pyochelin and pyoverdin

pyochelin has been researched along with pyoverdin* in 39 studies

Reviews

1 review(s) available for pyochelin and pyoverdin

ArticleYear
Metal complexes with valuable biomolecules produced by
    Dalton transactions (Cambridge, England : 2003), 2023, Apr-04, Volume: 52, Issue:14

    Topics: Coordination Complexes; Pseudomonas aeruginosa; Pyocyanine

2023

Other Studies

38 other study(ies) available for pyochelin and pyoverdin

ArticleYear
Iron removal from raw asbestos by siderophores-producing Pseudomonas.
    Journal of hazardous materials, 2020, 03-05, Volume: 385

    Asbestos, mineral present in soil, are highly toxic due to the presence of iron. Microbes-mineral interactions occur naturally through various processes leading to their alteration. We examined the effect of siderophore-producing Pseudomonas with a particular focus on the role of pyoverdine and pyochelin on raw asbestos fibers such as amosite, crocidolite and chrysotile. We compared the efficiency of pyoverdine to the iron chelating agent EDTA in the release of iron from raw asbestos fibers. Pyoverdine was able to extract iron from all the tested raw asbestos with the higher efficiency observed for chrysotile and crocidolite. When asbestos were grinded, the iron removal was more important for all types. We monitored the effect of bacterial growth and siderophores containing bacterial supernatant on raw asbestos dissolution by solution chemistry analysis and transmission electron microscopy. The siderophore-containing supernatant allowed a higher iron solubilisation than the one obtained after bacterial growth. Moreover, the iron dissolution was faster with pyoverdine-containing supernatant than pyochelin-containing supernatant, with approximately the same iron level for the maximum extraction with a delay of 48 h. Our study clearly showed the involvement of bacterial siderophores, pyoverdine and pyochelin on chrysotile, crocidolite and amosite fibers weathering.

    Topics: Asbestos, Amosite; Asbestos, Crocidolite; Asbestos, Serpentine; Biofilms; Edetic Acid; Iron; Oligopeptides; Phenols; Pseudomonas; Siderophores; Thiazoles

2020
Surface sensing triggers a broad-spectrum antimicrobial response in Pseudomonas aeruginosa.
    Environmental microbiology, 2020, Volume: 22, Issue:8

    Interspecies bacterial competition may occur via cell-associated or secreted determinants and is key to successful niche colonization. We previously evolved Pseudomonas aeruginosa in the presence of Staphylococcus aureus and identified mutations in the Wsp surface-sensing signalling system. Surprisingly, a ΔwspF mutant, characterized by increased c-di-GMP levels and biofilm formation capacity, showed potent killing activity towards S. aureus in its culture supernatant. Here, we used an unbiased metabolomic analysis of culture supernatants to identify rhamnolipids, alkyl quinoline N-oxides and two siderophores as members of four chemical clusters, which were more abundant in the ΔwspF mutant supernatants. Killing activities were quorum-sensing controlled but independent of c-di-GMP levels. Based on the metabolomic analysis, we formulated a synthetic cocktail of four compounds, showing broad-spectrum anti-bacterial killing, including both Gram-positive and Gram-negative bacteria. The combination of quorum-sensing-controlled killing and Wsp-system mediated biofilm formation endows P. aeruginosa with capacities essential for niche establishment and host colonization.

    Topics: Anti-Bacterial Agents; Antibiosis; Biofilms; Cyclic GMP; Glycolipids; Oligopeptides; Phenols; Pseudomonas aeruginosa; Quinolines; Quorum Sensing; Siderophores; Staphylococcus aureus; Thiazoles

2020
The pathogen
    Metallomics : integrated biometal science, 2020, 12-23, Volume: 12, Issue:12

    Siderophores are iron chelators produced by bacteria to access iron, an essential nutrient. The pathogen Pseudomonas aeruginosa produces two siderophores, pyoverdine and pyochelin, the former with a high affinity for iron and the latter with a lower affinity. Furthermore, the production of both siderophores involves a positive auto-regulatory loop: the presence of the ferri-siderophore complex is essential for their large production. Since pyochelin has a lower affinity for iron it was hard to consider the role of pyochelin in drastic competitive environments where the host or the environmental microbiota produce strong iron chelators and may inhibit iron chelation by pyochelin. We showed here that the pyochelin pathway overcomes this difficulty through a more complex regulating mechanism for pyochelin production than previously described. Indeed, in the absence of pyoverdine, and thus higher difficulty to access iron, the bacteria are able to produce pyochelin independently of the presence of ferri-pyochelin. The regulation of the pyochelin pathway appeared to be more complex than expected with a more intricate tuning between repression and activation. Consequently, when the bacteria cannot produce pyoverdine they are able to produce pyochelin even in the presence of strong iron chelators. Such results support a more complex and varied role for this siderophore than previously described, and complexify the battle for iron during P. aeruginosa infection.

    Topics: Humans; Iron; Oligopeptides; Phenols; Pseudomonas aeruginosa; Pseudomonas Infections; Siderophores; Thiazoles

2020
Non-specific interference of cobalt with siderophore-dependent iron uptake pathways.
    Metallomics : integrated biometal science, 2019, 11-01, Volume: 11, Issue:11

    Much data shows that biological metals other than Fe

    Topics: Bacterial Proteins; Cobalt; Down-Regulation; Gene Expression Regulation, Bacterial; Iron; Models, Biological; Oligopeptides; Operon; Phenols; Pseudomonas aeruginosa; Siderophores; Thiazoles; Up-Regulation

2019
Contribution of the Siderophores Pyoverdine and Enantio-Pyochelin to Fitness in Soil of Pseudomonas protegens Pf-5.
    Current microbiology, 2018, Volume: 75, Issue:12

    Pseudomonas protegens synthesizes two major iron-chelating metabolites (siderophores): pyoverdine (Pvd) and enantio-pyochelin (E-Pch). Although iron sequestration and uptake seem to be the main biological role of these siderophores, other functions including metal homeostasis and antibiotic activity have been proposed. The aim of this study was to evaluate the contribution of Pvd and E-Pch to the survival of P. protegens in soil using wild type and isogenic mutant strains unable to produce Pvd, E-Pch or both siderophores. Survival of these strains in sterile soil microcosms, in soil microcosms containing the native microflora and in sterile soil microcosms containing fusaric acid (a mycotoxin able to chelate iron and other metals), was compared by determination of colony forming units (CFU) per gram dry soil over time. In sterile soil, cell densities of Pvd-producing strains were significantly higher than that of non-producers after 21 days of permanence in the microcosms. In non-sterile soil, viability of all strains declined faster than in sterile soil and Pvd producers showed higher CFU × (g dry weight soil)

    Topics: Fusaric Acid; Iron; Oligopeptides; Phenols; Pseudomonas; Siderophores; Soil; Soil Microbiology; Thiazoles

2018
Environmental modification via a quorum sensing molecule influences the social landscape of siderophore production.
    Proceedings. Biological sciences, 2017, Apr-12, Volume: 284, Issue:1852

