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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: Sequence analysis, characterization and tissue distribution of channel catfish (Ictalurus punctatus Rafinesque, 1818) myeloperoxidase cDNA

Authors
item Yeh, Hung-Yueh
item Klesius, Phillip

Submitted to: Fish and Shellfish Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: December 28, 2009
Publication Date: January 4, 2010
Repository URL: http://hdl.handle.net/10113/44029
Citation: Yeh, H., Klesius, P.H. 2010. Sequence analysis, characterization and tissue distribution of channel catfish (Ictalurus punctatus Rafinesque, 1818) myeloperoxidase cDNA. Fish and Shellfish Immunology. 28:504-509.

Interpretive Summary: Myeloperoxidase in neutrophils plays a critical role in destruction of invading pathogens in the early stage of infection. In this communication, we cloned, sequenced, and characterized the channel catfish myeloperoxidase transcript. The complete nucleotide sequence of channel catfish myeloperoxidase cDNA had 3157 nucleotides, including an open reading frame, which appears to encode a putative peptide of 771 amino acid residues with a calculated molecular mass of 87.14 kDa. By comparison with the human counterpart, the channel catfish myeloperoxidase peptide can be divided into domains and has conservative features, including peroxidase catalytic sites, covalent linkage sites for the heme group and all cysteine residues. The channel catfish myeloperoxidase transcript was detected by RT-PCR in anterior kidneys. Reagent development and the role of this enzyme in Edwardsiella ictaluri infection are under way.

Technical Abstract: Myeloperoxidase (EC 1.11.1.7), a heme-containing lysosomal glycoprotein, is found predominantly in azurophilic granules of neutrophils. This enzyme upon activation catalyzes hydrogen peroxide in the presence of various halide ions to form hypohalous acids. Subsequently, these reagents are able to kill the invading microorganisms. In this study, we report the identification, characterization and expression analysis of the channel catfish myeloperoxidase transcript. The full-length nucleotide sequence of channel catfish myeloperoxidase cDNA had 3157 nucleotides, including an open reading frame, which appears to encode a putative peptide of 771 amino acid residues with a calculated molecular mass of 87.14 kDa. By comparison with the human counterpart, the channel catfish myeloperoxidase peptide can be divided into domains and has conservative features, including peroxidase catalytic sites, covalent linkage sites for the heme group and all cysteine residues. The channel catfish myeloperoxidase transcript was detected by RT-PCR in anterior kidneys, where the major leukocyte population is neutrophil precursors. Reagent development and the role of this enzyme in Edwardsiella ictaluri infection are under way.

Last Modified: 11/28/2014
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