Isolated hapten-binding receptors of sensitized lymphocytes I. Receptors from nylon wool-enriched mouse T lymphocyte lack serological markers of immunoglobulin constant domain but express heavy chain variable portions
✍ Scribed by U. Krawinkel; M. Cramer; Thereza Imanishi-Kari; R.S. Jack; K. Rajewsky; O. Makelä
- Publisher
- John Wiley and Sons
- Year
- 1977
- Tongue
- English
- Weight
- 1003 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0014-2980
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✦ Synopsis
Abstract
Hapten‐binding receptor material was isolated from hapten‐sensitized mouse lymphocytes, as described previously (Eur. J. Immunol 1976.6: 529; Cold Spring Harbor Symp. Quant. Biol. 1977. 41: 285). The material was separated into a fraction expressing immunoglobulin determinants (anti‐Ig^+^ fraction) and a fraction lacking determinants of the known Ig constant domains (anti‐Ig^−^fraction). We present further evidence in support of the notion that the anti‐Ig^+^ fraction is B cell‐derived, whereas the anti‐Ig^−^ fraction originates from T lymphocytes. Receptors derived from C57BL/6 mice of the anti‐Ig^_^ phenotype with specificity for the hapten (4‐hydroxy‐3‐nitrophenyl)acetyl (NP) are found to express markers which are characteristic for the variable portion of primary anti‐NP antibodies. One of these markers relates to the fine specificity of hapten binding [6, 24], the other is defined by anti‐idiotypic antibodies. Genetic studies show that the expression of these markers both in antibodies and the anti‐Ig^−^ receptor fraction is controlled by genes in the heavy chain linkage group.
The results demonstrate that in this system, humoral antibodies and receptor molecules of both the anti‐Ig^+^ and anti‐Ig^−^ phenotype bind the hapten with strikingly similar affinity and fine specificity. More specifically, they suggest that the molecules in the anti‐Ig^−^ receptor fraction carry the variable region (and in fact the en tire variable region) of the Ig heavy chain.