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J. Biol. Chem., Vol. 279, Issue 15, 14853-14859, April 9, 2004

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Primary Structure and in Vitro Antibacterial Properties of the Drosophila melanogaster Attacin C Pro-domain^*

David Rabel, Maurice Charlet, Laurence Ehret-Sabatier, Lionel Cavicchioli, Mare Cudic¶, Laszlo Otvos, Jr.¶, and Philippe Bulet||

From the Institut de Biologie Moléculaire et Cellulaire, UPR9022, CNRS, 15 Rue René Descartes, 67084 Strasbourg Cedex, France and ^¶The Wistar Institute, Philadelphia, Pennsylvania 19104

In Drosophila melanogaster, seven distinct families of antimicrobial peptides with different structures and specificities are synthesized by the fat body and released into the hemolymph during the immune response. Using microscale high performance liquid chromatography, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, and Edman degradation, we have isolated and characterized from immune-challenged Drosophila two novel induced molecules, under the control of the Imd pathway, that correspond to post-translationally modified antimicrobial peptides or peptide fragments. The first molecule is a doubly glycosylated form of drosocin, an O-glycosylated peptide that kills Gram-negative organisms. The second molecule represents a truncated form of the pro-domain of the Drosophila attacin C carrying two post-translational modifications and has significant structural similarities to proline-rich antibacterial peptides including drosocin. We have synthesized this peptide and found that it is active against Gram-negative bacteria. Furthermore, this activity is potentiated when the peptide is used in combination with the Drosophila antimicrobial peptide cecropin A. The synergistic action observed between these two molecules suggests that the truncated post-translationally modified pro-domain of attacin C by itself may play an important role in the antimicrobial defense of Drosophila.

Received for publication, December 12, 2003 , and in revised form, January 23, 2004.

^* This work was partially supported by grants from CNRS, the University Louis Pasteur of Strasbourg, and the Région Alsace (financing of mass spectrometry equipment). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence reported in this paper has been submitted to the Swiss Protein Database and TrEMBL knowledge base under Swiss-Prot accession no. P36193 and Q95NH6 for drosocin and for maturated pro-domain of attacin C (MPAC), respectively.

Financed by a Ministère del'Education Nationale de la Recherche et de la Technologie fellowship.

^|| To whom correspondence should be addressed. Atheris Laboratories, Case Postale 314, CH-1233 Bernex, Geneva-Switzerland. Tel.: 41-0-228500585; Fax: 41-0-228500586; E-mail: philippe.bulet{at}atheris.ch .

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