Abstract
It has been well established that antigen-specific suppression of antibody responses can be mediated by soluble factors derived from suppressor T cells1. However the chemical and functional properties of antigen-specific suppressor factors (TsF) are still controversial. We have recently described an antigen-specific suppressor T-cell factor composed of two distinct molecules. One is encoded by the gene located in the I–J subregion of the mouse H–2 complex on the 17th chromosome2,3, and the other which possesses the antigen-binding moiety2,3 and the constant region determinant (Ct), is the product of the Ct gene linked to the immunoglobulin heavy chain (Igh) gene cluster on the 12th chromosome4,5. The association of these two molecules is essential for the expression of the TsF activity2,3. However, Fresno et al.6 have shown that the TsF specific for sheep red blood cells (SRBC) is composed of a single polypeptide chain carrying the antigen-binding moiety. Kapp et al.7 have described another TsF with the antigen (GAT)-binding moiety and the I–J determinants on the same molecule. We describe here the identification of messenger RNAs (mRNAs) coding for the Ct-bearing molecules with antigen-binding moiety and the I–J encoded molecules in mRNA fractions derived from the T suppressor cell hybridoma by translation in Xenopus laevis oocytes. Furthermore, the mixture of the translation products of these two separate mRNA fractions was shown to reconstitute the antigen-specific TsF activity.
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Taniguchi, M., Tokuhisa, T., Kanno, M. et al. Reconstitution of antigen-specific suppressor activity with translation products of mRNA. Nature 298, 172–174 (1982). https://doi.org/10.1038/298172a0
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DOI: https://doi.org/10.1038/298172a0
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