Bell, Melissa J., Burrows, Jacqueline M., Brennan, Rebekah, Miles, John J., Tellam, Judy, McCluskey, James, Rossjohn, Jamie, Khanna, Rajiv, and Burrows, Scott R. (2009) The peptide length specificity of some HLA class I alleles is very broad and includes peptides of up to 25 amino acids in length. Molecular Immunology, 46 (8-9). pp. 1911-1917.

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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.

Item ID:	45386
Item Type:	Article (Research - C1)
ISSN:	1872-9142
Keywords:	human; MHC class I; antigen presentation/processing
Funders:	National Health and Medical Research Council of Australia (NHMRC)
Date Deposited:	06 Sep 2016 05:13
FoR Codes:	11 MEDICAL AND HEALTH SCIENCES > 1107 Immunology > 110702 Applied Immunology (incl Antibody Engineering, Xenotransplantation and T-cell Therapies) @ 100%
SEO Codes:	92 HEALTH > 9201 Clinical Health (Organs, Diseases and Abnormal Conditions) > 920108 Immune System and Allergy @ 100%
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