Xenorhabdus nematophila (Enterobacteriacea) Secretes a Cation-selective Calcium-independent Porin Which Causes Vacuolation of the Rough Endoplasmic Reticulum and Cell Lysis
| Autor: | Carlos Ribeiro, Michel Vignes, Michel Brehélin |
|---|---|
| Přispěvatelé: | Bruitparif, Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Plasticité cérébrale (PC), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Ecologie microbienne des insectes et interactions hôte-pathogène (EMIP), Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM) |
| Rok vydání: | 2003 |
| Předmět: |
0106 biological sciences
Hemocytes Lysis MESH: Xenorhabdus Endoplasmic Reticulum medicine.disease_cause 01 natural sciences Biochemistry Xenorhabdus Cytosol MESH: Cytosol Photorhabdus luminescens MESH: Animals Cells Cultured 0303 health sciences Cultured MESH: Spodoptera medicine.anatomical_structure MESH: Cell Survival MESH: Calcium Porin [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] Endoplasmic Reticulum Rough MESH: Cells Cultured medicine.drug Programmed cell death Cell Survival Cells MESH: Endoplasmic Reticulum Rough Bacterial Toxins Porins Spodoptera Biology MESH: Vacuoles 03 medical and health sciences Rough medicine Animals Calcium Vacuoles Molecular Biology 030304 developmental biology MESH: Porins Toxin Endoplasmic reticulum fungi Neurosciences MESH: Hemocytes Potassium channel blocker Cell Biology biology.organism_classification 010602 entomology Red blood cell MESH: Bacterial Toxins Neurons and Cognition |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (5), pp.3030-9. ⟨10.1074/jbc.M210353200⟩ Journal of Biological Chemistry 5 (278), 3030-9. (2003) |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.m210353200 |
| Popis: | International audience; 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 Ca(2+). 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|