Journal articles: 'Pyoverdine Pseudomonas fluorescen'

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Meyer, Jean-Marie, Valérie A. Geoffroy, Nader Baida, Louis Gardan, Daniel Izard, Philippe Lemanceau, Wafa Achouak, and Norberto J. Palleroni. "Siderophore Typing, a Powerful Tool for the Identification of Fluorescent and Nonfluorescent Pseudomonads." Applied and Environmental Microbiology 68, no. 6 (June 2002): 2745–53. http://dx.doi.org/10.1128/aem.68.6.2745-2753.2002.

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ABSTRACT A total of 301 strains of fluorescent pseudomonads previously characterized by conventional phenotypic and/or genomic taxonomic methods were analyzed through siderotyping, i.e., by the isoelectrophoretic characterization of their main siderophores and pyoverdines and determination of the pyoverdine-mediated iron uptake specificity of the strains. As a general rule, strains within a well-circumscribed taxonomic group, namely the species Pseudomonas brassicacearum, Pseudomonas fuscovaginae, Pseudomonas jessenii, Pseudomonas mandelii, Pseudomonas monteilii, “Pseudomonas mosselii,” “Pseudomonas palleronii,” Pseudomonas rhodesiae, “Pseudomonas salomonii,” Pseudomonas syringae, Pseudomonas thivervalensis, Pseudomonas tolaasii, and Pseudomonas veronii and the genomospecies FP1, FP2, and FP3 produced an identical pyoverdine which, in addition, was characteristic of the group, since it was structurally different from the pyoverdines produced by the other groups. In contrast, 28 strains belonging to the notoriously heterogeneous Pseudomonas fluorescens species were characterized by great heterogeneity at the pyoverdine level. The study of 23 partially characterized phenotypic clusters demonstrated that siderotyping is very useful in suggesting correlations between clusters and well-defined species and in detecting misclassified individual strains, as verified by DNA-DNA hybridization. The usefulness of siderotyping as a determinative tool was extended to the nonfluorescent species Pseudomonas corrugata, Pseudomonas frederiksbergensis, Pseudomonas graminis, and Pseudomonas plecoglossicida, which were seen to have an identical species-specific siderophore system and thus were easily differentiated from one another. Thus, the fast, accurate, and easy-to-perform siderotyping method compares favorably with the usual phenotypic and genomic methods presently necessary for accurate identification of pseudomonads at the species level.

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Xiao, Rong, and William S. Kisaalita. "Fluorescent Pseudomonad Pyoverdines Bind and Oxidize Ferrous Ion." Applied and Environmental Microbiology 64, no. 4 (April 1, 1998): 1472–76. http://dx.doi.org/10.1128/aem.64.4.1472-1476.1998.

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ABSTRACT Major pyoverdines from Pseudomonas fluorescens 2-79 (Pf-B), P. aeruginosa ATCC 15692 (Pa-C), and P. putida ATCC 12633 (Pp-C) were examined by absorption and fluorescence spectroscopic techniques to investigate the interaction between ferrous ion and the pyoverdine ligand. At physiological pH, ferrous ion quenched the fluorescence of all three pyoverdines much faster than ferric ion did. Also, increased absorbance at 460 nm was observed to be much faster for Fe2+-pyoverdine than for Fe3+-pyoverdine. At pH 7.4, about 90% of Fe3+was bound by pyoverdine Pa-C after 24 h whereas Fe2+was bound by the pyoverdine completely in only 5 min. The possibility that Fe2+ underwent rapid autoxidation before being bound by pyoverdine was considered unlikely, since the Fe2+concentration in pyoverdine-free samples remained constant over a 3-min period at pH 7.4. Incubating excess Fe2+ with pyoverdine in the presence of 8-hydroxyquinoline, an Fe3+-specific chelating agent, resulted in the formation of a Fe3+-hydroxyquinoline complex, suggesting that the iron in the Fe2+-pyoverdine complex existed in the oxidized form. These results strongly suggested that pyoverdines bind and oxidize the ferrous ion.

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Bultreys, Alain, Isabelle Gheysen, Bernard Wathelet, Henri Maraite, and Edmond de Hoffmann. "High-Performance Liquid Chromatography Analyses of Pyoverdin Siderophores Differentiate among Phytopathogenic Fluorescent Pseudomonas Species." Applied and Environmental Microbiology 69, no. 2 (February 2003): 1143–53. http://dx.doi.org/10.1128/aem.69.2.1143-1153.2003.

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ABSTRACT The relationship of pyoverdins produced by 41 pathovars of Pseudomonas syringae and by phytopathogenic Pseudomonas species was investigated. A high-performance liquid chromatography method for analyzing the culture medium proved to be superior to isoelectric focusing for detecting pyoverdin production, for differentiating slightly different pyoverdins, and for differentiating atypical from typical Fe(III)-chelated pyoverdins. Nonfluorescent strains were found in Pseudomonas amygdali, Pseudomonas meliae, Pseudomonas fuscovaginae, and P. syringae. Pseudomonas agarici and Pseudomonas marginalis produced typical pyoverdins. Among the arginine dihydrolase-negative fluorescent Pseudomonas species, spectral, amino acid, and mass spectrometry analyses underscored for the first time the clear similarities among the pyoverdins produced by related species. Within this group, the oxidase-negative species Pseudomonas viridiflava and Pseudomonas ficuserectae and the pathovars of P. syringae produced the same atypical pyoverdin, whereas the oxidase-positive species Pseudomonas cichorii produced a similar atypical pyoverdin that contained a glycine instead of a serine. The more distantly related species Pseudomonas asplenii and Pseudomonas fuscovaginae both produced a less similar atypical pyoverdin. The spectral characteristics of Fe(III)-chelated atypical pyoverdins at pH 7.0 were related to the presence of two β-hydroxyaspartic acids as iron ligands, whereas in typical pyoverdins one of the ligands is always ornithine based. The peptide chain influenced the chelation of iron more in atypical pyoverdins. Our results demonstrated that there is relative pyoverdin conservation in the amino acids involved in iron chelation and that there is faster evolution of the other amino acids, highlighting the usefulness of pyoverdins in systematics and in identification.

