摘要Oyster,as a common aquatic food,play an important role in shellfish allergy.In this study,2 tropomyosin(TM)isoforms TM-α and TM-β(TM-α/-β)in Alectryonella plicatula were identified.The sequences of 852 bp encoding 284 amino acids of TM-α/-β and 2 recombinant proteins were obtained,respectively.There were 12 amino acid differences between TM-α/-β.The results of immunological experiments indicated that TM-β had stronger immunobinding activity and immunoreactivity than those of TM-α.Structural analysis showed that TM-β had more α-helix and higher surface hydrophobicity than TM-α.Sequences and epitopes alignment with shellfish TMs revealed that amino acids of TM-β were more frequently recognized as IgE epitopes in other shellfish TMs than TM-α.Differences in structure and sequence account for the higher immunological activity of TM-β compared to TM-α.These findings provide a theoretical basis for enriching the understanding of shellfish TM and accurate diagnosis of allergic components.