scholarly journals Serratia Secondary Metabolite Prodigiosin Inhibits Pseudomonas aeruginosa Biofilm Development by Producing Reactive Oxygen Species that Damage Biological Molecules

2016 ◽  
Vol 7 ◽  
Author(s):  
Önder Kimyon ◽  
Theerthankar Das ◽  
Amaye I. Ibugo ◽  
Samuel K. Kutty ◽  
Kitty K. Ho ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Pseudomonas Aeruginosa ◽  
Secondary Metabolite ◽  
Reactive Oxygen ◽  
Biological Molecules ◽  
Oxygen Species ◽  
Biofilm Development

Scavenging of reactive oxygen species by tryptophan metabolites helps Pseudomonas aeruginosa escape neutrophil killing

2014 ◽  
Vol 73 ◽  
pp. 400-410 ◽  
Author(s):  
Charlotte Genestet ◽  
Audrey Le Gouellec ◽  
Hichem Chaker ◽  
Benoit Polack ◽  
Benoit Guery ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Pseudomonas Aeruginosa ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Tryptophan Metabolites

scholarly journals Evaluation of the interaction between polymyxin B and Pseudomonas aeruginosa biofilm and planktonic cells: reactive oxygen species induction and zeta potential

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Marlucy Rodrigues Lima ◽  
Gabriella Freitas Ferreira ◽  
Wallace Ribeiro Nunes Neto ◽  
Joveliane de Melo Monteiro ◽  
Áquila Rodrigues Costa Santos ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Pseudomonas Aeruginosa ◽  
Zeta Potential ◽  
Reactive Oxygen ◽  
Polymyxin B ◽  
Oxygen Species ◽  
Planktonic Cells

scholarly journals Antibiotic Korormicin A Kills Bacteria by Producing Reactive Oxygen Species

2019 ◽  
Vol 201 (11) ◽  
Author(s):  
Adam Maynard ◽  
Nicole L. Butler ◽  
Takeshi Ito ◽  
Adilson José da Silva ◽  
Masatoshi Murai ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Pseudomonas Aeruginosa ◽  
Vibrio Cholerae ◽  
Pathogenic Bacteria ◽  
Reactive Oxygen ◽  
Direct Result ◽  
Oxygen Species ◽  
Gram Negative ◽  
Content Type ◽  
Nadh:Quinone Oxidoreductase

ABSTRACT Korormicin is an antibiotic produced by some pseudoalteromonads which selectively kills Gram-negative bacteria that express the Na+-pumping NADH:quinone oxidoreductase (Na+-NQR.) We show that although korormicin is an inhibitor of Na+-NQR, the antibiotic action is not a direct result of inhibiting enzyme activity. Instead, perturbation of electron transfer inside the enzyme promotes a reaction between O2 and one or more redox cofactors in the enzyme (likely the flavin adenine dinucleotide [FAD] and 2Fe-2S center), leading to the production of reactive oxygen species (ROS). All Pseudoalteromonas contain the nqr operon in their genomes, including Pseudoalteromonas strain J010, which produces korormicin. We present activity data indicating that this strain expresses an active Na+-NQR and that this enzyme is not susceptible to korormicin inhibition. On the basis of our DNA sequence data, we show that the Na+-NQR of Pseudoalteromonas J010 carries an amino acid substitution (NqrB-G141A; Vibrio cholerae numbering) that in other Na+-NQRs confers resistance against korormicin. This is likely the reason that a functional Na+-NQR is able to exist in a bacterium that produces a compound that typically inhibits this enzyme and causes cell death. Korormicin is an effective antibiotic against such pathogens as Vibrio cholerae, Aliivibrio fischeri, and Pseudomonas aeruginosa but has no effect on Bacteroides fragilis and Bacteroides thetaiotaomicron, microorganisms that are important members of the human intestinal microflora. IMPORTANCE As multidrug antibiotic resistance in pathogenic bacteria continues to rise, there is a critical need for novel antimicrobial agents. An essential requirement for a useful antibiotic is that it selectively targets bacteria without significant effects on the eukaryotic hosts. Korormicin is an excellent candidate in this respect because it targets a unique respiratory enzyme found only in prokaryotes, the Na+-pumping NADH:quinone oxidoreductase (Na+-NQR). Korormicin is synthesized by some species of the marine bacterium Pseudoalteromonas and is a potent and specific inhibitor of Na+-NQR, an enzyme that is essential for the survival and proliferation of many Gram-negative human pathogens, including Vibrio cholerae and Pseudomonas aeruginosa, among others. Here, we identified how korormicin selectively kills these bacteria. The binding of korormicin to Na+-NQR promotes the formation of reactive oxygen species generated by the reaction of the FAD and the 2Fe-2S center cofactors with O2.