    Bacteria produce a wide variety of exoproducts that favourably modify their environment and increase their fitness. These are often termed 'public goods' because they are costly for individuals to produce and can be exploited by non-producers (cheats). The outcome of conflict over public goods is dependent upon the prevailing environment and the phenotype of the individuals in competition. Many bacterial species use quorum sensing (QS) signalling molecules to regulate the production of public goods. QS, therefore, determines the cooperative phenotype of individuals, and influences conflict over public goods. In addition to their regulatory functions, many QS molecules have additional properties that directly modify the prevailing environment. This leads to the possibility that QS molecules could influence conflict over public goods indirectly through non-signalling effects, and the impact of this on social competition has not previously been explored. The

    Topics: Genetic Fitness; Iron; Oligopeptides; Phenols; Pseudomonas aeruginosa; Quorum Sensing; Thiazoles

2017
Metallome of Pseudomonas aeruginosa: a role for siderophores.
    Environmental microbiology, 2016, Volume: 18, Issue:10

    In this paper, we describe the total metal composition (metallome) of Pseudomonas aeruginosa. Inductively coupled plasma atomic emission spectroscopy analyses showed that P. aeruginosa cells concentrate each metal of the metallome from the extracellular media with different efficiencies. Growth in nutrient-restricted media did not substantially affect the overall profile of the metallome; however, the uptake of some metals was strongly stimulated, showing the high potential of some metal acquisition pathways to adapt to changing growth conditions. We also investigated the role of the two major siderophores produced by P. aeruginosa, pyoverdine and pyochelin, in iron uptake and more generally in metallome homeostasis. In addition to their role in iron acquisition, siderophore production also significantly prevented the accumulation of toxic metals in P. aeruginosa cells, thus preserving the equilibrium of the metallome in a polluted environment.

    Topics: Biological Transport, Active; Metals; Oligopeptides; Phenols; Pseudomonas aeruginosa; Siderophores; Spectrophotometry, Atomic; Thiazoles

2016
The HigB/HigA toxin/antitoxin system of Pseudomonas aeruginosa influences the virulence factors pyochelin, pyocyanin, and biofilm formation.
    MicrobiologyOpen, 2016, Volume: 5, Issue:3

    Toxin/antitoxin (TA) systems are prevalent in most bacterial and archaeal genomes, and one of the emerging physiological roles of TA systems is to help regulate pathogenicity. Although TA systems have been studied in several model organisms, few studies have investigated the role of TA systems in pseudomonads. Here, we demonstrate that the previously uncharacterized proteins HigB (unannotated) and HigA (PA4674) of Pseudomonas aeruginosa PA14 form a type II TA system in which antitoxin HigA masks the RNase activity of toxin HigB through direct binding. Furthermore, toxin HigB reduces production of the virulence factors pyochelin, pyocyanin, swarming, and biofilm formation; hence, this system affects the pathogencity of this strain in a manner that has not been demonstrated previously for TA systems.

    Topics: Amino Acid Sequence; Bacterial Proteins; Bacterial Toxins; Biofilms; Cloning, Molecular; Escherichia coli; Oligopeptides; Phenols; Pseudomonas aeruginosa; Pyocyanine; Thiazoles; Virulence Factors

2016
The ferrichrome receptor A as a new target for Pseudomonas aeruginosa virulence attenuation.
    FEMS microbiology letters, 2016, Volume: 363, Issue:11

    Pseudomonas aeruginosa is an opportunistic pathogen, known to develop robust biofilms. Its biofilm development increases when antibiotics are presented at subminimal inhibitory concentrations (MICs) for reasons that remain unclear. In order to identify genes that affect biofilm development under such a sublethal antibiotic stress condition, we screened a transposon (Tn) mutant library of PAO1, a prototype P. aeruginosa strain. Among ∼5000 mutants, a fiuA gene mutant was verified to form very defective biofilms in the presence of sub-MIC carbenicillin. The fiuA gene encodes ferrichrome receptor A, involved in the iron acquisition process. Of note, biofilm formation was not decreased in the ΔpchΔpvd mutant defective in the production of pyochelin and pyoverdine, two well-characterized P. aeruginosa siderophore molecules. Moreover, ΔfiuA, a non-polar fiuA deletion mutant, produced a significantly decreased level of elastase, a major virulence determinant. Mouse airway infection experiments revealed that the mutant expressed significantly less pathogenicity. Our results suggest that the fiuA gene has pleiotropic functions that affect P. aeruginosa biofilm development and virulence. The targeting of FiuA could enable the attenuation of P. aeruginosa virulence and may be suitable for the development of a drug that specifically controls the virulence of this important pathogen.

    Topics: Animals; Bacterial Outer Membrane Proteins; Biofilms; Carbenicillin; DNA Transposable Elements; Ferrichrome; Gene Library; Iron; Lung; Mice; Microbial Sensitivity Tests; Oligopeptides; Pancreatic Elastase; Phenols; Pseudomonas aeruginosa; Sequence Deletion; Thiazoles; Virulence Factors

2016
Role of secondary metabolites in the interaction between Pseudomonas fluorescens and soil microorganisms under iron-limited conditions.
    FEMS microbiology ecology, 2016, Volume: 92, Issue:8

    Microorganisms can be versatile in their interactions with each other, being variously beneficial, neutral or antagonistic in their effect. Although this versatility has been observed among many microorganisms and in many environments, little is known regarding the mechanisms leading to these changes in behavior. In the present work, we analyzed the mechanism by which the soil bacterium Pseudomonas fluorescens BBc6R8 shifts from stimulating the growth of the ectomycorrhizal fungus Laccaria bicolor S238N to killing the fungus. We show that among the three secondary metabolites produced by the bacterial strain-the siderophores enantio-pyochelin and pyoverdine, and the biosurfactant viscosin-the siderophores are mainly responsible for the antagonistic activity of the bacterium under iron-limited conditions. While the bacterial strain continues to produce beneficial factors, their effects are overridden by the action of their siderophores. This antagonistic activity of the strain P. fluorescens BBC6R8 in iron-depleted environments is not restricted to its influence on L. bicolor, since it was also seen to inhibit the growth of the actinomycete Streptomyces ambofaciens ATCC23877. We show that the strain P. fluorescens BBc6R8 uses different strategies to acquire iron, depending on certain biotic and abiotic factors.

    Topics: Iron; Mycorrhizae; Oligopeptides; Phenols; Pseudomonas fluorescens; Siderophores; Soil; Soil Microbiology; Streptomyces; Thiazoles

2016
Evolutionary dynamics of interlinked public goods traits: an experimental study of siderophore production in Pseudomonas aeruginosa.
    Journal of evolutionary biology, 2015, Volume: 28, Issue:1

    Public goods cooperation is common in microbes, and there is much interest in understanding how such traits evolve. Research in recent years has identified several important factors that shape the evolutionary dynamics of such systems, yet few studies have investigated scenarios involving interactions between multiple public goods. Here, we offer general predictions about the evolutionary trajectories of two public goods traits having positive, negative or neutral regulatory influence on one another's expression, and we report on a test of some of our predictions in the context of Pseudomonas aeruginosa's production of two interlinked iron-scavenging siderophores. First, we confirmed that both pyoverdine and pyochelin siderophores do operate as public goods under appropriate environmental conditions. We then tracked their production in lines experimentally evolved under different iron-limitation regimes known to favour different siderophore expression profiles. Under strong iron limitation, where pyoverdine represses pyochelin, we saw a decline in pyoverdine and a concomitant increase in pyochelin - consistent with expansion of pyoverdine-defective cheats derepressed for pyochelin. Under moderate iron limitation, pyochelin declined - again consistent with an expected cheat invasion scenario - but there was no concomitant shift in pyoverdine because cross-suppression between the traits is unidirectional only. Alternating exposure to strong and moderate iron limitation caused qualitatively similar though lesser shifts compared to the constant-environment regimes. Our results confirm that the regulatory interconnections between public goods traits can significantly modulate the course of evolution, yet also suggest how we can start to predict the impacts such complexities will have on phenotypic divergence and community stability.

