Abstract
Superoxide dismutase (SOD, EC 1.15.1.1) is an enzyme catalyzing the dismutation of the superoxide anion into molecular oxygen and hydrogen peroxide. In the present study, the full length cDNA of extracellular copper–zinc superoxide dismutase (MnECSOD) from Macrobrachium nipponense was cloned (GenBank accession no. JX045662). Analysis of the nucleotide sequence revealed that the MnECSOD cDNA consisted of 817bp with an open reading frame (ORF) of 597bp encoding a polypeptide of 198 amino acids with a putative signal peptide of 19 amino acids. The mature protein had a predicted molecular weight of 18.71kDa with an estimated pI of 4.87. Four copper binding sites, 4 zinc binding sites and 2 cysteines involved in the formation of the disulfide bridge were conserved in the protein. Sequence comparison showed that the MnECSOD protein had 86% and 55% similarity to that of freshwater prawn Macrobrachium rosenbergii and white shrimp Litopenaeus vannamei, respectively. After challenge with Aeromonas hydrophila, the expression of MnECSOD mRNA in the hepatopancreas was increased responsively. After a drastic decrease at 12h, the expression level increased again by 6.75-fold compared to that in the control group at 48-h post-infection. These results may indicate that MnECSOD was involved in the innate immune responses of M. nipponense.
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