Physicochemical characterization and identification of major linear epitopes of sarcoplasmic calcium‐binding protein (SCP) allergen from Pacific oyster (Crassostrea gigas).
- Resource Type
- Article
- Authors
- Cheng, Qingli; Feng, Xiaowen; Zhao, Xiaohan; Gu, Ruizeng; Lu, Jun; Liu, Wenying; Li, Guoming
- Source
- Journal of the Science of Food & Agriculture. Jul2022, Vol. 102 Issue 9, p3551-3562. 12p.
- Subject
- *PACIFIC oysters
*IMMUNOGLOBULIN E
*CRASSOSTREA
*CALCIUM-binding proteins
*OYSTERS
*PEPSIN
*ALLERGENS
*EPITOPES
*MOLECULAR weights
- Language
- ISSN
- 0022-5142
BACKGROUND: Food allergy is a serious public nutritional health problem that has attracted extensive worldwide attention. Shellfish allergy is a long‐lasting disorder that has a lifelong impact on health. Sarcoplasmic calcium‐binding protein (SCP) plays a vital role in cell and muscle functions and has been identified as an allergen in oyster. RESULTS: In this study, recombinant SCP (rSCP) with a molecular mass of 21 kDa was produced and identified based on SCP amino acid sequencing of Pacific oyster (Crassostrea gigas), and was used as a follow‐up experimental material. Its physicochemical characterization showed that purified rSCP is highly stable to heat and acid‐alkali and trypsin digestion but less resistant to pepsin digestion. We established an animal sensitization model and rSCP displayed stronger Immunoglobulin E (IgE)‐binding activity with rat serum in the rSCP + cholera toxin (CT) group compared with the CT group and a control group. Five epitope peptides were identified as linear immunodominant epitopes by indirect competitive enzyme‐linked immunosorbent assay (icELISA) for the first time. We also found that conformational epitopes may play a major role in the immunoreactivity of SCP. CONCLUSION: These results are significant for understanding hypersensitization of humans to oyster and offer available preventive measures and treatment programs in further research. © 2021 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]