    Topics: Biological Evolution; Iron; Mutation; Oligopeptides; Phenols; Pseudomonas aeruginosa; Siderophores; Thiazoles

2015
Candida albicans Inhibits Pseudomonas aeruginosa Virulence through Suppression of Pyochelin and Pyoverdine Biosynthesis.
    PLoS pathogens, 2015, Volume: 11, Issue:8

    Bacterial-fungal interactions have important physiologic and medical ramifications, but the mechanisms of these interactions are poorly understood. The gut is host to trillions of microorganisms, and bacterial-fungal interactions are likely to be important. Using a neutropenic mouse model of microbial gastrointestinal colonization and dissemination, we show that the fungus Candida albicans inhibits the virulence of the bacterium Pseudomonas aeruginosa by inhibiting P. aeruginosa pyochelin and pyoverdine gene expression, which plays a critical role in iron acquisition and virulence. Accordingly, deletion of both P. aeruginosa pyochelin and pyoverdine genes attenuates P. aeruginosa virulence. Heat-killed C. albicans has no effect on P. aeruginosa, whereas C. albicans secreted proteins directly suppress P. aeruginosa pyoverdine and pyochelin expression and inhibit P. aeruginosa virulence in mice. Interestingly, suppression or deletion of pyochelin and pyoverdine genes has no effect on P. aeruginosa's ability to colonize the GI tract but does decrease P. aeruginosa's cytotoxic effect on cultured colonocytes. Finally, oral iron supplementation restores P. aeruginosa virulence in P. aeruginosa and C. albicans colonized mice. Together, our findings provide insight into how a bacterial-fungal interaction can modulate bacterial virulence in the intestine. Previously described bacterial-fungal antagonistic interactions have focused on growth inhibition or colonization inhibition/modulation, yet here we describe a novel observation of fungal-inhibition of bacterial effectors critical for virulence but not important for colonization. These findings validate the use of a mammalian model system to explore the complexities of polymicrobial, polykingdom infections in order to identify new therapeutic targets for preventing microbial disease.

    Topics: Animals; Candida albicans; Farnesol; Female; Gastrointestinal Tract; Iron; Male; Mice; Mice, Inbred C3H; Oligopeptides; Phenols; Pseudomonas aeruginosa; Thiazoles; Virulence

2015
A novel siderophore system is essential for the growth of Pseudomonas aeruginosa in airway mucus.
    Scientific reports, 2015, Oct-08, Volume: 5

    Pseudomonas aeruginosa establishes airway infections in Cystic Fibrosis patients. Here, we investigate the molecular interactions between P. aeruginosa and airway mucus secretions (AMS) derived from the primary cultures of normal human tracheal epithelial (NHTE) cells. PAO1, a prototype strain of P. aeruginosa, was capable of proliferating during incubation with AMS, while all other tested bacterial species perished. A PAO1 mutant lacking PA4834 gene became susceptible to AMS treatment. The ΔPA4834 mutant was grown in AMS supplemented with 100 μM ferric iron, suggesting that the PA4834 gene product is involved in iron metabolism. Consistently, intracellular iron content was decreased in the mutant, but not in PAO1 after the AMS treatment. Importantly, a PAO1 mutant unable to produce both pyoverdine and pyochelin remained viable, suggesting that these two major siderophore molecules are dispensable for maintaining viability during incubation with AMS. The ΔPA4834 mutant was regrown in AMS amended with 100 μM nicotianamine, a phytosiderophore whose production is predicted to be mediated by the PA4836 gene. Infectivity of the ΔPA4834 mutant was also significantly compromised in vivo. Together, our results identify a genetic element encoding a novel iron acquisition system that plays a previously undiscovered role in P. aeruginosa airway infection.

    Topics: Animals; Azetidinecarboxylic Acid; Chlorides; Coculture Techniques; Epithelial Cells; Ferric Compounds; Gene Expression Regulation, Bacterial; Genes, Bacterial; Host-Pathogen Interactions; Humans; Iron; Male; Mice; Mice, Inbred C57BL; Microarray Analysis; Microbial Viability; Mucus; Mutation; Oligopeptides; Phenols; Primary Cell Culture; Pseudomonas aeruginosa; Pseudomonas Infections; Siderophores; Thiazoles; Trachea

2015
The Gac/Rsm and cyclic-di-GMP signalling networks coordinately regulate iron uptake in Pseudomonas aeruginosa.
    Environmental microbiology, 2014, Volume: 16, Issue:3

    Pseudomonas aeruginosa is a versatile bacterial pathogen capable of occupying diverse ecological niches. To cope with iron limitation, P. aeruginosa secretes two siderophores, pyoverdine and pyochelin, whose ability to deliver iron to the cell is crucial for biofilm formation and pathogenicity. In this study, we describe a link between iron uptake and the Gac/Rsm system, a conserved signal transducing pathway of P. aeruginosa that controls the production of extracellular products and virulence factors, as well as the switch from planktonic to biofilm lifestyle. We have observed that pyoverdine and pyochelin production in P. aeruginosa is strongly dependent on the activation state of the Gac/Rsm pathway, which controls siderophore regulatory and biosynthetic genes at the transcriptional level, in a manner that does not involve regulation of ferric uptake regulator (Fur) expression. Gac/Rsm-mediated regulation of iron uptake genes appears to be conserved in different P. aeruginosa strains. Further experiments led to propose that the Gac/Rsm system regulates siderophore production through modulation of the intracellular levels of the second messenger c-di-GMP, indicating that the c-di-GMP and the Gac/Rsm regulatory networks essential for biofilm formation can also coordinately control iron uptake in P. aeruginosa.

    Topics: Bacterial Proteins; Cyclic GMP; Gene Expression Regulation, Bacterial; Iron; Oligopeptides; Phenols; Pseudomonas aeruginosa; Repressor Proteins; RNA-Binding Proteins; Siderophores; Sigma Factor; Thiazoles; Virulence Factors

2014
Pyoverdine and pyochelin measurements.
    Methods in molecular biology (Clifton, N.J.), 2014, Volume: 1149

    Siderophores are small organic chelators (of molecular weight between 200 and 2,000 Da), having a very high affinity for iron (10(17)-10(43) M(-1)). They are synthesized by bacteria and secreted into their environment in order to get access to iron, an essential element for bacterial growth. Pyoverdine (also called fluorescins or pseudobactins) and pyochelin are the two major siderophores produced by Pseudomonas aeruginosa in iron-limited media. Methods to specifically detect and measure the amount of pyoverdine and pyochelin in a bacterial culture are provided here. These methods are based on the spectral properties of these two siderophores.

