Cross-Reactivity between Scylla paramamosain and Dermatophagoides farinae : Identification of Tropomyosin and Arginine Kinase as Major Cross-Reactive Allergens

Abstract Scylla paramamosain and Dermatophagoides farinae are dominant allergen sources in Asia, yet the molecular basis of their cross-reactivity remains poorly defined. Among 385 HDM-positive sera, 13.5% exhibited IgE reactivity to S. paramamosain extract, demonstrating serological cosensitization between crustacean and mite in southeastern China. Four homologous allergen pairs, namely, tropomyosin (TM), arginine kinase (AK), troponin C (TnC), and triosephosphate isomerase (TIM), shared >50% sequence identity and were all cross-recognized by IgG on Western blot. Basophil activation testing nevertheless distinguished the pairs functionally, as TM and AK activated basophils in 95% and 88% of cross-reactive patients, whereas TnC and TIM did not reach statistical significance at the group level. AK, conventionally ranked below TM in crustacean allergy, therefore, contributes almost equally to cross-reactivity. Cross-inhibition ELISA further demonstrated directional asymmetry in IgE cross-reactivity, and eight and nine conserved B-cell epitope regions were mapped on TM and AK. These findings clarify the allergen basis of crab-mite cosensitization and support AK-inclusive component-resolved diagnosis.

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Publication Details

Journal
Journal of Agricultural and Food Chemistry
Published
2026-10-16
DOI
https://doi.org/10.1021/acs.jafc.6c11421
Primary Topic
Food Allergy and Anaphylaxis Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Cross-Reactivity between Scylla paramamosain and Dermatophagoides farinae : Identification of Tropomyosin and Arginine Kinase as Major Cross-Reactive Allergens

Fei Xia, Qing-Mei Liu, Chih-Jung Chang, Yixiang Liu et al.
Journal of Agricultural and Food Chemistry
Food Allergy and Anaphylaxis Research
article

Cross-Reactivity between Scylla paramamosain and Dermatophagoides farinae : Identification of Tropomyosin and Arginine Kinase as Major Cross-Reactive Allergens

Fei Xia, Qing-Mei Liu, Chih-Jung Chang, Yixiang Liu, Feng Lin, Yubao Cui, Liqiang Zhong, Mengsi Li, Guangming Liu
article en

Abstract

Abstract Scylla paramamosain and Dermatophagoides farinae are dominant allergen sources in Asia, yet the molecular basis of their cross-reactivity remains poorly defined. Among 385 HDM-positive sera, 13.5% exhibited IgE reactivity to S. paramamosain extract, demonstrating serological cosensitization between crustacean and mite in southeastern China. Four homologous allergen pairs, namely, tropomyosin (TM), arginine kinase (AK), troponin C (TnC), and triosephosphate isomerase (TIM), shared >50% sequence identity and were all cross-recognized by IgG on Western blot. Basophil activation testing nevertheless distinguished the pairs functionally, as TM and AK activated basophils in 95% and 88% of cross-reactive patients, whereas TnC and TIM did not reach statistical significance at the group level. AK, conventionally ranked below TM in crustacean allergy, therefore, contributes almost equally to cross-reactivity. Cross-inhibition ELISA further demonstrated directional asymmetry in IgE cross-reactivity, and eight and nine conserved B-cell epitope regions were mapped on TM and AK. These findings clarify the allergen basis of crab-mite cosensitization and support AK-inclusive component-resolved diagnosis.

Journal of Agricultural and Food Chemistry
Jimei University (CN), Zhejiang Institute of Freshwater Fisheries (CN), Xiamen Chang Gung Hospital (CN), Wuxi People's Hospital (CN), Xiamen Ocean Vocational College (CN), Nanjing Medical University (CN)
National Natural Science Foundation of China
Openalex Percentile: Top 15%
Food Allergy and Anaphylaxis Research
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