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Ciprofloxacin binding to GyrA causes global changes in the proteome of Pseudomonas aeruginosa.

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Jedrey, Hannah 
Lilley, Kathryn S 


Ciprofloxacin is one of the most widely-used antibiotics, and has proven especially effective at controlling infections associated with the opportunistic human pathogen, Pseudomonas aeruginosa. In this work, we show that sub-inhibitory concentrations of ciprofloxacin induce discrete changes in the intracellular proteome. Central metabolism and cell envelope-associated functions are particularly affected. In spite of the low magnitude of the intracellular proteomic changes, we found that sub-lethal concentrations of ciprofloxacin had substantial effects on motility and exoprotein secretion. Crucially, the proteomic and phenotypic modulations that we observed were absolutely dependent upon the presence of wild-type GyrA; an isogenic strain of P. aeruginosa carrying a ciprofloxacin-insensitive form of GyrA (a T83→I mutant) did not display ciprofloxacin-dependent changes unless complemented with wild-type gyrA in trans. These results show that the diverse effects of sub-inhibitory ciprofloxacin on the cell are routed through its primary target in the cell, DNA gyrase.



Anti-Bacterial Agents, Bacterial Proteins, Ciprofloxacin, DNA Gyrase, Microbial Sensitivity Tests, Mutation, Proteome, Pseudomonas aeruginosa

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FEMS Microbiol Lett

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Oxford University Press (OUP)
BBSRC (BB/C500252/1)
Biotechnology and Biological Sciences Research Council (BB/M019411/1)
This work was supported by BBSRC grants BB/C500252/1 and BB/M019411/1.