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Shirley, Matt, Laure Avoscan, Eric Bernaud, Gérard Vansuyt, and Philippe Lemanceau. "Comparison of iron acquisition from Fe–pyoverdine by strategy I and strategy II plants." Botany 89, no. 10 (October 2011): 731–35. http://dx.doi.org/10.1139/b11-054.

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Iron is an essential micronutrient for plants and associated microorganisms. However, the bioavailability of iron in cultivated soils is low. Plants and microorganisms have thus evolved active strategies of iron uptake. Two different iron uptake strategies have been described in dicotyledonous and monocotyledonous graminaceous species. In bacteria, this strategy relies on the synthesis of siderophores. Pyoverdines, a major class of siderophores produced by fluorescent pseudomonads, were previously shown to promote iron nutrition of the dicotyledonous species Arabidopsis thaliana L. (Heynh.), whereas contradictory reports were made on the contribution of those siderophores to the nutrition of graminaceous annuals. Furthermore, no information has so far been available on graminaceous perennials. Here, the contribution of purified pyoverdine of Pseudomonas fluorescens C7R12 to the iron nutrition of two annual and perennial graminaceous plants was assessed and compared with that of two dicotyledonous plant species. Fe–Pyoverdine promoted the iron status of all plant species tested. With the exception of wheat, this promotion was more dramatic in graminaceous species than in dicotyledonous species and was the highest in fescue, a perennial species. The incorporation of 15N-labeled pyoverdine was consistent with the effect on the iron status of the plants tested.

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Meyer, Jean-Marie, Christelle Gruffaz, Topi Tulkki, and Daniel Izard. "Taxonomic heterogeneity, as shown by siderotyping, of strains primarily identified as Pseudomonas putida." International Journal of Systematic and Evolutionary Microbiology 57, no. 11 (November 1, 2007): 2543–56. http://dx.doi.org/10.1099/ijs.0.65233-0.

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One hundred and forty-four fluorescent pseudomonad strains isolated from various environments (soil, water, plant rhizosphere, hospital) and received as Pseudomonas putida (83 strains), P. putida biovar A (49 strains), P. putida biovar B (10 strains) and P. putida biovar C (2 strains), were analysed by the pyoverdine-isoelectrofocusing and pyoverdine-mediated iron uptake methods of siderotyping. Both methods demonstrated a great diversity among these strains, which could be subdivided into 35 siderovars. Some siderovars specifically included strains that have subsequently been transferred to well-defined Pseudomonas species, e.g. Pseudomonas monteilii or Pseudomonas mosselii, or which could be related by their siderotype to Pseudomonas jessenii or Pseudomonas mandelii. Other siderovars included strains sharing a high level of DNA-DNA relatedness (>70 %), thus demonstrating that siderotyping could easily circumscribe strains at the species level. However, a group of seven strains, including the type strain, P. putida ATCC 12633T, were allocated into four siderovars, despite sharing DNA–DNA relatedness values of higher than 70 %. Interestingly, the strong genomic relationships between these seven strains were supported by the structural relationships among their pyoverdines, thus reflecting their phylogenetic affinities. These results strongly support the view that pyoverdine-based siderotyping could be used as a powerful tool in Pseudomonas taxonomy.

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Mohn, G., K. Taraz, and H. Budzikiewicz. "New Pyoverdin-Type Siderophores from Pseudomonas fluorescens." Zeitschrift für Naturforschung B 45, no. 10 (October 1, 1990): 1437–50. http://dx.doi.org/10.1515/znb-1990-1014.

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The structures of two new pyoverdins (GM-I and GM-II) isolated from the culture medium of Pseudomonas fluorescens have been elucidated by spectroscopic methods and degradation studies. The pyoverdins consist of a chromophore which could be identified as (1 S)-5-amino-2,3-dihydro-8,9-dihydroxy-1 H-pyrimido[1,2-a]quinoline-1-carboxylic acid substituted at the amino group with a 3-carboxypropanoyl or a succinamoyl residue and at the carboxy group with the N-terminus of D-Ala-D-Lys-Gly-Gly-D-threo-(OH)Asp-D-Glu-D-Ser-L-Ala-D-Ala-D-Ala-L-Ala-L-N5-(OH)Orn.According to the “short-hand” nomenclature proposed in [2]*** the two compounds should be characterized as pyoverdin-Q-akGGd'qsAaaAO′*-SUCA and pyoverdin-Q-akGGd'qsAaaAO′ *-SUC

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Rehm, Karoline, Vera Vollenweider, Rolf Kümmerli, and Laurent Bigler. "A comprehensive method to elucidate pyoverdines produced by fluorescent Pseudomonas spp. by UHPLC-HR-MS/MS." Analytical and Bioanalytical Chemistry 414, no. 8 (January 27, 2022): 2671–85. http://dx.doi.org/10.1007/s00216-022-03907-w.

