The T cell receptor alpha beta V-J shuffling shows lack of autonomy between the combining site and the constant domain of the receptor chains

Eur J Immunol. 1993 Feb;23(2):586-9. doi: 10.1002/eji.1830230246.

Abstract

In order to assess the structural independence of the T cell receptor (TCR) combining site from the rest of the molecule we have generated two recombinant chains consisting of a TCR V-J alpha region linked to the C beta and a TCR V-J beta linked to the C alpha. If the V and C domains of the TCR form independent domains, as has been shown for the Ig molecules, we would expect to obtain a functional chimeric TCR. Interestingly, it was found that the shuffled molecules are produced intracellularly in T cell hybridomas, but are not expressed on the cell surface. To explain this failure of the shuffled molecules we propose that the TCR has a more compact structure, compared to the Ig, and that it is indispensable to keep a longitudinal inter-domain contact between the V-J and C portion to have a functional molecule.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Binding Sites, Antibody / immunology*
  • Cells, Cultured
  • Gene Rearrangement, T-Lymphocyte / immunology*
  • Genes, Immunoglobulin / genetics*
  • Genes, Immunoglobulin / immunology*
  • Hybridomas / immunology
  • Mice
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Plasmids
  • Polymerase Chain Reaction
  • Receptors, Antigen, T-Cell, alpha-beta / genetics*
  • Receptors, Antigen, T-Cell, alpha-beta / immunology*
  • T-Lymphocytes / immunology*
  • T-Lymphocytes, Helper-Inducer / immunology
  • Transfection

Substances

  • Oligonucleotide Probes
  • Receptors, Antigen, T-Cell, alpha-beta