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Mol Immunol. 2009 May;46(8-9):1911-7. doi: 10.1016/j.molimm.2008.12.003. Epub 2009 Jan 20.

The peptide length specificity of some HLA class I alleles is very broad and includes peptides of up to 25 amino acids in length.

Author information

1
Queensland Institute of Medical Research and Australian Centre for Vaccine Development, Herston, Brisbane, Australia.

Abstract

The major ligands presented by MHC class I molecules after natural antigen processing are peptides of eight to ten residues in length, and it is widely accepted that the binding preferences of MHC class I molecules play a dominant role in dictating this classic feature of antigen presentation. In this report, we have reassessed the peptide size specificity of class I human leukocyte antigens (HLAs). By lengthening previously defined T cell epitopes by central amino acid insertion, we demonstrate that the peptide length specificity of some common HLA class I alleles (HLA-B*3501, B*0702 and A*2402) is very broad, and includes peptides of up to 25 residues. These data suggest that the length limitation of naturally processed MHC class I-associated peptides is primarily controlled by peptide availability after antigen processing rather than the binding specificity of MHC class I molecules. Furthermore, the findings provide an explanation for recent reports highlighting that epitopes of >10 amino acids play a minor but significant role in virus-specific immune surveillance by CD8(+) T cells.

PMID:
19157553
DOI:
10.1016/j.molimm.2008.12.003
[Indexed for MEDLINE]

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