Cross-reactivity and conserved epitope analysis of tropomyosin from Lateolabrax japonicus and shellfish species

Meng-Si Li; Fei Xia; Qing-Mei Liu; Fa-Jie Li; Yu-Ni Liao; Li-Qiang Zhong; Gui-Xia Chen; Lian-Zhong Luo; Yi-Xiang Liu; Guang-Ming Liu

doi:10.1016/j.foodchem.2025.144755

Cross-reactivity and conserved epitope analysis of tropomyosin from Lateolabrax japonicus and shellfish species

Food Chem. 2025 Sep 30:487:144755. doi: 10.1016/j.foodchem.2025.144755. Epub 2025 May 16.

Authors

Affiliations

¹ College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Jimei University, Xiamen, Fujian 361021, China; School of Food Engineering, Zhangzhou Institute of Technology, Zhangzhou, Fujian 363000, China.
² College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Jimei University, Xiamen, Fujian 361021, China.
³ Women and Children's Hospital Affiliated to Xiamen University, Xiamen, Fujian 361003, China.
⁴ Engineering Research Center of Marine Biopharmaceutical Resources, Xiamen Medical College, Xiamen, Fujian 361023, China.
⁵ College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Jimei University, Xiamen, Fujian 361021, China; Xiamen Ocean Vocational college, Xiamen, Fujian 361102, China. Electronic address: gmliu@jmu.edu.cn.

PMID: 40398224
DOI: 10.1016/j.foodchem.2025.144755

Abstract

The phenomenon of cross-reactivity within TM between fish and shellfish has received scant attention. In the study, TM of Lateolabrax japonicus, Scylla paramamosain and Mactra quadrangularis were considered as research objects. The results indicated L. japonicus TM exhibited weak binding for both rabbit anti-S. paramamosain/M. quadrangularis TM antibody. However, a significant IgE-binding capacity was observed for three TM in 11 of 18 fish-sensitised patients. Additionally, three TM also could activated basophils in 6 fish-sensitised patients. Subsequently, seven IgE epitopes of L. japonicus TM were confirmed. Two conserved epitopes (LERTEERA, LKTVQNN) and four critical amino acids (E, A, L, and R) were found across L. japonicus and shellfish TM, suggesting these could be responsible for cross-reactivity. These findings were expected to reduce the allergenicity of fish by destroying IgE epitopes through food processing or deleting IgE epitopes using molecular biotechnology, which have important implications for food safety and allergy management.

Keywords: Basophil activation test; Conserved epitope; Cross-reactivity; Lateolabrax japonicus; Shellfish; Tropomyosin.

MeSH terms

Allergens / chemistry
Allergens / immunology
Amino Acid Sequence
Animals
Cross Reactions
Epitopes* / chemistry
Epitopes* / genetics
Epitopes* / immunology
Fish Proteins* / chemistry
Fish Proteins* / genetics
Fish Proteins* / immunology
Fishes / immunology
Food Hypersensitivity / immunology
Humans
Immunoglobulin E / immunology
Rabbits
Shellfish* / analysis
Tropomyosin* / chemistry
Tropomyosin* / genetics
Tropomyosin* / immunology

Substances

Tropomyosin
Epitopes
Immunoglobulin E
Allergens
Fish Proteins