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AbstractMicrobial secondary metabolites represent a rich source for drug discovery, plant protective agents, and biotechnologically relevant compounds. Among them are siderophores, iron-chelating molecules, that show a great influence on bacterial community assembly and the potential to control pathogen invasions. One of such a siderophore is pyoverdine that is produced by fluorescent Pseudomonas members and consists of different peptide chains specific to each bacterial species. The identification and structural elucidation of such suites of siderophores remain widely underexplored as general high-throughput analytical protocols are missing. Therefore, a dedicated method was established allowing a rapid localization and structural elucidation of pyoverdines. Liquid bacterial culture samples were purified by an easy small-scale solid-phase extraction (SPE). Ultra-high-performance liquid chromatography high-resolution tandem mass spectrometry (UHPLC-HR-MS/MS) separated highly polar pyoverdines and their derivatives. All ion fragmentation (AIF) generated mass spectra containing the characteristic fragments of the biological precursor of pyoverdine, ferribactin. This led to the revelation of the mass of secreted pyoverdines. Targeted MS/MS experiments at multiple collision energies accomplished the full structure elucidation of the pyoverdine peptide chain. A mass calculator and a fragmentation predictor facilitated greatly the interpretation of MS/MS spectra by providing accurate masses for a straightforward comparison of measured and theoretical values. The method was successfully validated using four well-known pyoverdines with various peptide chains. Finally, the applicability was proven by the analysis of 13 unknown pyoverdines secreted by sampled bacterial cultures. Among these, 4 novel pyoverdine peptide chains were discovered and are herein reported for the first time. Graphical abstract

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Inoue, Hiroyuki, Osamu Takimura, Ken Kawaguchi, Teruhiko Nitoda, Hiroyuki Fuse, Katsuji Murakami, and Yukiho Yamaoka. "Tin-Carbon Cleavage of Organotin Compounds by Pyoverdine from Pseudomonas chlororaphis." Applied and Environmental Microbiology 69, no. 2 (February 2003): 878–83. http://dx.doi.org/10.1128/aem.69.2.878-883.2003.

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ABSTRACT The triphenyltin (TPT)-degrading bacterium Pseudomonas chlororaphis CNR15 produces extracellular yellow substances to degrade TPT. Three substances (F-I, F-IIa, and F-IIb) were purified, and their structural and catalytic properties were characterized. The primary structure of F-I was established using two-dimensional nuclear magnetic resonance techniques; the structure was identical to that of suc-pyoverdine from P. chlororaphis ATCC 9446, which is a peptide siderophore produced by fluorescent pseudomonads. Spectral and isoelectric-focusing analyses revealed that F-IIa and F-IIb were also pyoverdines, differing only in the acyl substituent attached to the chromophore part of F-I. Furthermore, we found that the fluorescent pseudomonads producing pyoverdines structurally different from F-I showed TPT degradation activity in the solid extracts of their culture supernatants. F-I and F-IIa degraded TPT to monophenyltin via diphenyltin (DPT) and degraded DPT and dibutyltin to monophenyltin and monobutyltin, respectively. The total amount of organotin metabolites produced by TPT degradation was nearly equivalent to that of the F-I added to the reaction mixture, whereas DPT degradation was not influenced by monophenyltin production. The TPT degradation activity of F-I was remarkably inhibited by the addition of metal ions chelated with pyoverdine. On the other hand, the activity of DPT was increased 13- and 8-fold by the addition of Cu2+ and Sn4+, respectively. These results suggest that metal-chelating ligands common to pyoverdines may play important roles in the Sn-C cleavage of organotin compounds in both the metal-free and metal-complexed states.

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Amann, Cordula, Kambiz Taraz, Herbert Budzikiewicz, and Jean-Marie Meyer. "The Siderophores of Pseudomonas fluorescens 18.1 and the Importance of Cyclopeptidic Substructures for the Recognition at the Cell Surface." Zeitschrift für Naturforschung C 55, no. 9-10 (October 1, 2000): 671–80. http://dx.doi.org/10.1515/znc-2000-9-1001.

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Abstract The structure of the pyoverdin siderophore of Pseudomonas fluorescens 18.1 was elucidated by spectroscopic methods and chemical degradation. By cross feeding studies structurally closely related pyoverdins containing a C-terminal cyclopeptidic substructure were tested regarding the mutual recognition by the producing strains. Partial recognition of foreign pyoverdins was observed.

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Calcott, Mark J., Jeremy G. Owen, Iain L. Lamont, and David F. Ackerley. "Biosynthesis of Novel Pyoverdines by Domain Substitution in a Nonribosomal Peptide Synthetase of Pseudomonas aeruginosa." Applied and Environmental Microbiology 80, no. 18 (July 11, 2014): 5723–31. http://dx.doi.org/10.1128/aem.01453-14.

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ABSTRACTPyoverdine is a fluorescent nonribosomal peptide siderophore made by fluorescent pseudomonads. ThePseudomonas aeruginosanonribosomal peptide synthetase (NRPS) PvdD contains two modules that each incorporate anl-threonine residue at the C-terminal end of pyoverdine. In an attempt to generate modified pyoverdine peptides, we substituted alternative-substrate-specifying adenylation (A) and peptide bond-catalyzing condensation (C) domains into the second module of PvdD. When just the A domain was substituted, the resulting strains produced only wild-type pyoverdine—at high levels if the introduced A domain specified threonine or at trace levels otherwise. The high levels of pyoverdine synthesis observed whenever the introduced A domain specified threonine indicated that these nonnative A domains were able to communicate effectively with the PvdD C domain. Moreover, the unexpected observation that non-threonine-specifying A domains nevertheless incorporated threonine into pyoverdine suggests that the native PvdD C domain exhibited stronger selectivity than these A domains for the incorporated amino acid substrate (i.e., misactivation of a threonine residue by the introduced A domains was more frequent than misincorporation of a nonthreonine residue by the PvdD C domain). In contrast, substitution of both the C and A domains of PvdD generated high yields of rationally modified pyoverdines in two instances, these pyoverdines having either a lysine or a serine residue in place of the terminal threonine. However, C-A domain substitution more commonly yielded a truncated peptide product, likely due to stalling of synthesis on a nonfunctional recombinant NRPS template.

