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

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: 1911-1917. doi:10.1016/j.molimm.2008.12.003


Author Bell, Melissa J.
Burrows, Jacqueline M.
Brennan, Rebekah
Miles, John J.
Tellam, Judy
McCluskey, James
Rossjohn, Jamie
Khanna, Rajiv
Burrows, Scott R.
Title The peptide length specificity of some HLA class I alleles is very broad and includes peptides of up to 25 amino acids in length
Journal name Molecular Immunology   Check publisher's open access policy
ISSN 0161-5890
1872-9142
Publication date 2009-05-01
Sub-type Article (original research)
DOI 10.1016/j.molimm.2008.12.003
Open Access Status Not yet assessed
Volume 46
Issue 8-9
Start page 1911
End page 1917
Total pages 7
Place of publication Kidlington, Oxford, United Kingdom
Publisher Pergamon
Language eng
Subject 2403 Immunology
1312 Molecular Biology
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.
Formatted 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.
Keyword Human
MHC class I
Antigen presentation/processing
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ
Additional Notes Published under Short Communications

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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Created: Thu, 03 Sep 2009, 18:06:11 EST by Mr Andrew Martlew on behalf of School of Medicine