Preferential binding of unusually long peptides to MHC class I and its influence on the selection of target peptides for T cell recognition

Jacqueline M. Burrows, Melissa J. Bell, Rebekah Brennan, John J. Miles, Rajiv Khanna, Scott R. Burrows

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24 Citations (Scopus)


A classic feature of antigen presentation for CD8+ T cell recognition is that MHC class I molecules generally present peptides of 8-10 amino acids in length. However, recent studies have demonstrated that peptides of >10 residues play a significant role in immune surveillance by T cells restricted by some HLA class I alleles. In the present study, we describe several examples of unusually long viral peptides of 11 or 12 residues, recognized by CTLs in the context of HLA-B35. Interestingly, all these immunogenic peptides completely encompass shorter canonical length sequences that conform to the HLA-B35 binding motif, but which fail to stimulate detectable T cell responses. The mechanism for this phenomenon appears to involve the preferential binding to HLA-B35 of the atypically long CD8+ T cell target peptides over the overlapping canonical length sequences. These data suggest that the peptide length specificity of some HLA class I alleles is broad, allowing peptides of >10 residues to sometimes dominate over canonical length class I ligands as targets for T cell recognition.

Original languageEnglish
Pages (from-to)1818-1824
Number of pages7
JournalMolecular Immunology
Issue number6
Publication statusPublished - 1 Mar 2008
Externally publishedYes


  • Antigen presentation/processing
  • CTL
  • Human
  • MHC class I
  • Viral

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