A study on loading multiple epitopes with a single peptide

Guo, Chunyan, Xu, Cuixiang, Feng, Qing, Xie, Xin, Li, Yan, Zhao, Xiangrong, Hu, Jun, Fang, Senbiao and Shang, Lijun (2024) A study on loading multiple epitopes with a single peptide. Journal of Medical Virology, 69(10) (e70004). ISSN 1096-9071

Abstract

Epitopes, the basic functional units of antigens, hold great significance in the field of immunology. However, the structure and composition of epitopes and their interactions with antibodies remain unclear, which limits in‐depth studies on epitopes and the development of subunit vaccines. In a previous study on the localization of anti‐influenza HA monoclonal antibodies (mAbs), three strains with different characteristics reacted with the same peptide. In this study, by conventional immunological assays, computer homology modeling, and molecular docking simulations, we found that (1) the peptide could bind to three strains of mAbs with different reaction characteristics utilizing dif- ferent combinations of immunodominant groups. (2) By computer molecular docking and simulation methods, the immunodominant groups on the two peptides could be com- bined into a multi‐epitope peptide bound to six strains of mAbs. We established a method for multi‐epitope peptide recombination from these immunodominant groups. (3) The immune effect of the recombinant multi‐epitope peptide was better than that of a single peptide. Our findings facilitate the understanding of the composition of antigen epitopes and provide a theoretical and experimental basis for developing polyvalent vaccines and understanding immune responses at the molecular level.

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