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Natural Shrimp (Litopenaeus vannamei) Tropomyosin Shows Higher Allergic Properties than Recombinant Ones as Compared
Li Li Xu1, Hong Wei Zhang2, Xiao Mei Zhang2
1College of Food Science and Engineering, Ocean University of China, No.5, Yushan Road, Qingdao, Shandong Province 266003, P. R. China.
Abstract:
Tropomyosin (TM) is the major shrimp allergen that could trigger anaphylactic reactions. Recently, recombinant TM (rTM) has been accepted widely in the field of allergen-specific immunotherapy, but the allergenicity of rTM has not been compared with natural TM (nTM) based on an in vitro digestion profile. In this work, IgG-/IgE binding, allergen peptides, and degranulation ability of the digested samples in simulated gastric fluid/simulated intestinal fluid/gastrointestinal models from nTM and rTM were evaluated by immunoassays, proteomics, and basophil degranulation assay. Results showed that pepsin-digested and trypsin-digested samples of rTM exhibited lower IgG-/IgE binding and degranulation than those of nTM. More peptides of the digested samples from rTM (57.8%) matched shrimp allergic epitopes than those from nTM (33.3%). However, the peptide SITDELDQTF (269-278) appeared most frequently. These findings would supply foundation data for epitope-based immunotherapy to shrimp allergic individuals.
