Modification of peptide interaction with MHC creates TCR partial agonists.

@article{Ryan2004ModificationOP,
  title={Modification of peptide interaction with MHC creates TCR partial agonists.},
  author={Kelli R. Ryan and Lisa K Mcneil and Chinh T. Dao and Peter Egede Jensen and Brian D Evavold},
  journal={Cellular immunology},
  year={2004},
  volume={227 1},
  pages={70-8}
}
We report the creation of TCR partial agonists by the novel approach of manipulating the interaction between immunogenic peptide and MHC. Amino acids at MHC anchor positions of the I-E(k)-restricted hemoglobin (64-76) and moth cytochrome c (88-103) peptides were exchanged with MHC anchor residues from the low affinity class II invariant chain peptide (CLIP), resulting in antigenic peptides with altered affinity for MHC class II. Several low affinity peptides were identified as TCR partial… CONTINUE READING

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