RESUMO
Parasitic infestations and their control programmes are one among the challenges to be considered the most significant in aquaculture. A parasitic infestation was studied elaborately in Asian Seabass, Lates calcarifer juveniles with clinical signs, post-mortem findings, morphological and molecular identifications. In addition, those fish were also treated with emamectin benzoate (EMB) @ 50 µg kg-1 of fish body weight (BW) d-1 for 10 consecutive days under the controlled wet lab facility by feeding through the medicated feed at 4% BW. Results showed that the parasitic prevalence, parasitic intensity (PI) and mortality were 45.5%, 8.17 ± 0.15 per fish and 40% over a period of one week in that existing cage culture. The parasite was identified as a crustacean bloodsucker, anchor worm Lernaea sp. and EMB was found to be 100% effective with significant reduction in PI over a period of 10 days with improved survival rate of 90% against the untreated group. Infested but treated group revealed substantial haematological improvement in parameters such as RBC, WBC, Hb, PCV, large lymphocytes, small lymphocytes and total lymphocytes (P < 0.01). Similarly, comparative histopathology of vital organs also revealed no discernible lesions between the healthy and treated fish juvenile as compared to that of infested untreated group. Hence, EMB can be used to control the Lernaea sp. infestation in Asian Seabass.
RESUMO
Copper Zinc Superoxide dismutase (CuZnSOD) is the family of most important antioxidant metalloenzymes that protects tissues from damage by reactive oxygen species (ROS). In the present study, the intracellular copper zinc SOD from the Asian seabass Lates calcarifer (Lc-icCuZnSOD) was identified by RNA ligase mediated rapid amplification of cDNA ends (RLM-RACE) technique. The full-length cDNA of Lc-icCuZnSOD consisted of 809 nucleotides with an open-reading frame of 465 bp encoding 154 amino acids and N-Glycosylation site (NVTA) within. The predicted molecular mass of the protein is 15.84 kDa with an estimated pI of 5.52. The deduced amino acid sequence of Lc-icCuZnSOD shared high degree of homology with known CuZnSODs from other species. CuZn binding sites (H47, H49, H64, and H121 for Cu(2+) and H72, H81, and ASP84 for Zn(2+)), two cysteine residues (aa 58 and 147) that form a disulfide bond, and CuZnSOD family signature sequences (GFHVHAFGDNT, aa 45-55 and GNAGGRLACGVI, aa 139-150) were highly conserved among fish species. Temporal and tissue specific expression of Lc-icCuZnSOD was significantly differentially altered in Asian seabass challenged with Vibrio anguillarum indicating possible role in antioxidant activities involved in the innate immune defense mechanisms.
