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<p>Fish allergy is a significant global health concern and often leads to persistent and potentially severe hypersensitivity reactions. The molecular heterogeneity of fish allergens poses challenges for developing broadly applicable immunotherapies. In this study, an integrated immunoinformatics pipeline was used to design a multi-epitope vaccine construct targeting three major fish allergens: parvalbumin, enolase, and aldolase. Predicted B-cell and T-cell epitopes were screened for immunogenicity, non-allergenicity, and lack of toxicity, and the selected peptides were assembled into a 432-amino acid chimeric construct using rationally chosen linkers to facilitate antigen processing. Computational analyses predicted the construct to exhibit favorable physicochemical properties, including stability, solubility, and a broad theoretical population coverage. Docking and molecular dynamics simulations suggested a potential interaction with Toll-like receptor 4, offering preliminary insight into possible innate immune engagement. As these findings are entirely in silico, they represent a theoretical framework; experimental validation is necessary to determine the construct’s biological behavior, safety, and immunological relevance.</p>

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Design of a multiepitope immunotherapy for fish allergy

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年2月13日

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  • Abdelfateh Chourir,
  • Hafs Essaadi,
  • Farah Makhloufi,
  • Aya Abidou,
  • Ouissal Hachlaf,
  • Zineb Lafi,
  • Boutaina Elgharbaoui,
  • Mohammed Hakmi,
  • Rachid Eljaoudi,
  • Naima El Hafidi

摘要

Fish allergy is a significant global health concern and often leads to persistent and potentially severe hypersensitivity reactions. The molecular heterogeneity of fish allergens poses challenges for developing broadly applicable immunotherapies. In this study, an integrated immunoinformatics pipeline was used to design a multi-epitope vaccine construct targeting three major fish allergens: parvalbumin, enolase, and aldolase. Predicted B-cell and T-cell epitopes were screened for immunogenicity, non-allergenicity, and lack of toxicity, and the selected peptides were assembled into a 432-amino acid chimeric construct using rationally chosen linkers to facilitate antigen processing. Computational analyses predicted the construct to exhibit favorable physicochemical properties, including stability, solubility, and a broad theoretical population coverage. Docking and molecular dynamics simulations suggested a potential interaction with Toll-like receptor 4, offering preliminary insight into possible innate immune engagement. As these findings are entirely in silico, they represent a theoretical framework; experimental validation is necessary to determine the construct’s biological behavior, safety, and immunological relevance.