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Georgias, Halka, Kambiz Taraz, Herbert Budzikiewicz, Valerie Geoffroy, and Jean-Marie Meyer. "The Structure of the Pyoverdin from Pseudomonas fluorescens 1.3. Structural and Biological Relationships of Pyoverdins from Different Strains." Zeitschrift für Naturforschung C 54, no. 5-6 (June 1, 1999): 301–8. http://dx.doi.org/10.1515/znc-1999-5-602.

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Abstract The structure of the pyoverdin siderophore of Pseudomonas fluorescens 1.3 was elucidated by spectroscopic methods and chemical degradation. It shows structural similarities with the pyoverdins of several other strains. Whether mutual recognition occurs was investigated by growth tests.

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Munsch, Patricia, Valerie A. Geoffroy, Tapani Alatossava, and Jean-Marie Meyer. "Application of Siderotyping for Characterization of Pseudomonas tolaasii and “Pseudomonas reactans” Isolates Associated with Brown Blotch Disease of Cultivated Mushrooms." Applied and Environmental Microbiology 66, no. 11 (November 1, 2000): 4834–41. http://dx.doi.org/10.1128/aem.66.11.4834-4841.2000.

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ABSTRACT Pyoverdine isoelectric focusing analysis and pyoverdine-mediated iron uptake were used as siderotyping methods to analyze a collection of 57 northern and central European isolates of P. tolaasiiand “P. reactans.” The bacteria, isolated from cultivated Agaricus bisporus or Pleurotus ostreatus mushroom sporophores presenting brown blotch disease symptoms, were identified according to the white line test (W. C. Wong and T. F. Preece, J. Appl. Bacteriol. 47:401–407, 1979) and their pathogenicity towards A. bisporus and were grouped into siderovars according to the type of pyoverdine they produced. Seventeen P. tolaasii isolates were recognized, which divided into two siderovars, with the first one containing reference strains and isolates of various geographical origins while the second one contained Finnish isolates exclusively. The 40 “P. reactans” isolates divided into eight siderovars. Pyoverdine isoelectric focusing profiles and cross-uptake studies demonstrated an identity for some “P. reactans” isolates, with reference strains belonging to theP. fluorescens biovars II, III, or V. Thus, the easy and rapid methods of siderotyping proved to be reliable by supporting and strengthening previous taxonomical data. Moreover, two potentially novel pyoverdines characterizing one P. tolaasiisiderovar and one “P. reactans” siderovar were found.

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Muratova, A. A., O. V. Evdokimova, M. N. Mandryk-Litvinkovich, L. N. Valentovich, and M. A. Titok. "MOLECULAR GENETIC AND FUNCTIONAL ANALYSIS OF GENES INFLUENCING PYOVERDINE SYNTHESIS IN PSEUDOMONAS BRASSICACEARUM S-1." Молекулярная и прикладная генетика 33 (November 12, 2022): 83–94. http://dx.doi.org/10.47612/1999-9127-2022-33-83-94.

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Molecular genetic and functional analysis allowed the identification and characterization of a number of new genetic determinants affecting the synthesis of pyoverdine by P. brassicacearum strain S-1. It was established that inactivation of genes encoding Zn-dependent peptidase (mtfA), peptidase of the C39 (GFU70_09550) family, transmembrane sensor protein (bvgS), heme transporter (ccmC), and protein with unknown function (ydgA) led to changes in fluorescence, efficacy of pyoverdine synthesis and antimicrobial activity in P. brassicacearum strain S-1. A previously undescribed genetic locus that determines the synthesis of pyoverdin was found in the chromosome of the studied bacteria. It was shown that the directed inactivation of this locus led to the complete absence of fluorescence and the production of pyoverdine by P. brassicacearum strain S-1, as well as to the loss of the ability to suppress the growth of the phytopathogenic strain Fusarium oxysporum BIM F-798.

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Taraz, K., R. Tappe, H. Schröder, U. Hohlneicher, I. Gwose, H. Budzikiewicz, G. Mohn, and J. F. Lefèvre. "Ferribactins -the Biogenetic Precursors of Pyoverdins." Zeitschrift für Naturforschung C 46, no. 7-8 (August 1, 1991): 527–33. http://dx.doi.org/10.1515/znc-1991-7-805.

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Abstract From ferribactins which accompany pyoverdins in iron deficient cultures of fluorescent pseudomonads a subunit has been obtained formed by condensation of D-tyrosin with L-2,4-diaminobutyric acid to give 2-(1-R-amino-2-p-hydroxyphenylethyl)-1,4,5,6-tetrahydropyrimidine-4-S′-carboxylic acid (1). Evidence is presented that 1 is the precur or of the typical pyoverdin chromophore 7 a.

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Fernández, Diana Uría, Regine Fuchs, Mathias Schäfer, Herbert Budzikiewicz, and Jean-Marie Meyer. "The Pyoverdin of Pseudomonas fluorescens G173, a Novel Structural Type Accompanied by Unexpected Natural Derivatives of the Corresponding Ferribactin." Zeitschrift für Naturforschung C 58, no. 1-2 (February 1, 2003): 1–10. http://dx.doi.org/10.1515/znc-2003-1-201.

