RE: study session31 Jan 2020 12:10
Modi-1 conjugates - novel cutting-edge products
? Strong bias toward hydrophobic amino acids at T-cell receptor
contact residues within immunogenic epitopes (Chowell et al 2015)
? Hydrophobic peptides
? Challenging synthetic properties
? Manufacturing
? Analytical development
Significance
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.
https://www.pnas.org/content/112/14/E1754
Edited by Ira Mellman, Genentech, Inc., South San Francisco, CA, and approved March 2, 2015 (received for review January 21, 2015)