The Lon protease is essential for full virulence in Pseudomonas aeruginosa.
Pseudomonas aeruginosa PAO1 lon mutants are supersusceptible to ciprofloxacin, and exhibit a defect in cell division and in virulence-related properties, such as swarming, twitching and biofilm formation, despite the fact that the Lon protease is not a traditional regulator. Here we set out to inves...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3492299?pdf=render |
| _version_ | 1828381382268682240 |
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| author | Elena B M Breidenstein Laure Janot Janine Strehmel Lucia Fernandez Patrick K Taylor Irena Kukavica-Ibrulj Shaan L Gellatly Roger C Levesque Joerg Overhage Robert E W Hancock |
| author_facet | Elena B M Breidenstein Laure Janot Janine Strehmel Lucia Fernandez Patrick K Taylor Irena Kukavica-Ibrulj Shaan L Gellatly Roger C Levesque Joerg Overhage Robert E W Hancock |
| author_sort | Elena B M Breidenstein |
| collection | DOAJ |
| description | Pseudomonas aeruginosa PAO1 lon mutants are supersusceptible to ciprofloxacin, and exhibit a defect in cell division and in virulence-related properties, such as swarming, twitching and biofilm formation, despite the fact that the Lon protease is not a traditional regulator. Here we set out to investigate the influence of a lon mutation in a series of infection models. It was demonstrated that the lon mutant had a defect in cytotoxicity towards epithelial cells, was less virulent in an amoeba model as well as a mouse acute lung infection model, and impacted on in vivo survival in a rat model of chronic infection. Using qRT-PCR it was demonstrated that the lon mutation led to a down-regulation of Type III secretion genes. The Lon protease also influenced motility and biofilm formation in a mucin-rich environment. Thus alterations in several virulence-related processes in vitro in a lon mutant were reflected by defective virulence in vivo. |
| first_indexed | 2024-12-10T04:14:41Z |
| format | Article |
| id | doaj.art-f069355e91584cdea25c83cadc7047d6 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-10T04:14:41Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-f069355e91584cdea25c83cadc7047d62022-12-22T02:02:38ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-01711e4912310.1371/journal.pone.0049123The Lon protease is essential for full virulence in Pseudomonas aeruginosa.Elena B M BreidensteinLaure JanotJanine StrehmelLucia FernandezPatrick K TaylorIrena Kukavica-IbruljShaan L GellatlyRoger C LevesqueJoerg OverhageRobert E W HancockPseudomonas aeruginosa PAO1 lon mutants are supersusceptible to ciprofloxacin, and exhibit a defect in cell division and in virulence-related properties, such as swarming, twitching and biofilm formation, despite the fact that the Lon protease is not a traditional regulator. Here we set out to investigate the influence of a lon mutation in a series of infection models. It was demonstrated that the lon mutant had a defect in cytotoxicity towards epithelial cells, was less virulent in an amoeba model as well as a mouse acute lung infection model, and impacted on in vivo survival in a rat model of chronic infection. Using qRT-PCR it was demonstrated that the lon mutation led to a down-regulation of Type III secretion genes. The Lon protease also influenced motility and biofilm formation in a mucin-rich environment. Thus alterations in several virulence-related processes in vitro in a lon mutant were reflected by defective virulence in vivo.http://europepmc.org/articles/PMC3492299?pdf=render |
| spellingShingle | Elena B M Breidenstein Laure Janot Janine Strehmel Lucia Fernandez Patrick K Taylor Irena Kukavica-Ibrulj Shaan L Gellatly Roger C Levesque Joerg Overhage Robert E W Hancock The Lon protease is essential for full virulence in Pseudomonas aeruginosa. PLoS ONE |
| title | The Lon protease is essential for full virulence in Pseudomonas aeruginosa. |
| title_full | The Lon protease is essential for full virulence in Pseudomonas aeruginosa. |
| title_fullStr | The Lon protease is essential for full virulence in Pseudomonas aeruginosa. |
| title_full_unstemmed | The Lon protease is essential for full virulence in Pseudomonas aeruginosa. |
| title_short | The Lon protease is essential for full virulence in Pseudomonas aeruginosa. |
| title_sort | lon protease is essential for full virulence in pseudomonas aeruginosa |
| url | http://europepmc.org/articles/PMC3492299?pdf=render |
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