scholarly journals Conditional quorum-sensing induction of a cyanide-insensitive terminal oxidase stabilizes cooperating populations of Pseudomonas aeruginosa

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Huicong Yan ◽  
Kyle L. Asfahl ◽  
Na Li ◽  
Feng Sun ◽  
Junwei Xiao ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Pseudomonas Aeruginosa ◽  
Quorum Sensing ◽  
Hydrogen Cyanide ◽  
Reactive Oxygen ◽  
Regulatory System ◽  
Metabolic Cost ◽  
Opportunistic Pathogen ◽  
Terminal Oxidase ◽  
Oxygen Species

Abstract Pseudomonas aeruginosa, an opportunistic pathogen of humans, uses quorum sensing (QS) to regulate the production of extracellular products that can benefit all members of the population. P. aeruginosa can police QS-deficient cheaters by producing hydrogen cyanide, which is also QS regulated; however, the mechanism by which cooperators selectively protect themselves from the toxicity of cyanide remained unresolved. Here, we show that a cyanide-insensitive terminal oxidase encoded by cioAB provides resistance to cyanide, but only in QS-proficient strains. QS-deficient cheaters do not activate cioAB transcription. QS-mediated regulation of cioAB expression depends on production of both cyanide by cooperators (which is QS regulated) and reactive oxygen species (ROS) from cheaters (which is not QS regulated). This type of regulatory system allows cooperating populations to respond, via ROS, to the presence of cheaters, and might allow them to defer the substantial metabolic cost of policing until cheaters are present in the population.

scholarly journals The Pseudomonas aeruginosa Secretory Product Pyocyanin Inactivates α1 Protease Inhibitor: Implications for the Pathogenesis of Cystic Fibrosis Lung Disease

1999 ◽  
Vol 67 (3) ◽  
pp. 1207-1212 ◽  
Author(s):  
Bradley E. Britigan ◽  
Michelle A. Railsback ◽  
Charles D. Cox
Keyword(s):  
Reactive Oxygen Species ◽  
Cystic Fibrosis ◽  
Pseudomonas Aeruginosa ◽  
Lung Injury ◽  
Protease Inhibitor ◽  
Lung Disease ◽  
Reactive Oxygen ◽  
Airway Epithelial Cells ◽  
Secretory Product ◽  
Oxygen Species

ABSTRACT α1 Protease inhibitor (α1PI) modulates serine protease activity in the lung. Reactive oxygen species inactivate α1PI, and this process has been implicated in the pathogenesis of a variety of forms of lung injury. An imbalance of protease-antiprotease activity is also detected in the airways of patients with cystic fibrosis-associated lung disease who are infected withPseudomonas aeruginosa. P. aeruginosa secretes pyocyanin, which, through its ability to redox cycle, induces cells to generate reactive oxygen species. We tested the hypothesis that redox cycling of pyocyanin could lead to inactivation of α1PI. When α1PI was exposed to NADH and pyocyanin, a combination that results in superoxide production, α1PI lost its ability to form an inhibitory complex with both porcine pancreatic elastase (PPE) and trypsin. Similarly, addition of pyocyanin to cultures of human airway epithelial cells to which α1PI was also added resulted in a loss of the ability of α1PI to form a complex with PPE or trypsin. Neither superoxide dismutase, catalase, nor dimethylthiourea nor depletion of the media of O2 to prevent formation of reactive oxygen species blocked pyocyanin-mediated inactivation of α1PI. These data raise the possibility that a direct interaction between reduced pyocyanin and α1PI is involved in the process. Consistent with this possibility, pretreatment of α1PI with the reducing agent β-mercaptoethanol also inhibited binding of trypsin to α1PI. These data suggest that pyocyanin could contribute to lung injury in the P. aeruginosa-infected airway of cystic fibrosis patients by decreasing the ability of α1PI to control the local activity of serine proteases.

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