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ZFIN ID: ZDB-PUB-140903-1
Comparative genomic of the teleost cathepsin B and H and involvement in bacterial induced immunity of miiuy croaker
Che, R., Wang, R., Xu, T.
Date: 2014
Source: Fish & shellfish immunology   41(2): 163-71 (Journal)
Registered Authors:
Keywords: Cathepsin, Comparative genomics, Expression pattern, Gene synteny, Immune responses, Miichthys miiuy (miiuy croaker), Teleost genome
MeSH Terms:
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cathepsin B/genetics*
  • Cathepsin B/immunology
  • Cathepsin H/genetics*
  • Cathepsin H/immunology
  • Gene Expression Regulation/immunology*
  • Liver/metabolism
  • Molecular Sequence Data
  • Perciformes/genetics*
  • Perciformes/immunology
  • Perciformes/microbiology*
  • Phylogeny*
  • Real-Time Polymerase Chain Reaction
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Species Specificity
  • Spleen/metabolism
  • Synteny
PubMed: 25181651 Full text @ Fish Shellfish Immunol.
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 characteristic 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.