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Heat shock proteins (HSPs) are molecular chaperone proteins that can help maintain cellular protein homeostasis, assist in correcting the folding of cellular proteins, and protect organisms from stress when the body is under stress conditions such as temperature changes or bacterial infections. In this study, the HSP10 and HSP40 genes of Eriocheir hepuensis were cloned and named Eh-HSP10 and Eh-HSP40. The results show that the coding sequence length of the HSP10 and HSP40 genes of E. hepuensis was 309 bp and 1191 bp, encoding 102 and 396 amino acids, respectively. The results of protein domain prediction show that Eh-HSP10 has a Cpn10 domain. The Eh-HSP40 protein contains a DnaJ domain, which is characteristic of the HSP40 gene family. The results of qRT-PCR show that the Eh-HSP10 and Eh-HSP40 genes were expressed in different normal tissues, with the highest expression in the heart. Under Vibrio parahaemolyticus stress, the Eh-HSP10 genes peaked at 6 h, and the Eh-HSP40 peaked at 9 h in the hepatopancreas. In the gill, Eh-HSP10 showed a double peak at 24 and 48 h, and the expression of Eh-HSP40 was time-dependent. In the heart, the expression of Eh-HSP10 increased first and then decreased, whereas Eh-HSP40 peaked at 48 h. The results indicate that the Eh-HSP10 and Eh-HSP40 proteins may play a role in protecting E. hepuensis under V. parahaemolyticus infection and that they may be involved in the innate immune response of E. hepuensis against bacteria.

Inhibitors of apoptosis proteins (IAPs) maintain a balance between cell growth and cell death by suppressing caspase activity and modulating immunological responses. Here, two IAPs (EhIap1 and EhIap2) were identified from Eriocheir hepuensis using RT-PCR technology and characterized using bioinformatics software. Sequence analysis showed that the open reading frames of EhIap1 and EhIap2 were composed of 1,839 bp and 696 bp and encoded 612 amino acids and 231 amino acids, respectively. EhIap1 contained two BIR domains, one UBA domain, and one RING domain, and EhIap2 only contained two BIR domains. qRT-PCR showed that EhIap1 and EhIap2 were expressed in various tissues, and their expression levels were highest in the hepatopancreas. Expression levels of EhIAP1 and Eh1ap2 were more than 87.09 and 411 times higher in the hepatopancreas than in muscle, respectively. Under azadirachtin stress, the expression of EhIap1 and EhIap2 was increased in three immune tissues (hepatopancreas, gill, and heart). The expression of EhIap1 was 18.44, 17.75, and 6.16 times higher in hepatopancreas, heart, and gill tissues under azadirachtin stress compared with the control group, respectively. The expression of EhIap2 was 18.44, 15.48, and 3.91 times higher in hepatopancreas, gill, and heart tissue under azadirachtin stress compared with the control group, respectively. The expression of EhIap1 and EhIap2 was higher in surviving individuals than in dead individuals. Overall, EhIap1 and EhIap2 genes were first cloned, and our findings indicate that EhIAPs might be involved in E. hepuensis against azadirachtin through regulating apoptosis.

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