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The siderophores produced by Pseudomonas fluorescens G173 are unusual in several respects. So far all pyoverdins with a C-terminal cyclopeptidic substructure have in common that the ε-amino group of an in-chain Lys is bound amidically to the carboxyl group of a C-terminal Ser or Thr and that N5-formyl-N5-hydroxy Orn (FoOHOrn) is the next amino acid after Lys. FoOHOrn may (cyclotetrapeptidic structures) be or may not (cyclotripeptidic structures) be followed by a further amino acid. In the pyoverdin described here Orn instead of Lys is the amino acid forming the cycle, FoOHOrn is replaced by AcOHOrn which does not follow the branching Orn but is the penultimate amino acid and finally the last amino acid is Asp. The producing strain which had been classified as Pseudomonas fluorescens may well be a new species. Pyoverdins are frequently accompanied by ferribactins which are considered to be their biogenetic precursors. They always have the same amino acid chain as the co-occurring pyoverdins but the pyoverdin chromophore is replaced by a condensation product of ʟ-Dab and ᴅ-Tyr with the amino group of Tyr bound to the γ-carboxyl group of Glu. A ferribactin having these structural characteristics is produced by the investigated strain, but it is accompanied by derivatives where the α-amino group of Glu is partially or completely transformed into a hydroxamic acid by substitution with a hydroxyl and/or acetyl group

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Bultreys, Alain, Isabelle Gheysen, Henri Maraite, and Edmond de Hoffmann. "Characterization of Fluorescent and Nonfluorescent Peptide Siderophores Produced by Pseudomonas syringaeStrains and Their Potential Use in Strain Identification." Applied and Environmental Microbiology 67, no. 4 (April 1, 2001): 1718–27. http://dx.doi.org/10.1128/aem.67.4.1718-1727.2001.

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ABSTRACT Nonfluorescent highly virulent strains of Pseudomonas syringae pv. aptata isolated in different European countries and in Uruguay produce a nonfluorescent peptide siderophore, the production of which is iron repressed and specific to these strains. The amino acid composition of this siderophore is identical to that of the dominant fluorescent peptide siderophore produced by fluorescentP. syringae strains, and the molecular masses of the respective Fe(III) chelates are 1,177 and 1,175 atomic mass units. The unchelated nonfluorescent siderophore is converted into the fluorescent siderophore at pH 10, and colors and spectral characteristics of the unchelated siderophores and of the Fe(III)-chelates in acidic conditions are similar to those of dihydropyoverdins and pyoverdins, respectively. The nonfluorescent siderophore is used by fluorescent and nonfluorescent P. syringae strains. These results and additional mass spectrometry data strongly suggest the presence of a pyoverdin chromophore in the fluorescent siderophore and a dihydropyoverdin chromophore in the nonfluorescent siderophore, which are both ligated to a succinamide residue. When chelated, the siderophores behave differently from typical pyoverdins and dihydropyoverdins in neutral and alkaline conditions, apparently because of the ionization occurring around pH 4.5 of carboxylic acids present in β-hydroxyaspartic acid residues of the peptide chains. These differences can be detected visually by pH-dependent changes of the chelate colors and spectrophotochemically. These characteristics and the electrophoretic behavior of the unchelated and chelated siderophores offer new tools to discriminate between saprophytic fluorescent Pseudomonas species and fluorescent P. syringae and P. viridiflava strains and to distinguish between the two siderovars in P. syringae pv. aptata.

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Jacques, Ph, M. Ongena, I. Gwose, D. Seinsche, H. Schröder, Ph Delfosse, Ph Thonart, K. Taraz, and H. Budzikiewicz. "Structure and Characterization of Isopyoverdin from Pseudomonas putida BTP1 and Its Relation to the Biogenetic Pathway Leading to Pyoverdins." Zeitschrift für Naturforschung C 50, no. 9-10 (October 1, 1995): 622–29. http://dx.doi.org/10.1515/znc-1995-9-1005.

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Abstract Pyoverdin type siderophores produced by six fluorescent Pseudomonas strains isolated from different rhizospheres were purified and characterized. The purified ferri-pyoverdins were tested for their ability to promote the growth of other strains grown under iron deficiency conditions. Only the one obtained from Pseudomonas putida BTP1 did not act as a growth promoter. The structure of the BTP1 siderophore was elucidated by spectroscopic methods and degradation studies. It turned out that it contains a chromophore which differs from the one typical for pyoverdins insofar as it carries the carboxyl group in 3- rather than in 1-position ((3S)-5-amino-1,2-dihydro-8,9-dihydroxy-3 H -pyrimido[1,2 a]quinoline-3-carboxylic acid). The amino group of the chromophore is substituted with the 5-carboxyl group of ʟ-glutamic acid and its carboxyl group with the N -terminus of the peptide ʟ -A sp -ʟ -A la-ʟ -Asp - ᴅ-N5- Ac - N5- OH - Orn - ʟ - Ser - ʟ - ᴄ - N5- OH - Orn . This isopyoverdin fits into the biogenetic scheme which postulates ferribactins as the precursors of pyoverdins

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Landa, Blanca B., Juana M. Cachinero-Díaz, Philippe Lemanceau, Rafael M. Jiménez-Díaz, and Claude Alabouvette. "Effect of fusaric acid and phytoanticipins on growth of rhizobacteria andFusarium oxysporum." Canadian Journal of Microbiology 48, no. 11 (November 1, 2002): 971–85. http://dx.doi.org/10.1139/w02-094.

