Exploration of digestion-resistant immunodominant epitopes in shrimp (Penaeus vannamei) allergens

The digestion products of Penaeus vannamei still had sensitizing and eliciting capacity; however, the underlying mechanism has not been identified. This study analyzed the structural changes of shrimp proteins during digestion, predicted the linear mimotope peptides and first validated the allergenicity of immunodominant e-pitopes with binding ability. The results showed that the shrimp proteins were gradually degraded into small peptides during digestion, which might lead to the destruction of linear epitopes. However, these peptides carried IgE epitopes that still trigger allergic reactions. Eighteen digestion-resistant epitopes were predicted by multiple immunoinformatics tools and digestomics. Five epitopes contained more critical amino acids and had strong molecular docking (P1: DSGVGIYAPDAEA, P2: EGELKGTYYPLTGM, P3: GRQGDPHGKFDLPPGV, P4: IFAWPHKDNNGIE, P5: KSTESSVTVPDVPSIHD), and these epitopes were identified as novel IgE binding immunodominant epitopes in Penaeus vannamei. These findings provide novel insight into allergenic epitopes, which might serve as key targets for reducing the allergenicity in shrimp.

Automated summary

This study analyzed the structural changes of shrimp proteins during digestion, predicted the immunodominant epitopes, and validated their allergenicity. The results showed that shrimp proteins were degraded into peptides during digestion, but still carried IgE epitopes that trigger allergic reactions.