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Originally published In Press as doi:10.1074/jbc.M210353200 on November 18, 2002

J. Biol. Chem., Vol. 278, Issue 5, 3030-3039, January 31, 2003
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Xenorhabdus nematophila (Enterobacteriacea) Secretes a Cation-selective Calcium-independent Porin Which Causes Vacuolation of the Rough Endoplasmic Reticulum and Cell Lysis*

Carlos RibeiroDagger §, Michel Vignes||, and Michel BrehélinDagger **

From the Departments of Dagger  Ecologie Microbienne des Insectes et Interactions Insecte-Pathogène (EMIP) Unité Mixte de Recherche 1133, Institut National de la Recherche Agronomique-Université de Montpellier II, Place Eugène Bataillon 34095 Montpellier, France and || Plasticité et Synapse Glutamatergique, Unité Mixte de Recherche 5102, Centre National de la Recherche Scientifique-Université de Montpellier II, Place Eugène Bataillon, 34095 Montpellier, France

Xenorhabdus nematophila and Photorhabdus luminescens are two related enterobacteriaceae studied for their use in biological control and for synthesis of original virulence factors and new kinds of antibiotics. X. nematophila broth growth exhibits different cytotoxic activities on insect (Spodoptera littoralis, lepidoptera) immunocytes (hemocytes). Here we report the purification of the flhDC-dependent cytotoxin, a 10,790-Da peptide we have called alpha -Xenorhabdolysin (alpha X). We show that plasma membrane of insect hemocytes and of mammal red blood cells is the first target of this toxin. Electrophysiological and pharmacological approaches indicate that the initial effect of alpha X on macrophage plasma membrane is an increase of monovalent cation permeability, sensitive to potassium channel blockers. As a consequence, several events can occur intracellularly, such as selective vacuolation of the endoplasmic reticulum, cell swelling, and cell death by colloid-osmotic lysis. These effects, inhibited by potassium channel blockers, are totally independent of Ca2+. However, the size of the pores created by alpha X on macrophage or red blood cell plasma membrane increases with toxin concentration, which leads to a rapid cell lysis.

* This work was supported by grants from INRA, CNRS, and Fondation pour la Recherche Médicale (France) and Instituto de Cooperacao Cientifica e Tecnologica Internacional (Portugal).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.

§ Funded by a grant PRAXIS XXI (BD/13935/97) (Portugal). Present address: Secção de Biologia Celular e Molecular, Universidade dos Açores, 9501-801 Ponta Delgada, Açores, Portugal.

Both authors contributed equally to this study.

** To whom correspondence should be addressed. Tel.: 33-4-67-14-46-72; Fax: 33-4-67-14-46-79; E-mail: brehelin@crit.univ-montp2.fr.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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