Background: T cells are pivotal in the elicitation of allergic diseases. Analogues of T-cell epitope peptides with a modification at a T-cell receptor (TCR) contact site can alter selected T-cell effector functions. Thus the ability to modulate allergen-specific T-cell responses towards TH1-like by stimulation with peptide analogues may downregulate allergic inflammation. Objectives: The purpose of this study was to characterize the minimal epitope recognized by cloned T cells of a dominant Lol p 5 epitope, p105-116, and identify the critical residues involved in TCR and MHC contact. Methods: Using peptides with progressive truncation of N- and C-terminal residues in T-cell proliferation assays, we identified the core epitope recognized by cloned CD4+ T cells. An additional series of peptides with single amino acid substitutions were used in T-cell proliferation and live-cell MHC binding assays. Taken together, these results allowed identification of MHC binding and TCR contact residues of p105-116. Results: The core epitope of p105-116 was identified as residues 107-114. Within this core epitope, 3 residues were found to be important for MHC binding, positions 107, 110, and 112, whereas those at positions 108, 109, 110, 111, and 113 were putative TCR contact residues. Conclusions: The identification of the TCR and MHC contact residues of a dominant Lol p 5 T-cell epitope and analogues of this peptide capable of modulating T-cell responses will allow the evaluation of these peptides' potential as immunotherapeu-tic agents for rye grass pollen allergic disease. Copyright © 1999 by Mosby, Inc.
Burton, M. D., Blaher, B., Suphioglu, C., O’Hehir, R. E., Carbone, F. F. R., & Rolland, J. M. (1999). T-cell receptor contact and MHC binding residues of a major rye grass pollen allergen T-cell epitope. Journal of Allergy and Clinical Immunology, 103(2 II), 255–261. https://doi.org/10.1016/s0091-6749(99)70499-9