Diversity of T cell receptors specific for the VSV antigenic peptide (N52-59) Bound by the H-2Kb class I molecule

As an approach to determine the structural basis of interactions between T cell receptors (TCRs) and MHC class I/peptide complexes, the fine specificities of a panel of vesicular stomatitis virus (VSV)-specific CTL clones recognizing the antigenic peptide (nucleoprotein 52–59) and the class I (Kb) molecule were correlated with the TCR primary structure. Each TCR showed a distinct interaction pattern with N52–59 and the Kb molecule. The large majority of the TCRs expressed by the panel of CTL clones used Vβ13 gene segments that had randomly recombined with Dβ and Jβ gene segments. The α chains were from randomly assorted Vα and Jα gene segments. Thus, the panel was found to be a highly heterogeneous set of TCRs, each member of which appeared to have an unique surface interface area, the recognition site, that interacted with a complementary surface formed by the single peptide bound in the class I antigenic groove.