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Suppression of soilborne diseases by biocontrol agents involves complex interactions among biocontrol agents and the pathogen and between these microorganisms and the plant. In general, these interactions are not well characterized. In this work, we studied (i) the diversity among strains of fluorescent Pseudomonas spp., Bacillus spp., and Paenibacillus sp. for their sensitivity to fusaric acid (FAc) and phytoanticipins from different host plants, (ii) the diversity of pathogenic and nonpathogenic Fusarium oxysporum isolates for their sensitivity to phytoanticipins, and (iii) the influence of FAc on the production of pyoverdine by fluorescent Pseudomonas spp. tolerant to this compound. There was a great diversity in the response of the bacterial strains to FAc; however, as a group, Bacillus spp. and Paenibacillus macerans were much more sensitive to FAc than Pseudomonas spp. FAc also affected production of pyoverdine by FAc-tolerant Pseudomonas spp. strains. Phytoanticipins differed in their effects on microbial growth, and sensitivity to a phytoanticipin varied among bacterial and fungal strains. Biochanin A did not affect growth of bacteria, but coumarin inhibited growth of Pseudomonas spp. strains and had no effect on Bacillus circulans and P. macerans. Conversely, tomatine inhibited growth of B. circulans and P. macerans. Biochanin A and tomatine inhibited growth of three pathogenic isolates of F. oxysporum but increased growth of three nonpathogenic F. oxysporum isolates. Coumarin inhibited growth of all pathogenic and nonpathogenic F. oxysporum isolates. These results are indicative of the complex interactions that can occur among plants, pathogens, and biological control agents in the rhizosphere and on the root surface. Also, these results may help to explain the low efficacy of some combinations of biocontrol agents, as well as the inconsistency in achieving disease suppression under field conditions.Key words: biocontrol, pyoverdines, fluorescent Pseudomonas spp., Bacillus spp., Paenibacillus spp., plantmicrobe interactions.

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Budzikiewicz, H., S. Kilz, K. Taraz, and J. M. Meyer. "Identical Pyoverdines from Pseudomonas fluorescens 9AW and from Pseudomonas putida 9BW." Zeitschrift für Naturforschung C 52, no. 11-12 (December 1, 1997): 721–28. http://dx.doi.org/10.1515/znc-1997-11-1202.

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Abstract Pseudomonas fluorescens, Pseudomonas putida, Pyoverdine, Siderophore, Bacterial Classification From Pseudom onas fluorescens 9AW and from Pseudomonas putida 9BW identical pyo-verdine-type siderophores were isolated and their structures were elucidated by spectroscopic methods and degradation studies. These novel compounds are of interest as they contain L-threo-β-hydroxy histidine in their peptide chains, an amino acid sofar encountered in nature only rarely. The co-occurence of the same pyoverdine in different Pseudom onas species and its significance for the classification is discussed.

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Schäfer, H., K. Taraz, and H. Budzikiewicz. "Zur Genese Der Amidisch An Den Chromophor Von Pyoverdinen Gebundenen Dicarbonsäuren [1]." Zeitschrift für Naturforschung C 46, no. 5-6 (June 1, 1991): 398–406. http://dx.doi.org/10.1515/znc-1991-5-611.

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Pseudomonas strains of the so-called fluorescent group usually produce several pyoverdins which differ only in the nature of a dicarboxylic acid bound amidically to the chromophor. For the pyoverdins isolated from the culture medium of Pseudomonas fluorescens 12 it is shown that succinic acid is an artefact formed by hydrolysis of succinic amide, and that a-ketoglutaric acid is transformed enzymatically to glutamic acid. This process is reversed after the phase of exponential growth of the bacteria. The ratio C4- vs. C5 -acids changes with the culture time and with increasing Fe3+ content of the medium in favor of the latter

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21

Liao, Ching-Hsing, Daniel E. McCallus, William F. Fett, and Yue-gyu Kang. "Identification of gene loci controlling pectate lyase production and soft-rot pathogenicity in Pseudomonas marginalis." Canadian Journal of Microbiology 43, no. 5 (May 1, 1997): 425–31. http://dx.doi.org/10.1139/m97-060.

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Pseudomonas marginalis is an important postharvest pathogen capable of causing soft rot in a wide variety of harvested fruits and vegetables. Following transposon mutagenesis, we isolated two groups of P. marginalis CY091 mutants deficient in production of pectate lyase (Pel) and soft-rot pathogenicity in plants. The first group, designated Pel−, was caused by the insertion of Tn5 into a pel structural gene, and the second group, designated LemA−, was caused by the insertion of Tn5 into a regulatory locus corresponding to the lemA gene previously identified in other Gram-negative bacteria. The LemA− mutants also exhibited alteration in colony morphology and showed deficiency in production of protease (Prt). A cosmid clone pCIC carrying the P. marginalis lemA gene was isolated and characterized. pCIC was capable of restoring Pel production and soft-rot pathogenicity in LemA− mutants of P. marginalis and Pseudomonas viridiflava, indicating that the function of lemA gene in these two pseudomonads was similar and interchangeable. Using MudI-mediated mutagenesis, we isolated a third group of P. marginalis mutants deficient in production of Pel, Prt, and soft-rot pathogenicity. Mutants in this group (designated GacA−1) contained an insertion of MudI in a locus corresponding to the gacA gene of P. viridiflava. Like LemA− mutants, GacA− mutants also exhibited alteration in colony morphology and showed deficiency in production of Pel and Prt. However, GacA− mutants produced much lower levels of levan and fluorescent pyoverdine siderophore than the wild type and LemA− mutants. These results provide the first genetic evidence that P. marginalis produces a single alkaline Pel for maceration of plant tissue and demonstrate that production of Pel, Prt, levan, and pyoverdin by this bacterium is mediated by the two-component lemA/gacA gene system.Key words: two-component regulators, pectate lyase, protease, levan, pyoverdin.

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22

Sultana, Razia, Regine Fuchs, Hans Schmickler, Karin Schlegel, Herbert Budzikiewicz, Bina Shaheen Siddiqui, Valerie Geoffrey, and Jean-Marie Meyer. "A Pyoverdin from Pseudomonas sp. CFML 95-275§." Zeitschrift für Naturforschung C 55, no. 11-12 (December 1, 2000): 857–65. http://dx.doi.org/10.1515/znc-2000-11-1201.

