6533b829fe1ef96bd128a48d

RESEARCH PRODUCT

cDNA sequence and tissue expression of an antimicrobial peptide, dicentracin; a new component of the moronecidin family isolated from head kidney leukocytes of sea bass, Dicentrarchus labrax

Giuseppina SalernoNicolò ParrinelloMatteo CammarataPhilippe Roch

subject

Fish ProteinsSignal peptideDNA ComplementaryPhysiologyMolecular Sequence DataIn situ hybridizationBiologyKidneyBiochemistryPeritoneal cavityComplementary DNAGene expressionLeukocytesmedicineAnimalsAmino Acid SequenceRNA MessengerCloning MolecularSea bassPeritoneal CavityMolecular BiologyPeptide sequencePhylogenyHead KidneyBase SequenceSequence Homology Amino AcidMolecular biologymedicine.anatomical_structureGene Expression RegulationBassAntimicrobial Cationic Peptides

description

A 483-bp cDNA was isolated from sea bass (Dicentrarchus labrax) head kidney leukocytes, dicentracin, using PCR primers designed from conserved moronecidin domains. Gene bank analysis revealed that dicentracin cDNA belongs to the moronecidin family. As deduced from alignment with Morone chrysops moronecidin, the precursor of 79 aa appeared to be composed of a signal peptide of 22 aa, followed by the mature AMP (antimicrobial peptide) of 22 aa named dicentracin, and a C-terminal extension of 35 aa. Dicentracin precursor displayed 3 aa substitutions with other moronecidin sequence but none in the mature peptide sequence. Using in situ hybridization assay, dicentracin gene expression was observed in 68-71% of peripheral blood leukocytes, kidney leukocytes or peritoneal cavity leukocytes without significant statistical differences. Dicentracin mRNA was observed in most of the granulocytes, as well as in monocytes from both peripheral blood and head kidney, and in macrophages from peritoneal cavity. No expression was observed in thrombocytes or in lymphocytes.

yearjournalcountryeditionlanguage
2007-04-01
http://hdl.handle.net/10447/7153