    Topics: Biochemistry; Chromatography, Thin Layer; Iron; Oligopeptides; Phenols; Pseudomonas aeruginosa; Siderophores; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thiazoles

2014
Monitoring iron uptake by siderophores.
    Methods in molecular biology (Clifton, N.J.), 2014, Volume: 1149

    Iron is an important element for almost all forms of life. In order to get access to this essential nutriment, Pseudomonads produce two major siderophores, pyoverdine PVD and pyochelin (PCH). Uptake of iron in bacterial cells can be monitored accurately using (55)Fe. Bacteria cells are incubated in the presence of either PVD or PCH loaded with (55)Fe. After incubation, extracellular iron ions are separated from those accumulated in the bacteria cells by either centrifugation or filtration on glass microfiber filters, for the PCH and PVD assays, respectively. (55)Fe contained in the harvested cells on the filter or in the cell pellet is counted in scintillation cocktail. The number of moles of (55)Fe transported can be determined using the specific activity of the radionuclide.

    Topics: Biochemistry; Iron; Oligopeptides; Phenols; Pseudomonas aeruginosa; Siderophores; Solutions; Thiazoles

2014
Pyochelin potentiates the inhibitory activity of gallium on Pseudomonas aeruginosa.
    Antimicrobial agents and chemotherapy, 2014, Volume: 58, Issue:9

    Gallium (Ga) is an iron mimetic that has successfully been repurposed for antibacterial chemotherapy. To improve the antibacterial potency of Ga on Pseudomonas aeruginosa, the effect of complexation with a variety of siderophores and synthetic chelators was tested. Ga complexed with the pyochelin siderophore (at a 1:2 ratio) was more efficient than Ga(NO3)3 in inhibiting P. aeruginosa growth, and its activity was dependent on increased Ga entrance into the cell through the pyochelin translocon.

    Topics: Anti-Bacterial Agents; Biological Transport; Citrates; Deferoxamine; Drug Combinations; Drug Synergism; Ferrichrome; Gallium; Oligopeptides; Phenols; Pseudomonas aeruginosa; Siderophores; Sodium Citrate; Thiazoles

2014
Switching between apparently redundant iron-uptake mechanisms benefits bacteria in changeable environments.
    Proceedings. Biological sciences, 2013, Aug-07, Volume: 280, Issue:1764

    Bacteria often possess multiple siderophore-based iron uptake systems for scavenging this vital resource from their environment. However, some siderophores seem redundant, because they have limited iron-binding efficiency and are seldom expressed under iron limitation. Here, we investigate the conundrum of why selection does not eliminate this apparent redundancy. We focus on Pseudomonas aeruginosa, a bacterium that can produce two siderophores-the highly efficient but metabolically expensive pyoverdine, and the inefficient but metabolically cheap pyochelin. We found that the bacteria possess molecular mechanisms to phenotypically switch from mainly producing pyoverdine under severe iron limitation to mainly producing pyochelin when iron is only moderately limited. We further show that strains exclusively producing pyochelin grew significantly better than strains exclusively producing pyoverdine under moderate iron limitation, whereas the inverse was seen under severe iron limitation. This suggests that pyochelin is not redundant, but that switching between siderophore strategies might be beneficial to trade off efficiencies versus costs of siderophores. Indeed, simulations parameterized from our data confirmed that strains retaining the capacity to switch between siderophores significantly outcompeted strains defective for one or the other siderophore under fluctuating iron availabilities. Finally, we discuss how siderophore switching can be viewed as a form of collective decision-making, whereby a coordinated shift in behaviour at the group level emerges as a result of positive and negative feedback loops operating among individuals at the local scale.

    Topics: Biological Availability; Biological Evolution; Computer Simulation; Environment; Feedback, Physiological; Iron; Mutation; Oligopeptides; Phenols; Pseudomonas aeruginosa; Siderophores; Thiazoles

2013
TonB-dependent outer-membrane proteins and siderophore utilization in Pseudomonas fluorescens Pf-5.
    Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2011, Volume: 24, Issue:2

    The soil bacterium Pseudomonas fluorescens Pf-5 produces two siderophores, a pyoverdine and enantio-pyochelin, and its proteome includes 45 TonB-dependent outer-membrane proteins, which commonly function in uptake of siderophores and other substrates from the environment. The 45 proteins share the conserved β-barrel and plug domains of TonB-dependent proteins but only 18 of them have an N-terminal signaling domain characteristic of TonB-dependent transducers (TBDTs), which participate in cell-surface signaling systems. Phylogenetic analyses of the 18 TBDTs and 27 TonB-dependent receptors (TBDRs), which lack the N-terminal signaling domain, suggest a complex evolutionary history including horizontal transfer among different microbial lineages. Putative functions were assigned to certain TBDRs and TBDTs in clades including well-characterized orthologs from other Pseudomonas spp. A mutant of Pf-5 with deletions in pyoverdine and enantio-pyochelin biosynthesis genes was constructed and characterized for iron-limited growth and utilization of a spectrum of siderophores. The mutant could utilize as iron sources a large number of pyoverdines with diverse structures as well as ferric citrate, heme, and the siderophores ferrichrome, ferrioxamine B, enterobactin, and aerobactin. The diversity and complexity of the TBDTs and TBDRs with roles in iron uptake clearly indicate the importance of iron in the fitness and survival of Pf-5 in the environment.

    Topics: Bacterial Outer Membrane Proteins; Oligopeptides; Phenols; Phylogeny; Polymerase Chain Reaction; Protein Structure, Secondary; Pseudomonas fluorescens; Siderophores; Thiazoles

2011
FvbA is required for vibriobactin utilization in Pseudomonas aeruginosa.
    Microbiology (Reading, England), 2011, Volume: 157, Issue:Pt 7

    Bacteria acquire iron through a highly specific mechanism involving iron-chelating molecules termed siderophores. The Gram-negative bacterium Pseudomonas aeruginosa can utilize siderophores produced by other micro-organisms to facilitate iron uptake. Here we show that a P. aeruginosa strain deficient in siderophore production can use the Vibrio cholerae siderophore vibriobactin as an iron source. In addition, we identified a P. aeruginosa gene, PA4156 (fvbA), encoding a protein highly homologous to the V. cholerae vibriobactin receptor (ViuA). A P. aeruginosa mutant in the two endogenous siderophores (pyoverdine and pyochelin) and in fvbA was unable to utilize vibriobactin as an iron source. Additionally, preliminary analyses revealed the involvement of vibriobactin, Fur protein and an IclR-type regulator, FvbR (PA4157), in fvbA regulation.

