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Title: Channel catfish, Ictalurus punctatus, cysteine proteinases: Cloning, characterization and expression of cathepsin H and L

Author
item Yeh, Hung-Yueh
item Klesius, Phillip

Submitted to: Fish and Shellfish Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/20/2008
Publication Date: 2/13/2009
Citation: Yeh, H., Klesius, P.H. 2009. Channel catfish, Ictalurus punctatus, cysteine proteinases: cloning, characterization and expression of cathepsin H and L. Fish and Shellfish Immunology. 26:332-338.

Interpretive Summary: Cathepsin H and cathepsin L (CTSH and CTSSL, respectively), a lysosomal cysteine endopeptidase of the papain family, are involved in antigen presentation. In this report, we sequenced, and characterized the channel catfish CTSH and CTSSL complimentary DNA (cDNA). The complete CTSH and CTSSL cDNA had 1415 and 1639 base pairs, respectively. The open reading frame of CTSH and CTSSL had 326 and 336 amino acid residues, respectively. The degree of identity of the channel catfish CTSH and CTSSL amino acid sequence to the counterparts of other species ranged from 61% to 77%, and 67% to 85%, respectively. The CTSL cDNA was expressed in all tissues examined, while the CTSH was expressed in restrictive tissues. These results provide important information for further exploring the roles of channel catfish cathepsins in antigen processing.

Technical Abstract: The antigen recognition by the host immune system is a complex biochemical process that requires a battery of enzymes. Cathepsins are one of the enzyme superfamilies involving in antigenic degradations. We observed the up-regulation of cathepsin H and L transcripts during the early stage of Edwardsiella ictaluri infection in the preliminary results, and speculated that the cathepsin H and L may play roles in infection. In this report, we identified, sequenced and characterized the channel catfish cathepsin H and L cDNA. The complete channel catfish cathepsin H and L cDNA comprised 1,415 and 1,639 nucleotides, respectively. The open reading frames of cathepsin H and L appear to encode proteins of 326 and 336 amino acid residues, respectively. The degree of conservation of the channel catfish cathepsin H and L amino acid sequence in comparison to other species ranged from 61% to 77%, and 67% to 85%, respectively. The catalytic triad and substrate binding sites are conserved in cathepsin H and L amino acid sequences. The CTSL transcript was expressed in all tissues examined, while the CTSH was expressed in restrictive tissues. These results provide important information for further exploring the roles of channel catfish cathepsins in antigen processing.