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Originally published In Press as doi:10.1074/jbc.M111099200 on January 15, 2002

J. Biol. Chem., Vol. 277, Issue 13, 11208-11216, March 29, 2002
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Cupiennin 1, a New Family of Highly Basic Antimicrobial Peptides in the Venom of the Spider Cupiennius salei (Ctenidae)*

Lucia Kuhn-NentwigDagger §, Jürg MüllerDagger , Johann Schaller, Alfred Walz||, Margitta Dathe**, and Wolfgang NentwigDagger

From the Dagger   Zoological Institute, University of Bern, Baltzerstrasse 6, CH-3012 Bern, Switzerland,  Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, CH-3012 Bern, Switzerland, || Theodor Kocher Institute, University of Bern, Freiestrasse 1, CH-3012 Bern, Switzerland, and ** Institute of Molecular Pharmacology, Campus Berlin-Buch, Robert Rössle-Strasse 10, D-13125 Berlin, Germany

A new family of antimicrobial peptides was isolated from the venom of Cupiennius salei. The peptides were purified to homogeneity, and the sequence of cupiennin 1a was determined by Edman degradation: GFGALFKFLAKKVAKTVAKQAAKQGAKYVVNKQME-NH2. The amino acid sequences of cupiennin 1b, c, and d were obtained by a combination of sequence analysis and mass spectrometric measurements of comparative tryptic peptide mapping. All peptides consist of 35 amino acid residues and are characterized by a more hydrophobic N-terminal chain region and a C terminus composed preferentially of polar and charged residues. The total charge of all cupiennins calculated under physiological conditions is +8, and their C terminus, formed by a glutamic acid residue, is amidated. Conformational studies of the peptides revealed a high helix forming potential. Antimicrobial assays on bacteria with cupiennin 1a, 1d, and synthesized cupiennins 1a* and 1d* showed minimal inhibitory concentrations for bacteria in the submicromolar range. Their lytic effect on human red blood cells was lower by a factor of 8 to 14 than the highly hemolytic melittin. Cupiennin 1a, 1b, 1d, 1a*, and 1d* showed pronounced insecticidal activity. The immediate biological effects and the structural properties of the isolated cupiennins indicate a membrane-destroying mode of action on prokaryotic as well as eukaryotic cells.

* This research was supported by the Swiss National Science Foundation (Grant 31-52238-97). These peptides have been patent-protected.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.

§ To whom correspondence should be addressed. Tel:+41-31-631-45-32; Fax:+41-31-631-48-88; E-mail: lucia.kuhn@zos.unibe.ch.

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