    Topics: Bacterial Outer Membrane Proteins; Bacterial Proteins; Catechols; Gene Expression Regulation, Bacterial; Genes, Bacterial; Iron; Oligopeptides; Oxazoles; Phenols; Polymerase Chain Reaction; Pseudomonas aeruginosa; Receptors, Cell Surface; Repressor Proteins; Siderophores; Thiazoles; Vibrio cholerae

2011
Pseudomonas siderophores in the sputum of patients with cystic fibrosis.
    Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2011, Volume: 24, Issue:6

    The lungs of patients with cystic fibrosis become chronically infected with the bacterium Pseudomonas aeruginosa, which heralds progressive lung damage and a decline in health. Iron is a crucial micronutrient for bacteria and its acquisition is a key factor in infection. P. aeruginosa can acquire this element by secreting pyoverdine and pyochelin, iron-chelating compounds (siderophores) that scavenge iron and deliver it to the bacteria. Siderophore-mediated iron uptake is generally considered a key factor in the ability of P. aeruginosa to cause infection. We have investigated the amounts of pyoverdine in 148 sputum samples from 36 cystic fibrosis patients (30 infected with P. aeruginosa and 6 as negative controls). Pyoverdine was present in 93 samples in concentrations between 0.30 and 51 μM (median 4.6 μM) and there was a strong association between the amount of pyoverdine and the number of P. aeruginosa present. However, pyoverdine was not present, or below the limits of detection (~0.3 μM), in 21 sputum samples that contained P. aeruginosa. Pyochelin was also absent, or below the limits of detection (~1 μM), in samples from P. aeruginosa-infected patients with little or no detectable pyoverdine. Our data show that pyoverdine is an important iron-scavenging molecule for P. aeruginosa in many cystic fibrosis patients, but other P. aeruginosa iron-uptake systems must be active in some patients to satisfy the bacterial need for iron.

    Topics: Adult; Cystic Fibrosis; Female; Humans; Iron; Male; Oligopeptides; Phenols; Pseudomonas aeruginosa; Pseudomonas Infections; Siderophores; Sputum; Thiazoles; Young Adult

2011
Siderophore production and utilization by milk spoilage Pseudomonas species.
    Journal of dairy science, 2010, Volume: 93, Issue:4

    Many bacteria respond to potentially growth-limiting availability of iron by producing low-molecular-weight iron chelators (siderophores). The aim of this work was to examine the siderophores synthesized and utilized by Pseudomonas spp. implicated in milk spoilage. Twenty isolates of Pseudomonas spp. previously shown to have significant milk spoilage potential were tested for the ability to produce siderophores. Of these, 14 produced pyoverdin and 2 of these also produced pyochelin; 1 produced only pyochelin; 1 produced only salicylate; 2 produced non-pyoverdin, hydroxamate-containing siderophore; and 2 produced chrome azurol sulfonate reactive material that was neither pyoverdin nor pyochelin. There was considerable diversity among the pyoverdins produced. All isolates were shown to utilize iron complexed with exogenous pyoverdin, but usage of particular exogenous pyoverdins differed among isolates. Interference with the iron-uptake systems of the Pseudomonas spp. may be a means by which food spoilage can be slowed, and the pyoverdin system would appear to be a potential target. However, given the diversity of pyoverdins produced and utilized, and the presence of other siderophores, successful interference with bacterial iron acquisition in this context may be challenging.

    Topics: Animals; Food Contamination; Food Microbiology; Food Preservation; Iron; Milk; Oligopeptides; Phenols; Pseudomonas; Siderophores; Thiazoles

2010
Multiple phenotypic alterations caused by a c-type cytochrome maturation ccmC gene mutation in Pseudomonas aeruginosa.
    Microbiology (Reading, England), 2008, Volume: 154, Issue:Pt 1

    In some Proteobacteria biogenesis of c-type cytochromes depends on the products of the ccmABCDEFG(H) genes, which encode inner-membrane proteins. Inactivation of some ccm genes, in particular ccmC, has an impact on other processes as well, including siderophore production and utilization. Non-polar insertions were generated in the Pseudomonas aeruginosa ccmA, ccmC, ccmE, ccmF and ccmH genes, and their impacts on different phenotypes were compared. Only in the case of the ccmC mutant was cytochrome c production totally abrogated. The ccmC mutant, and to a lesser extent the ccmF mutant, showed a range of other phenotypic changes. The production of the siderophore pyoverdine was very low and growth under the condition of iron limitation was severely restricted, but production of the second siderophore, pyochelin, was increased. Interestingly, other traits were also strongly affected by the ccmC mutation, including the production of pyocyanin, swarming and twitching motility, and rhamnolipid production. The production of N-acyl homoserine lactones or the Pseudomonas quinolone signal (PQS) was, however, not affected in the ccmC and ccmF mutants. The ccmC mutant was also found to accumulate porphyrins, and catalase production was undetectable, consistent with the increased sensitivity to hydrogen peroxide. Finally, reduction in the content of [Fe-S] clusters was evidenced in both ccmC and ccmF mutants. Wild-type phenotypes were restored by complementation with a ccmC gene from Pseudomonas fluorescens ATCC 17400. In conclusion, we have demonstrated that CcmC is a key determinant for cytochrome c biogenesis, pyoverdine maturation, and expression of some quorum sensing-regulated traits.

    Topics: Acyl-Butyrolactones; Bacterial Outer Membrane Proteins; Bacterial Proteins; Catalase; Cytochromes c; Genetic Complementation Test; Glycolipids; Locomotion; Membrane Proteins; Mutagenesis, Insertional; Mutation; Oligopeptides; Phenols; Porphyrins; Pseudomonas aeruginosa; Pyocyanine; Quinolones; Thiazoles

2008
Iron acquisition from Pseudomonas aeruginosa siderophores by human phagocytes: an additional mechanism of host defense through iron sequestration?
    Infection and immunity, 2000, Volume: 68, Issue:3

    Chelation of iron to iron-binding proteins is a strategy of host defense. Some pathogens counter this via the secretion of low-molecular-weight iron-chelating agents (siderophores). Human phagocytes possess a high-capacity mechanism for iron acquisition from low-molecular-weight iron chelates. Efficient acquisition and sequestration of iron bound to bacterial siderophores by host phagocytes could provide a secondary mechanism to limit microbial access to iron. In the present work we report that human neutrophils, macrophages, and myeloid cell lines can acquire iron from the two Pseudomonas aeruginosa siderophores. Analogous to iron acquisition from other low-molecular-weight chelates, iron acquisition from the siderophores is ATP independent, induced by multivalent cationic metals, and unaffected by inhibitors of endocytosis and pinocytosis. In vivo, this process could serve as an additional mechanism of host defense to limit iron availability to invading siderophore-producing microbes.

