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J. Biol. Chem., Vol. 276, Issue 21, 17823-17829, May 25, 2001

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Ponericins, New Antibacterial and Insecticidal Peptides from the Venom of the Ant Pachycondyla goeldii^*

Jérôme Orivel, Virginie Redeker^§¶, Jean-Pierre Le Caer^§, François Krier, Anne-Marie Revol-Junelles, Arlette Longeon^**, Alain Chaffotte, Alain Dejean^§§, and Jean Rossier^§

From the  Laboratoire d'Ethologie Expérimentale et Comparée, CNRS ESA 7025, Université Paris 13, avenue JB Clément, 93430 Villetaneuse, France, ^§ Laboratoire de Neurobiologie et Diversité Cellulaire, CNRS UMR 7637, Ecole Supérieure de Physique et de Chimie Industrielles de la Ville de Paris, 10 rue Vauquelin, 75005 Paris, France,  Laboratoire de Fermentations et de Bioconversions Industrielles, Ecole Nationale Supérieure d'Agronomie et des Industries Alimentaires, Institut National Polytechnique de Lorraine (ENSAIA-INPL), 2 avenue de la Forêt de Haye, BP 172, 54505 Vandoeuvre-les-Nancy, France, ^** Laboratoire de Chimie des Substances Naturelles, CNRS ESA 8041, Museum National d'Histoire Naturelle, 63 rue Buffon, 75005 Paris, France,  Unité de Biochimie Cellulaire, CNRS URA 1129, Institut Pasteur, 28 rue du Dr Roux, 75015 Paris, France, and ^§§ Laboratoire d'Ecologie Terrestre, CNRS UMR 5552, Université Toulouse III, 118 route de Narbonne, 31062 Toulouse Cedex, France

The antimicrobial, insecticidal, and hemolytic properties of peptides isolated from the venom of the predatory ant Pachycondyla goeldii, a member of the subfamily Ponerinae, were investigated. Fifteen novel peptides, named ponericins, exhibiting antibacterial and insecticidal properties were purified, and their amino acid sequences were characterized. According to their primary structure similarities, they can be classified into three families: ponericin G, W, and L. Ponericins share high sequence similarities with known peptides: ponericins G with cecropin-like peptides, ponericins W with gaegurins and melittin, and ponericins L with dermaseptins. Ten peptides were synthesized for further analysis. Their antimicrobial activities against Gram-positive and Gram-negative bacteria strains were analyzed together with their insecticidal activities against cricket larvae and their hemolytic activities. Interestingly, within each of the three families, several peptides present differences in their biological activities. The comparison of the structural features of ponericins with those of well-studied peptides suggests that the ponericins may adopt an amphipathic -helical structure in polar environments, such as cell membranes. In the venom, the estimated peptide concentrations appear to be compatible with an antibacterial activity in vivo. This suggests that in the ant colony, the peptides exhibit a defensive role against microbial pathogens arising from prey introduction and/or ingestion.

The amino acid sequences reported in this paper have been submitted to the Swiss Protein Database under Swiss-Prot accession numbers P82414 (Ponericin G1), P82415 (Ponericin G2), P82416 (Ponericin G3), P82417 (Ponericin G4), P82418 (Ponericin G5), P82419 (Ponericin G6), P82420 (Ponericin G7), P82421 (Ponericin L1), P82422 (Ponericin L2), P82423 (Ponericin W1), P82424 (Ponericin W2), P82425 (Ponericin W3), P82426 (Ponericin W4), P82427 (Ponericin W5), and P82428 (Ponericin W6).

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