Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality.
Pseudomonas entomophila is an entomopathogenic bacterium that infects and kills Drosophila. P. entomophila pathogenicity is linked to its ability to cause irreversible damages to the Drosophila gut, preventing epithelium renewal and repair. Here we report the identification of a novel pore-forming t...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-09-01
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| Series: | PLoS Pathogens |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21980286/pdf/?tool=EBI |
| _version_ | 1818400862099210240 |
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| author | Onya Opota Isabelle Vallet-Gély Renaud Vincentelli Christine Kellenberger Ioan Iacovache Manuel Rodrigo Gonzalez Alain Roussel Françoise-Gisou van der Goot Bruno Lemaitre |
| author_facet | Onya Opota Isabelle Vallet-Gély Renaud Vincentelli Christine Kellenberger Ioan Iacovache Manuel Rodrigo Gonzalez Alain Roussel Françoise-Gisou van der Goot Bruno Lemaitre |
| author_sort | Onya Opota |
| collection | DOAJ |
| description | Pseudomonas entomophila is an entomopathogenic bacterium that infects and kills Drosophila. P. entomophila pathogenicity is linked to its ability to cause irreversible damages to the Drosophila gut, preventing epithelium renewal and repair. Here we report the identification of a novel pore-forming toxin (PFT), Monalysin, which contributes to the virulence of P. entomophila against Drosophila. Our data show that Monalysin requires N-terminal cleavage to become fully active, forms oligomers in vitro, and induces pore-formation in artificial lipid membranes. The prediction of the secondary structure of the membrane-spanning domain indicates that Monalysin is a PFT of the ß-type. The expression of Monalysin is regulated by both the GacS/GacA two-component system and the Pvf regulator, two signaling systems that control P. entomophila pathogenicity. In addition, AprA, a metallo-protease secreted by P. entomophila, can induce the rapid cleavage of pro-Monalysin into its active form. Reduced cell death is observed upon infection with a mutant deficient in Monalysin production showing that Monalysin plays a role in P. entomophila ability to induce intestinal cell damages, which is consistent with its activity as a PFT. Our study together with the well-established action of Bacillus thuringiensis Cry toxins suggests that production of PFTs is a common strategy of entomopathogens to disrupt insect gut homeostasis. |
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| format | Article |
| id | doaj.art-38015d4decfb4c639a0ce5075303d43b |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-14T07:43:19Z |
| publishDate | 2011-09-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-38015d4decfb4c639a0ce5075303d43b2022-12-21T23:10:58ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742011-09-0179e100225910.1371/journal.ppat.1002259Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality.Onya OpotaIsabelle Vallet-GélyRenaud VincentelliChristine KellenbergerIoan IacovacheManuel Rodrigo GonzalezAlain RousselFrançoise-Gisou van der GootBruno LemaitrePseudomonas entomophila is an entomopathogenic bacterium that infects and kills Drosophila. P. entomophila pathogenicity is linked to its ability to cause irreversible damages to the Drosophila gut, preventing epithelium renewal and repair. Here we report the identification of a novel pore-forming toxin (PFT), Monalysin, which contributes to the virulence of P. entomophila against Drosophila. Our data show that Monalysin requires N-terminal cleavage to become fully active, forms oligomers in vitro, and induces pore-formation in artificial lipid membranes. The prediction of the secondary structure of the membrane-spanning domain indicates that Monalysin is a PFT of the ß-type. The expression of Monalysin is regulated by both the GacS/GacA two-component system and the Pvf regulator, two signaling systems that control P. entomophila pathogenicity. In addition, AprA, a metallo-protease secreted by P. entomophila, can induce the rapid cleavage of pro-Monalysin into its active form. Reduced cell death is observed upon infection with a mutant deficient in Monalysin production showing that Monalysin plays a role in P. entomophila ability to induce intestinal cell damages, which is consistent with its activity as a PFT. Our study together with the well-established action of Bacillus thuringiensis Cry toxins suggests that production of PFTs is a common strategy of entomopathogens to disrupt insect gut homeostasis.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21980286/pdf/?tool=EBI |
| spellingShingle | Onya Opota Isabelle Vallet-Gély Renaud Vincentelli Christine Kellenberger Ioan Iacovache Manuel Rodrigo Gonzalez Alain Roussel Françoise-Gisou van der Goot Bruno Lemaitre Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality. PLoS Pathogens |
| title | Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality. |
| title_full | Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality. |
| title_fullStr | Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality. |
| title_full_unstemmed | Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality. |
| title_short | Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality. |
| title_sort | monalysin a novel ss pore forming toxin from the drosophila pathogen pseudomonas entomophila contributes to host intestinal damage and lethality |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21980286/pdf/?tool=EBI |
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