    Topics: HL-60 Cells; Humans; Iron; Metals; Oligopeptides; Phagocytes; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Thiazoles

2000
Requirement of the Pseudomonas aeruginosa tonB gene for high-affinity iron acquisition and infection.
    Infection and immunity, 2000, Volume: 68, Issue:8

    To investigate the contribution of the TonB protein to high-affinity iron acquisition in Pseudomonas aeruginosa, we constructed tonB-inactivated mutants from strain PAO1 and its derivative deficient in producing the siderophores pyoverdin and pyochelin. The tonB mutants could not grow in a free-iron-restricted medium prepared by apotransferrin addition, even though the medium was supplemented with each purified siderophore or with a heme source (hemoglobin or hemin). The tonB inactivation was shown to make P. aeruginosa unable to acquire iron from the transferrin with either siderophore. Introduction of a plasmid carrying the intact tonB gene restored growth of the tonB mutant of PAO1 in the free-iron-restricted medium without any supplements and restored growth of the tonB mutant of the siderophore-deficient derivative in the medium supplemented with pyoverdin, pyochelin, hemoglobin, or hemin. In addition, animal experiments showed that, in contrast to PAO1, the tonB mutant of PAO1 could not grow in vivo, such as in the muscles and lungs of immunosuppressed mice, and could not kill any of the animals. The in vivo growth ability and lethal virulence were also restored by introduction of the tonB-carrying plasmid in the tonB mutant. These results indicate clearly that the intact tonB gene-and, therefore, the TonB protein encoded by it-is essential for iron acquisition mediated by pyoverdin and pyochelin and via heme uptake in P. aeruginosa and suggest that the TonB-dependent iron acquisition may be essential for P. aeruginosa to infect the animal host.

    Topics: Animals; Bacterial Proteins; Biological Transport; Genes, Bacterial; Heme; Iron; Iron Chelating Agents; Male; Membrane Proteins; Mice; Mutagenesis; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Thiazoles

2000
Vanadium interferes with siderophore-mediated iron uptake in Pseudomonas aeruginosa.
    Microbiology (Reading, England), 2000, Volume: 146 ( Pt 10)

    Vanadium is a metal that under physiological conditions can exist in two oxidation states, V(IV) (vanadyl ion) and V(V) (vanadate ion). Here, it was demonstrated that both ions can form complexes with siderophores. Pseudomonas aeruginosa produces two siderophores under iron-limiting conditions, pyoverdine (PVD) and pyochelin (PCH). Vanadyl sulfate, at a concentration of 1-2 mM, strongly inhibited growth of P. aeruginosa PAO1, especially under conditions of severe iron limitation imposed by the presence of non-utilizable Fe(III) chelators. PVD-deficient mutants were more sensitive to vanadium than the wild-type, but addition of PVD did not stimulate their growth. Conversely, PCH-negative mutants were more resistant to vanadium than the wild-type strain. Both siderophores could bind and form complexes with vanadium after incubation with vanadyl sulfate (1:1, in the case of PVD; 2:1, in the case of PCH). Although only one complex with PVD, V(IV)-PVD, was found, both V(IV)- and V(V)-PCH were detected. V-PCH, but not V-PVD, caused strong growth reduction, resulting in a prolonged lag phase. Exposure of PAO1 cells to vanadium induced resistance to the superoxide-generating compound paraquat, and conversely, exposure to paraquat increased resistance to V(IV). Superoxide dismutase (SOD) activity of cells grown in the presence of V(IV) was augmented by a factor of two. Mutants deficient in the production of Fe-SOD (SodB) were particularly sensitive to vanadium, whilst sodA mutants deficient for Mn-SOD were only marginally affected. In conclusion, it is suggested that V-PCH catalyses a Fenton-type reaction whereby the toxic superoxide anion O(2)- is generated, and that vanadium compromises PVD utilization.

    Topics: Bacterial Proteins; Drug Resistance, Microbial; Herbicides; Humans; Iron; Iron Chelating Agents; Mass Spectrometry; Oligopeptides; Paraquat; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Superoxide Dismutase; Thiazoles; Vanadium

2000
The ferripyoverdine receptor FpvA of Pseudomonas aeruginosa PAO1 recognizes the ferripyoverdines of P. aeruginosa PAO1 and P. fluorescens ATCC 13525.
    FEMS microbiology letters, 1999, Jan-01, Volume: 170, Issue:1

    FpvA, the ferripyoverdine outer membrane receptor of Pseudomonas aeruginosa ATCC 15692 (PAO1 strain), is not specific to the pyoverdine produced by PAO1, but is also able to recognize the structurally different (ferri)pyoverdine of P. fluorescens ATCC 13525. The specificity of FpvA was assessed by iron uptake competitions using the wild-type strains P. aeruginosa ATCC 15692 and P. fluorescens ATCC 13525 and their respective ferripyoverdines, and by fpvA gene complementation of a FpvA-deficient mutant of P. aeruginosa ATCC 15692. The receptor mutant was able to utilize none of the two pyoverdines, while the same but fpvA-complemented mutant recovered simultaneously the ability to incorporate iron thanks to each of the two siderophores. The broad specificity of recognition of FpvA is viewed as an advantage for the strain in iron competition. Moreover, it allows an interesting approach for the understanding of the recognition mechanism between a (ferri)pyoverdine and its cognate outer membrane receptor.

    Topics: Bacterial Outer Membrane Proteins; Genetic Complementation Test; Iron; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Pseudomonas fluorescens; Siderophores; Thiazoles; Time Factors

1999
Fumarase C activity is elevated in response to iron deprivation and in mucoid, alginate-producing Pseudomonas aeruginosa: cloning and characterization of fumC and purification of native fumC.
    Journal of bacteriology, 1997, Volume: 179, Issue:5

    We report the discovery of fumC, encoding a fumarase, upstream of the sodA gene, encoding manganese superoxide dismutase, in Pseudomonas aeruginosa. The fumC open reading frame, which terminates 485 bp upstream of sodA, contains 1,374 bp that encode 458 amino acids. A second 444-bp open reading frame located between fumC and sodA, called orfX, showed no homology with any genes or proteins in database searches. A fumarase activity stain revealed that P. aeruginosa possesses at least two and possibly three fumarases. Total fumarase activity was at least approximately 1.6-fold greater in mucoid, alginate-producing bacteria than in nonmucoid bacteria and decreased 84 to 95% during the first 5 h of aerobic growth, followed by a rapid rise to maximum activity in stationary phase. Bacteria exposed to the iron chelator 2,2'-dipyridyl, but not ferric chloride, demonstrated an increase in fumarase activity. Mucoid bacteria produced approximately twofold-higher levels of the siderophores pyoverdin and pyochelin than nonmucoid bacteria. Northern blot analysis revealed a transcript that included fumC, orfX, and sodA, the amount of which was increased in response to iron deprivation. A P. aeruginosa fumC mutant produced only approximately 40% the alginate of wild-type bacteria. Interestingly, a sodA mutant possessed an alginate-stable phenotype, a trait that is typically unstable in vitro. These data suggest that mucoid bacteria either are in an iron-starved state relative to nonmucoid bacteria or simply require more iron for the process of alginate biosynthesis. In addition, the iron-regulated, tricarboxylic acid cycle enzyme fumarase C is essential for optimal alginate production by P. aeruginosa.

