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Originally published In Press as doi:10.1074/jbc.M200511200 on April 25, 2002

J. Biol. Chem., Vol. 277, Issue 26, 23627-23637, June 28, 2002
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Oxyopinins, Large Amphipathic Peptides Isolated from the Venom of the Wolf Spider Oxyopes kitabensis with Cytolytic Properties and Positive Insecticidal Cooperativity with Spider Neurotoxins*

Gerardo CorzoDagger §, Elba VillegasDagger , Froylan Gómez-Lagunas, Lourival D. Possani||, Olga S. BelokonevaDagger , and Terumi NakajimaDagger

From the Dagger  Suntory Institute for Bioorganic Research, Mishima-Gun, Shimamoto-Cho, Wakayamadai 1-1-1, Osaka 618-8503, Japan, the  Department of Physiology, School of Medicine, National Autonomous University of Mexico (UNAM), Cd. Universitaria, Mexico City 04510, Mexico, and the || Department of Molecular Recognition and Structural Biology, Institute of Biotechnology, Av. Universidad 2001, Cuernavaca, Morelos 62210, Mexico

Five amphipathic peptides with antimicrobial, hemolytic, and insecticidal activity were isolated from the crude venom of the wolf spider Oxyopes kitabensis. The peptides, named oxyopinins, are the largest linear cationic amphipathic peptides from the venom of a spider that have been chemically characterized at present. According to their primary structure Oxyopinin 1 is composed of 48 amino acid residues showing extended sequence similarity to the ant insecticidal peptide ponericinL2 and to the frog antimicrobial peptide dermaseptin. Oxyopinins 2a, 2b, 2c, and 2d have highly similar sequences. At least 27 out of 37 amino acid residues are conserved. They also show a segment of sequence similar to ponericinL2. Circular dichroism analyses showed that the secondary structure of the five peptides is essentially alpha -helical. Oxyopinins showed disrupting activities toward both biological membranes and artificial vesicles, particularly to those rich in phosphatidylcholine. Electrophysiological recordings performed on insect cells (Sf9) showed that the oxyopinins produce a drastic reduction of cell membrane resistance by opening non-selective ion channels. Additionally, a new paralytic neurotoxin named Oxytoxin 1 was purified from the same spider venom. It contains 69 amino acid residue cross-linked by five disulfide bridges. Application of mixtures containing oxyopinins and Oxytoxin 1 to insect larvae showed a potentiation phenomenon, by which an increase lethality effect is observed. These results suggest that the linear amphipathic peptides in spider venoms and neuropeptides cooperate to capture insects efficiently.

* This work was supported by a grant from the Research for the Future Program from the Japanese Society for the Promotion of Science and by Grant z-005 from the National Council of Science and Technology (to F. G. L. and L. D. P.).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 amino acid sequences reported in this paper has been submitted to the Swiss Protein Database under Swiss-Prot accession no. P83247 for Oxyopinin 1 (Oxki1), P83248 for Oxyopinin 2a (Oxki2a), P83249 for Oxyopinin 2b (Oxki2b), P83250 for Oxyopinin 2c (Oxki2c), P83251 for Oxyopinin 2d (Oxki2d), and P83288 for Oxytoxin 1 (OxyTx1).

§ To whom correspondence should be addressed. Tel.: 81-75-962-8792; Fax: 81-75-962-2115; E-mail: corzo@sunbor.or.jp.

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