Abstract

Heat shock protein 90 family, a class highly conserved protein and important molecular chaperone and its plays a role in enhancing animal adaptability to environmental stress and improving immunity. In this study, a full-length HSP90β cDNA (ToHSP90β) sequence was identified from Trachinotus ovatus. The cDNA of ToHSP90β was 2648 base-pairs (bp) long and contained a 5′-terminal untranslated region of 130 bp, a 3′-terminal untranslated region of 334 bp, and the open reading frame length 2184 bp, which can encode 728 amino acids. The ToHSP90β has a heat shock protein 90 family signature. The ToHSP90β amino acid sequence has high homology with other fish HSP90β amino acids (92.5-99.17%) and contains five conserved signal regions and a structural feature of the cytoplasmic HSP90 family. Phylogenetic tree analysis indicated that ToHSP90β was most closely related to Seriola dumerili HSP90β. Tissues expression analysis showed that the ToHSP90β was expressed in all nine tissues of T. ovatus, and its expression was the highest in the intestine. The stocking density significantly affected the expression of ToHSP90β in the kidney and brain tissues, and its expression levels increased significantly with increasing stocking densities, indicating that it plays an important regulatory role in the process of T. ovatus’ chronic stress response. After Cryptocaryon irritans infection, the mRNA expression of ToHSP90β was significantly increased in liver and kidney tissues, indicating that ToHSP90β would be involved in the immune regulatory response. This study was the first to analyze the expression pattern of HSP90β mRNA in T. ovatus tissues and their expression responses to stocking density stress and C. irritans infection. To provide a theoretical basis for further study of the function of fish HSP90 and its physiological mechanism in environmental stress and parasite infection.

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