    Topics: Alginates; Amino Acid Sequence; Bacterial Proteins; Base Sequence; Cloning, Molecular; Enzyme Stability; Escherichia coli; Fumarate Hydratase; Gene Expression Regulation, Bacterial; Iron; Molecular Sequence Data; Mutagenesis; Oligopeptides; Phenols; Phenotype; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Superoxide Dismutase; Thiazoles; Transcription, Genetic

1997
Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities.
    Journal of bacteriology, 1996, Volume: 178, Issue:14

    Pseudomonas aeruginosa is considered a strict aerobe that possesses several enzymes important in the disposal of toxic oxygen reduction products including iron- and manganese-cofactored superoxide dismutase and catalase. At present, the nature of the regulation of these enzymes in P. aeruginosa Is not understood. To address these issues, we used two mutants called A4 and C6 which express altered Fur (named for ferric uptake regulation) proteins and constitutively produce the siderophores pyochelin and pyoverdin. Both mutants required a significant lag phase prior to log-phase aerobic growth, but this lag was not as apparent when the organisms were grown under microaerobic conditions. The addition of iron salts to mutant A4 and, to a greater extent, C6 cultures allowed for an increased growth rate under both conditions relative to that of bacteria without added iron. Increased manganese superoxide dismutase (Mn-SOD) and decreased catalase activities were also apparent in the mutants, although the second catalase, KatB, was detected in cell extracts of each fur mutant. Iron deprivation by the addition of the iron chelator 2,2'-dipyridyl to wild-type bacteria produced an increase in Mn-SOD activity and a decrease in total catalase activity, similar to the fur mutant phenotype. Purified wild-type Fur bound more avidly than mutant Fur to a PCR product containing two palindromic 19-bp "iron box" regions controlling expression of an operon containing the sodA gene that encodes Mn-SOD. All mutants were defective in both ferripyochelin- and ferripyoverdin-mediated iron uptake. Two mutants of strain PAO1, defective in pyoverdin but not pyochelin biosynthesis, produced increased Mn-SOD activity. Sensitivity to both the redox-cycling agent paraquat and hydrogen peroxide was greater in each mutant than in the wild-type strain. In summary, the results indicate that mutations in the P. aeruginosa fur locus affect aerobic growth and SOD and catalase activities in P. aeruginosa. We postulate that reduced siderophore-mediated iron uptake, especially that by pyoverdin, may be one possible mechanism contributing to such effect.

    Topics: Aerobiosis; Bacterial Proteins; Base Sequence; Catalase; Gene Expression Regulation, Bacterial; Iron; Isoenzymes; Molecular Sequence Data; Mutation; Oligopeptides; Phenols; Pigments, Biological; Protein Binding; Pseudomonas aeruginosa; Repressor Proteins; Siderophores; Superoxide Dismutase; Thiazoles

1996
Zinc affects siderophore-mediated high affinity iron uptake systems in the rhizosphere Pseudomonas aeruginosa 7NSK2.
    Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 1993,Summer, Volume: 6, Issue:2

    Zinc concentrations ranging between 0.1 and 1 mM only slightly reduced maximal growth of wild-type Pseudomonas aeruginosa 7NSK2 in iron-limiting casamino acid medium, but had a clear negative effect on the growth of mutant MPFM1 (pyoverdin negative) and especially mutant KMPCH (pyoverdin and pyochelin negative). Production of pyoverdin by wild-type strain 7NSK2 was significantly increased in the presence of 0.5 mM zinc and could not be repressed by iron even at a concentration of 100 microM. Siderophore detection via isoelectrofocusing revealed that mutant KMPCH did not produce any siderophores, while mutant MPFM1 overproduced a siderophore with an acidic isoelectric point, most likely pyochelin. Pyochelin production by MPFM1 was stimulated by the presence of zinc in a similar way as pyoverdin for the wild-type. Analysis of outer membrane proteins revealed that three iron regulated outer membrane proteins (IROMPs) (90, 85 and 75 kDa) were induced by iron deficiency in the wild-type, while mutants were found to have altered IROMP profiles. Zinc specifically enhanced the production of a 85 kDa IROMP in 7NSK2, a 75 kDa IROMP in MPFM1 and a 90 kDa IROMP in KMPCH.

    Topics: Bacterial Outer Membrane Proteins; Cell Membrane; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Iron; Isoelectric Focusing; Kinetics; Mutagenesis; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Thiazoles; Zinc

1993
Iron metabolism in Pseudomonas: salicylic acid, a siderophore of Pseudomonas fluorescens CHAO.
    BioFactors (Oxford, England), 1992, Volume: 4, Issue:1

    Under iron-starvation conditions of growth, Pseudomonas fluorescens CHA0, a soil isolate involved in phytopathogenic fungi antagonisms, produced, together with pyoverdine, a second iron-chelating compound which was purified and identified by spectroscopy, HPLC and 1H-NMR to be salicylic acid. Mutants unable to synthesize pyoverdine overproduced this compound by a factor of 9-14. The biosynthesis of salicylic acid was under iron control; it was fully inhibited by 5 microM added iron in the growth medium. In contrast, salicylic acid of either bacterial or commercial origin facilitated labeled iron incorporation in iron-starved cells. Based on these two relationships observed with bacterial iron metabolism it is concluded that salicylic acid has a siderophore function for this strain.

    Topics: Iron; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas fluorescens; Salicylates; Salicylic Acid; Siderophores; Thiazoles

1992
Siderophore-specific induction of iron uptake in Pseudomonas aeruginosa.
    Journal of general microbiology, 1992, Volume: 138, Issue:11

    Pseudomonas aeruginosa has two siderophore-based high-affinity iron-uptake systems utilizing pyoverdin and pyochelin. Using strain IA1, a mutant deficient in production of both siderophores, we have shown that addition of purified siderophore to the growth medium induces expression of specific iron-regulated outer-membrane proteins and increases 55Fe-siderophore transport. Addition of pyoverdin from the parent strain PAO1 or from a clinical strain 0:12 induced expression of an 85 kDa IROMP and increased the rate of 55Fe-pyoverdin transport. Transport rates for 55Fe-PAO1 pyoverdin increased from 1.27 to 3.57 pmol Fe min-1 per 10(9) cells. Addition of purified pyochelin induced expression of a 75 kDa IROMP accompanied with increased 55Fe-pyochelin uptake without affecting 55Fe-pyoverdin transport. 55Fe-pyochelin transport increased from 0.3 to 10.6 pmol min-1 per 10(9) cells. Addition of pyoverdin from the parent strain or a chromatographically distinct pyoverdin caused increased reactivity with an anti-85 kDa mAb in Western blotting, indicating that the same receptor is being induced. These results suggest that P. aeruginosa can respond specifically to the presence of siderophore and moreover that not only can the pyoverdin receptor transport its cognate ferri-pyoverdin but also different ferri-pyoverdins, albeit at a reduced rate.

    Topics: Bacterial Outer Membrane Proteins; Biological Transport; Ferric Compounds; Gene Expression Regulation, Bacterial; Iron; Mutation; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Receptors, Cell Surface; Siderophores; Thiazoles

1992
Metal regulation of siderophore synthesis in Pseudomonas aeruginosa and functional effects of siderophore-metal complexes.
    Applied and environmental microbiology, 1992, Volume: 58, Issue:9

    Pseudomonas aeruginosa synthesizes two siderophores, pyochelin and pyoverdin, characterized by widely different structures, physicochemical properties, and affinities for Fe(III). Titration experiments showed that pyochelin, which is endowed with a relatively low affinity for Fe(III), binds other transition metals, such as Cu(II), Co(II), Mo(VI), and Ni(II), with appreciable affinity. In line with these observations, Fe(III) and Co(II) at 10 microM or Mo(VI), Ni(II), and Cu(II) at 100 microM repressed pyochelin synthesis and reduced expression of iron-regulated outer membrane proteins of 75, 68, and 14 kDa. In contrast, pyoverdin synthesis and expression of the 80-kDa receptor protein were affected only by Fe(III). All of the metals tested, except Mo(VI), significantly promoted P. aeruginosa growth in metal-poor medium; Mo(VI), Ni(II), and Co(II) were more efficient as pyochelin complexes than the free metal ions and the siderophore. The observed correlation between the affinity of pyochelin for Fe(III), Co(II), and Mo(VI) and the functional effects of these metals indicates that pyochelin may play a role in their delivery to P. aeruginosa.

