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The Sox family plays essential roles as transcription factors in vertebrates; however, little is known about the Sox family in Lutraria sieboldii. L. sieboldii are pleasant to eat with a short growth cycle and have become one of the best bottom-seeded enrichment species in Guang Xi. In this study, Sox2 (named LsSox2) and Sox9 (named LsSox9) from L. sieboldii were cloned, and their expression patterns were analyzed. The length of the LsSox2 gene coding sequence was 1011 bp, encoding 336 amino acids, and LsSox9 was 1449 bp, encoding 482 amino acids. LsSox2 had its highest expression levels in the ovary, which were 356 times those in testis, whereas LsSox9 presented higher expression in testis, which was 6 times more highly expressed than in the ovary. LsSox2 exhibited the highest expression during the morula stage, which was 20 times that of the D-shaped larvae or zygote. LsSox9 exhibited two expression peaks, one at the four-cell stage and the other at the trochophore stage, while the lowest expression was in the zygote. LsSox9 was 73 times more highly expressed in the four-cell stage than in the zygote stage. During gonadal development, LsSox2 presented the highest expression in the mature ovary, which was 756 times more highly expressed than in mature testis. LsSox9 presented higher expression in testis at the emission stage which was 6 times more highly expressed than in the ovary. These results indicate that LsSox2 and LsSox9 may play important roles in embryonic and gonadal development. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]