Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: International Journal of Biological Macromolecules
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
