Have we cut ourselves too short in mapping CTL epitopes?

MHC class I molecules generally present peptides of eight to ten amino acids; however, peptides of 11–14 residues can also elicit dominant cytotoxic T lymphocyte responses, sometimes at the expense of overlapping shorter peptides. Although long-bulged epitopes are considered to represent a barrier f...

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Bibliographic Details
Published in:Trends in Immunology 2006, Vol.27 (1), p.11-16
Main Authors: Burrows, Scott R., Rossjohn, Jamie, McCluskey, James
Format: Article
Language:English
Subjects:
Algorithms
Animals
Cytotoxicity
Epitopes, T-Lymphocyte - chemistry
Epitopes, T-Lymphocyte - immunology
Histocompatibility Antigens - immunology
Humans
Ligands
Lymphocytes
Peptides
Receptors, Antigen, T-Cell - chemistry
Receptors, Antigen, T-Cell - immunology
T cell receptors
T-Lymphocytes, Cytotoxic - chemistry
T-Lymphocytes, Cytotoxic - immunology
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Summary:MHC class I molecules generally present peptides of eight to ten amino acids; however, peptides of 11–14 residues can also elicit dominant cytotoxic T lymphocyte responses, sometimes at the expense of overlapping shorter peptides. Although long-bulged epitopes are considered to represent a barrier for T cell receptor recognition, recent structural data reveal how these super-bulged peptides are engaged while simultaneously maintaining MHC restriction. We propose that algorithms widely used to predict class I-binding peptides should now be broadened to include peptides of over ten residues in length.
ISSN:1471-4906
1471-4981
1365-2567
DOI:10.1016/j.it.2005.11.001