Detection of antimicrobial peptides related to piscidin 4 in important aquacultured fish

Epithelial surfaces of fish, such as the gut, skin and gills, comprise a large surface area for possible pathogen invasion. Antimicrobial peptides (AMPs), innate immunity components, play a significant role in protecting fish. Piscidins are a family of AMPs. In this study, we detected the presence of the recently discovered piscidin 4 via bug blot, Western blot, ELISA and/or immunohistochemistry in striped bass ( Morone saxatilis), white bass ( M. chrysops), European seabass ( Dicentrarchus labrax), gilthead seabream ( Sparus aurata), red drum ( Sciaenops ocellatus), and barramundi ( Lates calcarifer). Via bug blot, gill extracts from all species had antibacterial activity corresponding to the migration rate of piscidin 4. Western blotting showed that piscidin 4 immunoreactivity was greatest in striped bass gill extract. The concentrations of piscidin 4 detected by the ELISA in striped bass gill (∼20 μg/ml) were well within the levels that are inhibitory to important fish bacterial pathogens. Piscidin 4 was also detected via immunohistochemistry in all fish except barramundi. Piscidin 4-positive cells were identified as mast cells (MC), but not all MC were piscidin 4-positive. Species, age, size and physiological condition at sampling were some factors that might affect piscidin expression in different species. Our data provide strong evidence that piscidin 4 isoforms are present in all these commercially important species.