Natural shrimp (Litopenaeus vannamei) tropomyosin shows higher allergic properties than that of recombinant one as compared through SWATH-MS based proteomics and immunological response.

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. While the allergenicity of rTM has not been compared with natural TM (nTM) based on in vitro digestion profile. In this work, IgG-/IgE binding, allergen peptides and degranulation ability of the digested samples in simulated gastric fluid (SGF) /simulated intestinal fluid (SIF) /gastrointestinal (GI) from nTM and rTM were evaluated by immunoassay assays, 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 digested samples from rTM (57.8%) matched shrimp allergic epitopes than those from nTM (33.3%). While, the peptide of SITDELDQTF (269-278) appeared most frequently. These findings would supply foundation data for epitope-based immunotherapy to shrimp allergic individuals.