title: Have we cut ourselves too short in mapping CTL epitopes?
abstract: 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.
authors.affiliation: Queensland Institute of Medical Research, 300 Herston Road, Brisbane, Qld 4029, Australia. Scott.Burrows@qimr.edu.au
authors.forename: Scott R
authors.initials: SR
authors.lastname: Burrows
authors.forename: Jamie
authors.initials: J
authors.lastname: Rossjohn
authors.forename: James
authors.initials: J
authors.lastname: McCluskey
mesh_terms: D000818:Animals; D018984:Epitopes, T-Lymphocyte / Q000737:chemistry / Q000276:immunology*; D006649:Histocompatibility Antigens / Q000276:immunology; D006801:Humans; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry / Q000276:immunology; D013602:T-Lymphocytes, Cytotoxic / Q000737:chemistry / Q000276:immunology*
chemical_list: D018984:Epitopes, T-Lymphocyte; D006649:Histocompatibility Antigens; D011948:Receptors, Antigen, T-Cell