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Title: Channel catfish (Ictalurus punctatus Rafinesque, 1818) tetraspanin membrane protein family: Identification, characterization, and expression analysis of CD63 cDNA

Author
item Yeh, Hung-Yueh
item Klesius, Phillip

Submitted to: Veterinary Immunology and Immunopathology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 8/5/2009
Publication Date: 1/10/2010
Citation: Yeh, H., Klesius, P.H. 2010. Channel catfish (Ictalurus punctatus Rafinesque, 1818) tetraspanin membrane protein family: Identification, characterization, and expression analysis of CD63 cDNA. Veterinary Immunology and Immunopathology. 133:302-308.

Interpretive Summary: Channel catfish lysosome associated membrane protein 3 (LAMP-3), also called CD63, plays many important roles in immuno-physiological functions. In this report, we cloned, sequenced and characterized the channel catfish CD63 transcript. The complete nucleic acid sequence of channel catfish CD63 cDNA comprised of 1,159 nucleotides, including an open reading frame, which appears to encode a putative peptide of 237 amino acid residues. By comparison with human CD63, the channel catfish CD63 peptide can be divided into domains, including four transmembrane domains, three intracellular domains, and one of each small and large extracellular loops. The channel catfish CD63 transcript was detected by RT-PCR in spleen, head kidney, liver, intestine, skin and gill. This result provides important information for further elucidating CD63 in channel catfish.

Technical Abstract: CD63, known as lysosome associated membrane protein 3 (LAMP-3), is a member of the tetraspanin integral membrane protein family. This protein plays many important roles in immuno-physiological functions. In this communication, we report the identification, characterization, and expression analysis of the channel catfish CD63 transcript. The complete nucleic acid sequence of channel catfish CD63 cDNA was comprised of 1,159 nucleotides, including an open reading frame, which appears to encode a putative peptide of 237 amino acid residues. Like other tetraspanin proteins, the channel catfish CD63 peptide can be divided into domains, including four transmembrane domains, three intracellular domains, and one of each small and large extracellular loops. The channel catfish CD63 peptide shares 52-55% identity among fish counterparts, but only 43-46% identity among mammalian counterparts. The characteristic Cys-Cys-Gly motif and four Cys residues in the large extracellular loop were conserved. The channel catfish CD63 transcript was detected by RT-PCR in spleen, anterior kidney, liver, intestine, skin and gill. This result provides important information for further elucidating CD63 functions in channel catfish.