immunoglobulins from all five rabbits immunized with monoclonal primary antibodies were able to inhibit the interaction between [¹²⁵I]T₄ and the primary antibody. The preimmune sera were inactive. This effect was not due to endogenous T₄ contamination or contamination with the injected primary antibody. Half-maximal inhibition of binding of primary antibody with anti-idiotype was between 1.6 and 30 µg of total immunoglobulins. Addition of normal mouse IgG1 did not alter the inhibitory effect of the anti-idiotypic antibody. suggesting that this effect is specific. These anti-idiotypic antibodies reacted differently with different polyclonal antibodies, reflecting the heterogeneous nature of polyclonal antibody populations. Polyclonal antibodies were less effective in stimulating anti-idiotypic antibody production. One polyclonal anti-T₄ and one anti-Triac antibody produced weak anti-idiotypic antibody that had to be used at a concentration of > 600 µg of total immunoglobulins to be inhibitory. Both inhibited the binding of T₄ to the monoclonal anti-T₄ antibody. However, they were ineffective in inhibiting the function of their own antigen, the polyclonal anti-T₄ or anti-Triac antibody. We tested the most potent anti-idiotypic antibodies for their ability to compete with T₄ for other T₄-binding proteins. Specific inhibition of T₄ binding to thyroid-binding globulin was observed with half-maximal effect at approximately 450 µg of total IgG. The antibody was negative when tested against Transthyretin, rat liver deiodinase type I, triiodothyronine cell uptake and liver cytoplasmic triiodothyronine binding. In conclusion, the technique described herein allows production of anti-idiotypic anti-T₄, which can be useful in the characterization of the range of iodothyronine-binding sites involved in thyroid hormone action.

AG Burger, Unité de la Thyroïde, Hôpital Cantonal Universitaire, 1211 Genève 4, Switzerland