Exploring the allergenic potential of sesame oleosins: Isolation and bioinformatics analysis.

This study examined two oleosins of 17 kDa and 15 kDa isolated from Yuzhi white sesame seeds through oil body extraction. The allergens were identified as oleosin H1 (Ses i 4) and oleosin L (Ses i 5) using SDS-PAGE, dot blot analysis, and LC-MS/MS. PCR analysis revealed high sequence homology for the oleosin proteins in the sesame seeds. Utilizing AlphaFold2, bioinformatics tools, and protein-protein docking, the structure and function of these oleosins were analyzed. Ten potential B cell epitope peptides were predicted and mapped onto the α-helix and random coil-dominated oleosome membrane conformation. IgE binding simulations identified key epitopes, B3 (FLTSGAFGL) and B4 (KRGVQEGTLY) for oleosin H1, and B8 (GGFGVAALSV) and B9 (DQLESAKTKL) for oleosin L. Mutational analysis highlighted Glu135, Phe102, Tyr128, Tyr139, Gly136, and Gly132 in oleosin H1, and Leu120, Lys119, and Leu113 in oleosin L as critical residues for binding stability, providing insights into the sensitization mechanism of these epitopes. The integration of bioinformatics and immunoinformatics in this study has contributed to a deeper understanding of the allergy properties of sesame oleosins.