Identification and Cross-reactivity Analysis of Sarcoplasmic-Calcium-Binding Protein: A Novel Allergen in Crassostrea angulata.
Tian-Jiao HanMeng LiuFei HuanMeng-Si LiFei XiaYi-Yu ChenGui-Xia ChenMin-Jie CaoGuang-Ming LiuPublished in: Journal of agricultural and food chemistry (2020)
Oysters are an important shellfish group known to cause food allergy; however, knowledge of their sensitization components and cross-reactivity is limited. This study aimed to identify a novel allergen in Crassostrea angulata and investigate its cross-reactivity. To this end, a 20 kDa protein was purified from oyster and confirmed to be a sarcoplasmic-calcium-binding protein (SCP) by LC-MS/MS. A 537 bp open reading frame was obtained from oyster SCP total RNA, which encoded 179 amino acids, and was expressed in Escherichia coli. According to the circular dichroism results, digestion assay, and inhibition ELISA, the recombinant SCP (rSCP) exhibited similar physicochemical properties and IgG-binding activity to native SCP. rSCP displayed stronger IgE-binding activity by immunological method. Moreover, a different intensity of cross-reactivity and sequence homology were demonstrated between shellfish species. Collectively, these findings provide novel insight into shellfish allergens, which can be used to aid in the in vitro diagnosis of oyster-sensitized patients.
Keyphrases
- binding protein
- escherichia coli
- amino acid
- end stage renal disease
- newly diagnosed
- ejection fraction
- chronic kidney disease
- prognostic factors
- high throughput
- high intensity
- dna binding
- transcription factor
- peritoneal dialysis
- cystic fibrosis
- allergic rhinitis
- multidrug resistant
- biofilm formation
- cell free
- protein protein