Comparative genomic of the teleost cathepsin B and H and involvement in bacterial induced immunity of miiuy croaker.

Cathepsins are a family of lysosomal proteases play different roles at physiological and pathological states and present in almost all animals as well as other organisms. Cathepsins B and H are both cysteine proteases of cathepsins. Cathepsin B and H have been studied playing parts in protein degradation/turnover, antigen presentation/processing and hormone maturation in mammals. However, little is known about the structures and functions of cathepsin B and H in teleosts. In the present study, we identified and characterized the full-length miiuy croaker (Miichthys miiuy) cathepsin B and H genes. The sequence analysis results showed that both cathepsin B and H contain the characteristics of papain family with a signal peptide, propeptide and mature peptide regions. The comparison of the genomic organizations and locations indicated the conserved synteny and mild evolution in the cathepsin B and H genes adjacent regions. In addition, the gene synteny analysis showed that miiuy croaker cathepsin B has a closer relationship to stickleback and fugu than to cave fish and zebrafish, and cathepsin H was most similar with the 2 subtype in tilapia and fugu. By phylogenetic analysis, miiuy croaker cathepsin B and H were all assigned to cysteine proteases, and with a close relationship to Salmo salar cathepsin B and Oplegnathus fasciatus cathepsin H, respectively. Quantitative real-time RT-PCR analysis results confirmed that cathepsin B and H genes expressed ubiquitously in all tested healthy tissues from miiuy croaker. Furthermore, up-regulated expression of the cathepsin B and H transcripts in liver, spleen and kidney after exposure upon Vibrio anguillarum suggested that they may play important roles in innate immune response and antigen processing of miiuy croaker.