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From Pseudomonas sp. CFML 95-275 a pyoverdin was isolated with a cyclopeptidic substructure. It could be shown that this pyoverdin is identical with one obtained from Pseudomonas fluorescens BTP 7 for which a lactone structure had been deduced from the interpretation of a FAB spectrum. The elucidation of the correct structure of the pyoverdin is described.

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Mossialos, Dimitris, Jean-Marie Meyer, Herbert Budzikiewicz, Ulrich Wolff, Nico Koedam, Christine Baysse, Vanamala Anjaiah, and Pierre Cornelis. "Quinolobactin, a New Siderophore ofPseudomonas fluorescens ATCC 17400, the Production of Which Is Repressed by the Cognate Pyoverdine." Applied and Environmental Microbiology 66, no. 2 (February 1, 2000): 487–92. http://dx.doi.org/10.1128/aem.66.2.487-492.2000.

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ABSTRACT Transposon mutant strain 3G6 of Pseudomonas fluorescensATCC 17400 which was deficient in pyoverdine production, was found to produce another iron-chelating molecule; this molecule was identified as 8-hydroxy-4-methoxy-quinaldic acid (designated quinolobactin). The pyoverdine-deficient mutant produced a supplementary 75-kDa iron-repressed outer membrane protein (IROMP) in addition to the 85-kDa IROMP present in the wild type. The mutant was also characterized by substantially increased uptake of 59Fe-quinolobactin. The 75-kDa IROMP was produced by the wild type after induction by quinolobactin-containing culture supernatants obtained from the pyoverdine-negative mutant or by purified quinolobactin. Conversely, adding purified wild-type pyoverdine to the growth medium resulted in suppression of the 75-kDa IROMP in the pyoverdine-deficient mutant; however, suppression was not observed when Pseudomonas aeruginosa PAO1 pyoverdine, a siderophore utilized by strain 3G6, was added to the culture. Therefore, we assume that the quinolobactin receptor is the 75-kDa IROMP and that the quinolobactin-mediated iron uptake system is repressed by the cognate pyoverdine.

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24

LIAO, CHING-HSING, and GERALD M. SAPERS. "Influence of Soft Rot Bacteria on Growth of Listeria monocytogenes on Potato Tuber Slices†." Journal of Food Protection 62, no. 4 (April 1, 1999): 343–48. http://dx.doi.org/10.4315/0362-028x-62.4.343.

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Growth of Listeria monocytogenes on potato tuber slices and its interaction with four representative species of soft rot bacteria (Pseudomonas fluorescens, P. viridiflava, Erwinia carotovora subsp. carotovora, and Xanthomonas campestris) were investigated. When potato tuber slices were inoculated with one of two L. monocytogenes strains (Scott A and ATCC 15313), an increase in numbers of 3 to 4 logs per gram of tissue was observed with samples that were stored at 20°C for 6 days. However, an increase of about 2 logs was observed with samples that were stored at 8°C for 12 days. When potato slices were simultaneously inoculated with L. monocytogenes and one of the four soft rot bacteria, the growth of L. monocytogenes was inhibited in the presence of P. fluorescens or P. viridiflava but was not significantly affected in the presence of E. carotovora or X. campestris. The antagonism of the two pseudomonads to L. monocytogenes was also observed in potato tuber extract and in culture media. Formation of inhibition zones was observed only in iron-deficient media but not in the medium supplemented with FeCl3. In addition, production of fluorescent siderophore (pyoverdin) by these two pseudomonads was demonstrated. L. monocytogenes was unable to colonize macerated plant tissue induced by soft-rotting bacteria 2 days before inoculation of the pathogen. These results indicate that growth of L. monocytogenes on potato tuber slices is differentially affected by soft rot bacteria and that antagonism of fluorescent pseudomonads to L. monocytogenes is possibly caused by the production of iron-chelating siderophore by these pseudomonads.

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Hohlneicher, U., R. Hartmann, K. Taraz, and H. Budzikiewicz. "Pyoverdin, Ferribactin, Azotobactin -a New Triade of Siderophores from Pseudomonas chlororaphis ATCC 9446 and Its Relation to Pseudomonas fluorescens ATCC 13525." Zeitschrift für Naturforschung C 50, no. 5-6 (June 1, 1995): 337–44. http://dx.doi.org/10.1515/znc-1995-5-602.

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Abstract It is shown that Pseudomonas fluorescens ATCC 13525 and Pseudomonas chlororaphis ATCC 9446 produce identical pyoverdins and ferribactins. As the structures of these sidero phores are usually species or even strain specific this exception should be kept in mind in view of the reclassification of the genus Pseudomonas. From Pseudomonas chlororaphis an additional siderophore could be obtained which has the same peptide chain as the co-occur ring pyoverdins and ferribactin, but a chromophore which is typical for azotobactins from Azotobacter vinelandii.

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26

Vandenende, Chris S., Matthew Vlasschaert, and Stephen Y. K. Seah. "Functional Characterization of an Aminotransferase Required for Pyoverdine Siderophore Biosynthesis in Pseudomonas aeruginosa PAO1." Journal of Bacteriology 186, no. 17 (September 1, 2004): 5596–602. http://dx.doi.org/10.1128/jb.186.17.5596-5602.2004.

