IgE Epitope Mapping of Cross-Reactive Tropomyosin between Shrimp and Edible Cricket ( Gryllus bimaculatus )

Abstract Tropomyosin is a pan-allergen in crustaceans known to cross-react with homologous proteins from edible insects. However, epitope-level cross-reactivity in edible insects remains poorly defined. This study aimed to identify IgE-binding epitopes of tropomyosin and to evaluate their cross-reactivity between shrimp and the edible two-spotted cricket. Here, sera from shrimp-allergic patients were screened for IgE-binding to proteins from Pacific white shrimp (Penaeus vannamei) and two-spotted cricket (Gryllus bimaculatus). Candidate tropomyosin epitopes from the two-spotted cricket were predicted. The cross-reactivity of tropomyosin was assessed using an inhibition dot blot assay, inhibition ELISA, and LAD2 cell degranulation assay. Approximately 40% of shrimp-allergic patients showed IgE reactivity to crude proteins from shrimp and the two-spotted cricket. Four identified peptide epitopes induced β-hexosaminidase release from LAD2 cells. These findings provide insights into the molecular basis of tropomyosin cross-reactivity essential for the development of biomarker-based tools for allergen risk assessment in the food industry.

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Journal
Journal of Agricultural and Food Chemistry
Published
2026-09-04
DOI
https://doi.org/10.1021/acs.jafc.6c04758
Primary Topic
Food Allergy and Anaphylaxis Research
Type
article
Field-Weighted Citation Impact
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article

IgE Epitope Mapping of Cross-Reactive Tropomyosin between Shrimp and Edible Cricket ( Gryllus bimaculatus )

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article

IgE Epitope Mapping of Cross-Reactive Tropomyosin between Shrimp and Edible Cricket ( Gryllus bimaculatus )

Chotika Yokthongwattana, Chomdao Sinthuvanich, Yiwa Suksawat, Pharima Phiriyangkul, Chama Inson, Siriluk Kumsui, Tran Thi Cam Lien, Kunlanan Thuraphan
article en

Abstract

Abstract Tropomyosin is a pan-allergen in crustaceans known to cross-react with homologous proteins from edible insects. However, epitope-level cross-reactivity in edible insects remains poorly defined. This study aimed to identify IgE-binding epitopes of tropomyosin and to evaluate their cross-reactivity between shrimp and the edible two-spotted cricket. Here, sera from shrimp-allergic patients were screened for IgE-binding to proteins from Pacific white shrimp (Penaeus vannamei) and two-spotted cricket (Gryllus bimaculatus). Candidate tropomyosin epitopes from the two-spotted cricket were predicted. The cross-reactivity of tropomyosin was assessed using an inhibition dot blot assay, inhibition ELISA, and LAD2 cell degranulation assay. Approximately 40% of shrimp-allergic patients showed IgE reactivity to crude proteins from shrimp and the two-spotted cricket. Four identified peptide epitopes induced β-hexosaminidase release from LAD2 cells. These findings provide insights into the molecular basis of tropomyosin cross-reactivity essential for the development of biomarker-based tools for allergen risk assessment in the food industry.

Journal of Agricultural and Food Chemistry
Can Tho University (VN), Kasetsart University (TH), Phramongkutklao Hospital (TH)
Kasetsart University Research and Development Institute, Faculty of Science, Kasetsart University
Openalex Percentile: Top 13%
Food Allergy and Anaphylaxis Research
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