TCR contact residue hydrophobicity is a hallmark of immunogenic CD8+ T cell epitopes
Abstract
The design of effective T-cell vaccines against pathogens and tumor antigens is challenged by the highly inefficient identification of the subset of peptides from a given antigen that effectively stimulate an immune response. Here we report that the relative hydrophobicity of T-cell receptor contact residues is markedly enriched in immunogenic major histocompatibility complex class I epitopes in both human and murine MHCs, and in both self and pathogen-derived immunogenic epitopes. Incorporating hydrophobicity into T-cell epitope prediction models increases the efficiency of epitope identification, which will manifest in the time and cost of T-cell vaccine development. Amino acid hydrophobicity may represent a biochemical basis by which T cells discriminate immunogenic epitopes within the background of self peptides.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- April 2015
- DOI:
- 10.1073/pnas.1500973112
- Bibcode:
- 2015PNAS..112E1754C