Structural and kinetic basis for low affinity cross-reactivity in T cell allorecognition.

@article{Guimezanes2003StructuralAK,
  title={Structural and kinetic basis for low affinity cross-reactivity in T cell allorecognition.},
  author={Annick Guimezanes and F{\'e}lix A. Montero-Julian and Anne-Marie Schmitt-Verhulst},
  journal={European journal of immunology},
  year={2003},
  volume={33 11},
  pages={3060-9}
}
The alloreactive BM3.3TCR interacts with high affinity with H-2Kb loaded with the endogenous peptide pBM1 (INFDFNTI), and shows low affinity cross-reactivity for H-2Kb loaded with a viral peptide VSV8 (RGYVYQGL), CTL activity requiring 10(3)-fold higher peptide concentration and being highly sensitive to inhibition by anti-CD8 monoclonal antibody. VSV8 peptides substituted with pBM1/TCR contact residues (N6 and T7) retained low affinity characteristics and among pBM1 peptides substituted with… CONTINUE READING