Characterization, Epitope Identification, and Cross-reactivity Analysis of Tropomyosin: An Important Allergen of Crassostrea angulata .
Xiao YunMeng-Si LiYiyu ChenFei HuanMin-Jie CaoDong LaiGui-Xia ChenGuang-Ming LiuPublished in: Journal of agricultural and food chemistry (2022)
Oyster is a common shellfish product in China, which is associated with food allergy. However, there is still lack of research on allergens in oysters. In this study, tropomyosin (TM), an important allergen of Crassostrea angulata , was purified and identified by mass spectrometry. Subsequently, TM was cloned and expressed, with a sequence of size 852 bp, encoding 284 amino acid residues. The results of circular dichroism, digestion assay, inhibition enzyme-linked immunosorbent assay, and basophil activation test showed that recombinant TM had similar physicochemical properties and immunological properties to native TM. Furthermore, two conformational mimotopes were obtained and 10 IgE linear epitopes were verified. Meanwhile, different degrees of cross-reactivity were observed between C. angulata TM and the other 8 shellfish TMs using antibodies and serological analysis, which may relate to the 3 conserved epitope regions. These findings are expected to provide a theoretical basis for the molecular diagnosis of oyster allergy and cross-reactivity among shellfish.
Keyphrases
- mass spectrometry
- amino acid
- high throughput
- high resolution
- molecular dynamics
- liquid chromatography
- transcription factor
- monoclonal antibody
- high performance liquid chromatography
- transcranial magnetic stimulation
- allergic rhinitis
- capillary electrophoresis
- simultaneous determination
- ms ms
- infectious diseases
- tandem mass spectrometry