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Updated: Aug 14, 2026
A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
Published on: March 25, 2014
Have we cut ourselves too short in mapping CTL epitopes?
Scott R Burrows1, Jamie Rossjohn, James McCluskey
1Queensland Institute of Medical Research, 300 Herston Road, Brisbane, Qld 4029, Australia. Scott.Burrows@qimr.edu.au
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.
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.