    Topics: Bacterial Outer Membrane Proteins; Iron Chelating Agents; Metals; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Spectrophotometry, Ultraviolet; Thiazoles; Titrimetry

1992
Siderophore synthesis by mucoid Pseudomonas aeruginosa strains isolated from cystic fibrosis patients.
    Canadian journal of microbiology, 1991, Volume: 37, Issue:8

    Nonmucoid Pseudomonas aeruginosa responds to iron deprivation by synthesizing the siderophores pyochelin and pyoverdine. When grown in iron-deficient medium, six mucoid P. aeruginosa strains isolated from cystic fibrosis patients synthesized copious amounts of the exopolysaccharide alginate. A procedure that eliminated the interference of alginate was developed so that siderophores could be extracted from the growth medium. All six isolates were then noted to produce both pyoverdine and pyochelin. This report thus confirms that mucoid P. aeruginosa, like its nonmucoid counterparts, elicits the siderophores commonly cited as those of the microbe.

    Topics: Cystic Fibrosis; Iron Chelating Agents; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Pseudomonas Infections; Siderophores; Thiazoles

1991
Role of pyocyanin in the acquisition of iron from transferrin.
    Infection and immunity, 1986, Volume: 52, Issue:1

    Pseudomonas aeruginosa produces a blue pigment called pyocyanin. In the presence of oxidizable substrates, bacteria reduce this pigment to a colorless product, leukopyocyanin. Pyocyanin can also be nonenzymatically reduced by NADH. Leukopyocyanin formed by cell- or NADH-mediated reduction nonenzymatically reduces oxygen or Fe(III). Pyocyanin-dependent iron reduction by whole bacterial cells was measured by the formation of the ferrous-ferrozine complex. In addition, leukopyocyanin reduced chelated Fe(III) including ferric iron in complex with transferrin, the serum iron-binding protein. High-pressure liquid chromatography was used to display the reductive removal of iron from transferrin and the accumulation of iron in the ferrous-ferrozine complex. Pyocyanin stimulated the accumulation of 55Fe from [55Fe]transferrin when it was added to bacteria incubated under low-oxygen conditions. Although bacteria grown in the presence of 100 microM FeCl3 reduced pyocyanin just as rapidly as iron-limited bacteria, these cells did not accumulate iron in the presence or absence of pyocyanin. Therefore, P. aeruginosa participates indiscriminantly in the reduction of pyocyanin, but soluble or available iron generated by the pyocyanin is taken up specifically by iron-limited bacteria.

    Topics: Culture Media; Ferric Compounds; Iron; Iron Chelating Agents; Oligopeptides; Oxidation-Reduction; Phenazines; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Pyocyanine; Siderophores; Thiazoles; Transferrin

1986
Siderophore-mediated iron acquisition from transferrin by Pseudomonas aeruginosa.
    Infection and immunity, 1986, Volume: 52, Issue:3

    Pseudomonas aeruginosa placed across a dialysis membrane from [55Fe]transferrin caused the mobilization of the iron from the transferrin side to the bacterial or dialysate side of the membrane. Although the bacteria were capable of obtaining iron from transferrin for growth, the siderophores of P. aeruginosa failed to convert iron bound to transferrin into dialyzable, low-molecular-weight chelates. The crucial factor produced by the bacteria which was not present when the siderophores were added alone was the acid produced from the glucose minimal medium. The siderophores mobilized considerable iron from transferrin when used in the dialysis assay at pH values between 5.0 and 6.0, values which were commonly found during incubation of bacteria in the assays. When the siderophores were tested individually, pyoverdin was more effective than pyochelin in mobilizing iron across dialysis membranes at pH values of 5.0 and 6.0, but neither had appreciable activity at pH 7.4. The amounts of iron mobilized from conalbumin were comparable to the amounts from transferrin, but there was negligible release from lactoferrin at the three pH values. When the two siderophores were combined, the level of iron mobilization was identical to that demonstrated by pyoverdin alone. When the dialysis membrane was removed and the bacteria were mixed with the siderophores and transferrin, pyoverdin was again more active than pyochelin in mediating iron transport. Although no pyochelin-mediated iron mobilization could be detected at pH 7.4, there was transport. Therefore, the bacteria appeared to be aiding the siderophores in iron mobilization from transferrin.

    Topics: Conalbumin; Hydrogen-Ion Concentration; Iron; Iron Chelating Agents; Lactoferrin; Mutation; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Thiazoles; Transferrin

1986
Iron transport and serum resistance in Pseudomonas aeruginosa.
    Antibiotics and chemotherapy, 1985, Volume: 36

    Topics: Biological Transport; Blood Bactericidal Activity; Humans; Iron; Iron Chelating Agents; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Pseudomonas Infections; Pyocyanine; Siderophores; Thiazoles; Transferrin

1985
Effects of siderophores on the growth of Pseudomonas aeruginosa in human serum and transferrin.
    Infection and immunity, 1985, Volume: 49, Issue:1

    A combination of the siderophores produced by Pseudomonas aeruginosa, pyochelin and pyoverdin, dramatically stimulates the growth of this bacterium in medium containing human transferrin. The amount of growth stimulation observed when each siderophore was added alone was only slightly less than the amount observed with the combination. Siderophore-defective mutants of strain PAO1 were isolated to test the effects of siderophore production on growth in transferrin and human serum. The pyoverdin-proficient (Pvd+), pyochelin-deficient (Pch-) strain (IA5) grows just as well as the parent (PAO1), which produces both siderophores. On the other hand, the Pvd- Pch+ strain (211-5) has severely retarded growth, similar to that demonstrated by a mutant lacking production of both siderophores (IA1), but has an accelerated log phase compared with strain IA1 at the later stages of the growth curve. However, the Pvd- Pch+ strain (211-5) had no observable advantage over the Pvd- Pch- strain, IA1, during incubation in human serum. The inability of P. aeruginosa strains to produce pyochelin in glucose-minimal medium may explain the poor growth of 211-5 in this medium and in human serum. The 211-5 strain grows much better than the IA1 strain in the medium that allows pyochelin synthesis, but it still does not grow as well as the Pvd+ Pch- strain (IA5). Therefore, pyoverdin appears to be the most important siderophore for growth in human serum.

    Topics: Blood Proteins; Culture Media; Humans; Iron; Iron Chelating Agents; Oligopeptides; Phenols; Pigments, Biological; Pseudomonas aeruginosa; Siderophores; Thiazoles; Transferrin

1985