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Originally published In Press as doi:10.1074/jbc.M109173200 on December 5, 2001

J. Biol. Chem., Vol. 277, Issue 7, 5030-5039, February 15, 2002
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Discovery and Characterization of Two Isoforms of Moronecidin, a Novel Antimicrobial Peptide from Hybrid Striped Bass*

Xavier LauthDagger , Hiroko ShikeDagger , Jane C. BurnsDagger §, Mark E. Westerman, Vaughn E. Ostland, James M. Carlberg, Jon C. Van Olst, Victor NizetDagger , Steven W. Taylor||, Chisato ShimizuDagger , and Philippe Bulet**

From the Dagger  Department of Pediatrics, University of California, San Diego School of Medicine, La Jolla, California 92093-0830,  Kent SeaTech Corp., San Diego, California 92121, || Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, La Jolla, California 92093-0204, and ** Institut de Biologie Moléculaire et Cellulaire, UPR 9022, CNRS, "Réponse Immunitaire et Développement chez les Insectes," 15 rue Rene Descartes, Strasbourg 67084, France

We isolated a novel 22-residue, C-terminally amidated antimicrobial peptide, moronecidin, from the skin and gill of hybrid striped bass. Two isoforms, differing by only one amino acid, are derived from each parental species, white bass (Morone chrysops) and striped bass (Morone saxatilis). Molecular masses (2543 and 2571 Da), amino acid sequences (FFHHIFRGIVHVGKTIH(K/R)LVTGT), cDNA, and genomic DNA sequences were determined for each isoform. A predicted 79-residue moronecidin prepropeptide consists of three domains: a signal peptide (22 amino acids), a mature peptide (22 amino acids), and a C-terminal prodomain (35 amino acids). The synthetic, amidated white bass moronecidin exhibited broad spectrum antimicrobial activity that was retained at high salt concentration. An alpha -helical structure was confirmed by circular dichroism spectroscopy. The moronecidin gene consists of three introns and four exons. Peptide sequence and gene organization were similar to pleurocidin, an antimicrobial peptide from winter flounder. A TATA box and several consensus-binding motifs for transcription factors were found in the region 5' to the transcriptional start site. Moronecidin gene expression was detected in gill, skin, intestine, spleen, anterior kidney, and blood cells by kinetic reverse transcription (RT)-PCR. Thus, moronecidin is a new alpha -helical, broad spectrum antimicrobial peptide isolated from the skin and gills of hybrid striped bass.

* This work was supported in part by the Advanced Technology Program from the Department of Commerce to Kent SeaTech Corp. and in part by CNRS and the University Louis Pasteur of Strasbourg. The Molecular Pathology Shared Resource (University of California San Diego Cancer Center) is funded in part by NCI, National Institutes of Health, Cancer Center Support Grant 5P0CA23100-16.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF332621 and AF385583 (moronecidin cDNA of white bass and striped bass, respectively) and AF394243 and AF394244 (moronecidin gene of white bass and striped bass, respectively).

§ To whom correspondence should be addressed: Dept. of Pediatrics, UCSD School of Medicine, 9500 Gilman Dr., La Jolla, CA 92093-0830. Tel.: 619-543-5326; Fax: 619-543-3546; E-mail: jcburns@ucsd.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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