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Literature summary for 3.4.21.53 extracted from

  • Breidenstein, E.B.; Janot, L.; Strehmel, J.; Fernandez, L.; Taylor, P.K.; Kukavica-Ibrulj, I.; Gellatly, S.L.; Levesque, R.C.; Overhage, J.; Hancock, R.E.
    The Lon protease is essential for full virulence in Pseudomonas aeruginosa (2012), PLoS ONE, 7, e49123.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
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gene lon
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Synonyms

Synonyms Comment Organism
lon protease
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Pseudomonas aeruginosa

General Information

General Information Comment Organism
malfunction 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. The lon mutant has a defect in cytotoxicity towards epithelial cells, is less virulent in an amoeba model as well as a mouse acute lung infection model, and is impacted on in vivo survival in a rat model of chronic infection. The lon mutation leads to a downregulation of Type III secretion genes. The Lon protease also influenced motility and biofilm formation in a mucin-rich environment, defective virulence in vivo. Phenotype detailed overview Pseudomonas aeruginosa
physiological function the Lon protease is essential for full virulence in Pseudomonas aeruginosa. The Lon protease is not a traditional regulator Pseudomonas aeruginosa