Cloning and sequence analysis of hepcidin-like cDNA Hepc2 from liver of Lateolabrax japonicus

Hepcidin is a unique antimicrobial peptide which exerts broad-spectrum antimicrobial action against Gram-negative and Gram-positive bacteria,as well as fungi.A Hepc-like cDNA was amplified from the liver of Lateolabrax japonicus challenged with a mixed bacteria solution.Using RT-PCR and RACE with a specific primer pair,a full length cDNA sequence Hepc2 of the Hepc-like antimicrobial peptide (GenBank accession number:AY604195) was obtained.Hepc2 cDNA is composed of 581 bases,which contains an ORF of 258 bases,encoding 86 amino acids.The deduced amino acid sequence is conserved between white bass and other fish species,which share eight cysteines at the identical conserved position.The relative molecular weight of the protein is 9418.55dal.The 3′non-coding region is composed of 225bp,with a polyadenylation signal AATAAA sequence appearing at position 189 nt,and poly (A) tail at 212 nt, downstream codon TAA.The signal peptide cleavage site of its deduced protein is presumed between codon 24 and 25. High homologies with Hepc cDNAs and proteins of white bass (Morone chrysops),human and other fish are shown.It indicates that Hepc2 cDNA from Lateolabrax japonicus liver is a new member of the Hepc gene family.