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United States Department of Agriculture

Agricultural Research Service

Research Project: MOLECULAR ANALYSIS OF VIRULENCE DETERMINANTS OF SELECT BACTERIA IN FISH DISEASES Title: Channel Catfish (Ictalurus punctatus Rafinesque, 1818) CD156a (ADAM Metallopeptidase Domain 8): cDNA Clone, Characterization and Expression in Tissues

Authors
item Yeh, Hung-Yueh
item Klesius, Phillip

Submitted to: Veterinary Immunology and Immunopathology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: April 28, 2009
Publication Date: November 15, 2009
Repository URL: http://hdl.handle.net/10113/38247
Citation: Yeh, H., Klesius, P.H. 2009. Channel catfish (Ictalurus punctatus Rafinesque, 1818) CD156a (ADAM Metallopeptidase domain 8): cDNA clone, characterization and expression in tissues. Veterinary Immunology and Immunopathology. 132:307-313.

Interpretive Summary: Channel catfish is the most important aquacultural industry in the southeastern U.S. Like mammalian cells, channel catfish has many clusters of differentiation (CD) antigens on the cell surface. One of them is CD156a, which plays many roles in physiological and immune functions. In this study, we cloned, sequenced and characterized the channel catfish CD156a complimentary DNA (cDNA). The length of the channel catfish CD156a cDNA had 3035 nucleotides. An open reading frame appears to encode an 850-amino-acid peptide with a calculated molecular mass of 94.6 kDa. The peptide had three potential N-glycosylation sites. By comparison with other species counterparts, the degree of homology of the CD156a amino acid sequences ranged from 31.6% (vs. chicken CD156a) to 59.5% (vs. zebrafish CD156a). The channel catfish CD156a peptide could be structurally divided into nine domains. Several features for CD156a functions were conserved in channel catfish. The CD156a transcript was detected by two-step RT-PCR in anterior kidney and gill, suggesting that CD156a may involve in innate immune response in channel catfish.

Technical Abstract: CD156a, also known as a disintegrin and metalloprotease domain 8 (ADAM-8), is a type 1 transmembrane glycoprotein of the ADAM family. This protein plays important roles in immune and other physiological functions. In this communication, the channel catfish CD156a cDNA was characterized and its expression in various tissues was determined. The full-length of the channel catfish CD156a cDNA had 3035 nucleotides, including an open reading frame which appears to encode an 850-amino-acid peptide with a calculated molecular mass of 94.6 kDa. The peptide had three potential N-glycosylation sites. By comparison with other species counterparts, the degree of homology of the CD156a amino acid sequences ranged from 31.6% (vs. chicken CD156a) to 59.5% (vs. zebrafish CD156a). The channel catfish CD156a peptide could be structurally divided into nine domains. Several canonical features for CD156a functions were conserved in channel catfish. The CD156a transcript was detected by two-step RT-PCR in anterior kidney and gill, suggesting that CD156a may involve in innate immune response in channel catfish. Reagents for further elucidating the immune functions of channel catfish CD156a are under developing.

Last Modified: 11/28/2014
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