Molecular Cloning,\nProkaryotic Expression, and Immunological\nCharacterization of β‑Enolase from Grass Carp (Ctenopharyngodon idella)

β-Enolase\nis a cross-allergen commonly found in\nfungi, plants,\nand aquatic products. Although studies on the allergenicity of fish\nenolase have been reported in recent years, they are still limited\nto a few species of marine fish. Therefore, the detection of freshwater\nfish in the food industry requires more studies of the molecular characterization\nas well as the allergenicity of enolase. In this study, the nucleotide\nsequence of β-enolase from grass carp was obtained by molecular\ncloning technology. Structural domain analysis showed that it contained\nthe characteristic structural domains of the enolase superfamily,\nand homology analysis indicated that enolases are highly conserved\nevolutionarily. Recombinant β-enolase was obtained by prokaryotic\nexpression, and its allergenicity was assessed by β-enolase-sensitized\nmice, which confirmed the ability of β-enolase to trigger an\nallergic response and cause a rise in Th1 and Th2 immune responses\nin mice. These results suggest that β-enolase could be used\nas a characterizing substance for the detection of fish allergens\nin the food industry as well as the preparation of drugs for allergy-related\nstudies.

Publication Details

Journal
Figshare
Published
2024-09-19
DOI
https://doi.org/10.1021/acs.jafc.4c05931.s001
Primary Topic
S100 Proteins and Annexins
Type
article
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article

Molecular Cloning,\nProkaryotic Expression, and Immunological\nCharacterization of β‑Enolase from Grass Carp (Ctenopharyngodon idella)

Figshare
S100 Proteins and Annexins
article

Molecular Cloning,\nProkaryotic Expression, and Immunological\nCharacterization of β‑Enolase from Grass Carp (Ctenopharyngodon idella)

article en

Abstract

β-Enolase\nis a cross-allergen commonly found in\nfungi, plants,\nand aquatic products. Although studies on the allergenicity of fish\nenolase have been reported in recent years, they are still limited\nto a few species of marine fish. Therefore, the detection of freshwater\nfish in the food industry requires more studies of the molecular characterization\nas well as the allergenicity of enolase. In this study, the nucleotide\nsequence of β-enolase from grass carp was obtained by molecular\ncloning technology. Structural domain analysis showed that it contained\nthe characteristic structural domains of the enolase superfamily,\nand homology analysis indicated that enolases are highly conserved\nevolutionarily. Recombinant β-enolase was obtained by prokaryotic\nexpression, and its allergenicity was assessed by β-enolase-sensitized\nmice, which confirmed the ability of β-enolase to trigger an\nallergic response and cause a rise in Th1 and Th2 immune responses\nin mice. These results suggest that β-enolase could be used\nas a characterizing substance for the detection of fish allergens\nin the food industry as well as the preparation of drugs for allergy-related\nstudies.

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S100 Proteins and Annexins
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