The responsive expression of a chitinase gene in the ridgetail white prawn Exopalaemon carinicauda against Vibrio anguillarum and WSSV challenge.

Chitinases are essential enzymes for crustaceans and participates in several biological processes, such as nutrient digestion, morphogenesis, pathogenesis, and pathogen defense. In the present study, the full-length cDNA of Chi (named EcChi) was cloned from the hemocytes of ridgetail white prawn Exopalaemon carinicauda by rapid amplification of cDNA ends methods. The full-length cDNA of EcChi was 1,319 bp, including contains a 5'-untranslated region (UTR) of 42 bp, 3'-UTR of 101 bp with a poly (A) tail, an open-reading frame of 1,176 bp, encoding a 391-amino acid polypeptide with the predicted molecular weight of 43.71 kDa and estimated isoelectric point of 4.78. Sequence analysis revealed that the conserved chitinases family 18 active site was predicted in the amino acid sequence of EcChi. BLAST analysis revealed that amino acids of EcChi shared high identity (61-77 %) with that of other crustaceans. Quantitative real-time PCR analysis indicated that EcChi could be detected in all the tested tissues, and strongly expressed in hepatopancreas of E. carinicauda. After challenged with Vibrio anguillarum and WSSV, EcChi transcripts both in hemocytes and hepatopancreas increased significantly in the first 3 h, respectively. These results indicated that EcChi might be involved in the innate immune responses to V. anguillarum and WSSV in E. carinicauda.