Cloning of Two HSP Genes of Eriocheir hepuensis and Their Expression under Vibrio parahaemolyticus Stress

Abstract

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.