Linear Epitopes Play an Important Role in the Immunoglobulin G (IgG)/Immunoglobulin E (IgE)-Binding Capacity of Scy p 4

Sarcoplasmic calcium-binding protein is a stable allergen in Scylla paramamosain and named Scy p 4. To explore the importance of linear epitopes in the immunoglobulin G (IgG)/immunoglobulin E (IgE)-binding capacity of Scy p 4, chemical denaturants were used to destroy the structure. Scy p 4 was reduced with dithiothreitol and subsequently alkylated with iodoacetamide (IAA). Furthermore, the structural analysis indicated that IAA-Scy p 4 was an unstructured protein. The inhibition enzyme-linked immunosorbent assay showed that IAA-Scy p 4 could inhibit the binding of Scy p 4 to sensitize serum, with inhibition rates reached 55%. Moreover, the linear mimotopes of Scy p 4 were predicted in silico. Three linear epitopes were verified by serological tests and named L-Scy p 4-1 (AA(76-91)), L-Scy p 4-2 (AA(111-125)), and L-Scy p 4-3 (AA(137-146)). Overall, these data provide an understanding of the relationship between the structure and allergenicity about Scy p 4, and the identified linear epitopes can be used for diagnosis and food processing of shellfish allergy.

Automated summary

The study identified linear epitopes of Sarcoplasmic calcium-binding protein (Scy p 4) that play a significant role in the binding capacity of immunoglobulin G (IgG) and immunoglobulin E (IgE). These linear epitopes were able to inhibit the binding of Scy p 4 to sensitized serum, highlighting their potential diagnostic and food processing applications in shellfish allergy. The findings contribute to a better understanding of the relationship between the structure and allergenicity of Scy p 4.