High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance.

@article{Tynan2005HighRS,
  title={High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance.},
  author={Fleur E. Tynan and Natalie A. Borg and John J. Miles and Travis Beddoe and Diah El-Hassen and Sharon L. Silins and Wendy J M van Zuylen and Anthony W. Purcell and Lars Kjer-Nielsen and James McCluskey and Scott R. Burrows and Jamie Rossjohn},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 25},
  pages={23900-9}
}
Although HLA class I alleles can bind epitopes up to 14 amino acids in length, little is known about the immunogenicity or the responding T-cell repertoire against such determinants. Here, we describe an HLA-B*3508-restricted cytotoxic T lymphocyte response to a 13-mer viral epitope (LPEPLPQGQLTAY). The rigid, centrally bulged epitope generated a biased T-cell response. Only the N-terminal face of the peptide bulge was critical for recognition by the dominant clonotype SB27. The SB27 public T… CONTINUE READING

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