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ABSTRACT The fluorescent dihydroxyquinoline chromophore of the pyoverdine siderophore in Pseudomonas is a condensation product of d-tyrosine and l-2,4-diaminobutyrate. Both pvdH and asd (encoding aspartate β-semialdehyde dehydrogenase) knockout mutants of Pseudomonas aeruginosa PAO1 were unable to synthesize pyoverdine under iron-limiting conditions in the absence of l-2,4-diaminobutyrate in the culture media. The pvdH gene was subcloned, and the gene product was hyperexpressed and purified from P. aeruginosa PAO1. PvdH was found to catalyze an aminotransferase reaction, interconverting aspartate β-semialdehyde and l-2,4-diaminobutyrate. Steady-state kinetic analysis with a novel coupled assay established that the enzyme adopts a ping-pong kinetic mechanism and has the highest specificity for α-ketoglutarate. The specificity of the enzyme toward the smaller keto acid pyruvate is 41-fold lower. The enzyme has negligible activity toward other keto acids tested. Homologues of PvdH were present in the genomes of other Pseudomonas spp. These homologues were found in the DNA loci of the corresponding genomes that contain other pyoverdine synthesis genes. This suggests that there is a general mechanism of l-2,4-diaminobutyrate synthesis in Pseudomonas strains that produce the pyoverdine siderophore.

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27

Meyer, Jean-Marie, Valérie A. Geoffroy, Christine Baysse, Pierre Cornelis, Insa Barelmann, Kambiz Taraz, and Herbert Budzikiewicz. "Siderophore-Mediated Iron Uptake in Fluorescent Pseudomonas: Characterization of the Pyoverdine-Receptor Binding Site of Three Cross-Reacting Pyoverdines." Archives of Biochemistry and Biophysics 397, no. 2 (January 2002): 179–83. http://dx.doi.org/10.1006/abbi.2001.2667.

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28

Mirleau, Pascal, Laurent Philippot, Thérèse Corberand, and Philippe Lemanceau. "Involvement of Nitrate Reductase and Pyoverdine in Competitiveness of Pseudomonas fluorescens Strain C7R12 in Soil." Applied and Environmental Microbiology 67, no. 6 (June 1, 2001): 2627–35. http://dx.doi.org/10.1128/aem.67.6.2627-2635.2001.

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ABSTRACT Involvement of nitrate reductase and pyoverdine in the competitiveness of the biocontrol strain Pseudomonas fluorescens C7R12 was determined, under gnotobiotic conditions, in two soil compartments (bulk and rhizosphere soil), with the soil being kept at two different values of matric potential (−1 and −10 kPa). Three mutants affected in the synthesis of either the nitrate reductase (Nar−), the pyoverdine (Pvd−), or both (Nar− Pvd−) were used. The Nar− and Nar− Pvd− mutants were obtained by site-directed mutagenesis of the wild-type strain and of the Pvd− mutant, respectively. The selective advantage given by nitrate reductase and pyoverdine to the wild-type strain was assessed by measuring the dynamic of each mutant-to-total-inoculant (wild-type strain plus mutant) ratio. All three mutants showed a lower competitiveness than the wild-type strain, indicating that both nitrate reductase and pyoverdine are involved in the fitness of P. fluorescens C7R12. The double mutant presented the lowest competitiveness. Overall, the competitive advantages given to C7R12 by nitrate reductase and pyoverdine were similar. However, the selective advantage given by nitrate reductase was more strongly expressed under conditions of lower aeration (−1 kPa). In contrast, the selective advantage given by nitrate reductase and pyoverdine did not differ in bulk and rhizosphere soil, indicating that these bacterial traits are not specifically involved in the rhizosphere competence but rather in the saprophytic ability of C7R12 in soil environments.

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29

Matthijs, Sandra, Herbert Budzikiewicz, Mathias Schäfer, Bernard Wathelet, and Pierre Cornelis. "Ornicorrugatin, a New Siderophore from Pseudomonas fluorescens AF76." Zeitschrift für Naturforschung C 63, no. 1-2 (February 1, 2008): 8–12. http://dx.doi.org/10.1515/znc-2008-1-202.

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From a pyoverdin-negative mutant of Pseudomonas fluorescens AF76 a new lipopeptidic siderophore (ornicorrugatin) could be isolated. It is structurally related to the siderophore of Pseudomonas corrugata differing in the replacement of one Dab unit by Orn.

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30

Schröder, H., J. Adam K. Taraz, and H. Budzikiewicz. "Dihydropyoverdinsulfonsäuren - Zwischenstufen bei der Biogenese? / Dihydropyoverdin Sulfonic Acids - Intermediates in the Biogenesis?" Zeitschrift für Naturforschung C 50, no. 9-10 (October 1, 1995): 616–21. http://dx.doi.org/10.1515/znc-1995-9-1004.

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Abstract From the culture media of Pseudomonas aptata 4b and of Pseudomonas fluorescens ATCC 13525 5,6-dihydropyoverdin-7-sulfonic acids could be isolated. Their possible role in the biogenetic pathway leading to the pyoverdins will be discussed

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31

Gandouzi, Islem, Mihaela Tertis, Andreea Cernat, Dalila Saidane-Mosbahi, Aranka Ilea, and Cecilia Cristea. "A Nanocomposite Based on Reduced Graphene and Gold Nanoparticles for Highly Sensitive Electrochemical Detection of Pseudomonas aeruginosa through Its Virulence Factors." Materials 12, no. 7 (April 11, 2019): 1180. http://dx.doi.org/10.3390/ma12071180.

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Pyoverdine is a fluorescent siderophore produced by Pseudomonas aeruginosa that can be considered as a detectable marker in nosocomial infections. The presence of pyoverdine in water can be directly linked to the presence of the P. aeruginosa, thus being a nontoxic and low-cost marker for the detection of biological contamination. A novel platform was developed and applied for the electrochemical selective and sensitive detection of pyoverdine, based on a graphene/graphite-modified screen-printed electrode (SPE) that was electrochemically reduced and decorated with gold nanoparticles (NPs). The optimized sensor presenting higher sensitivity towards pyoverdine was successfully applied for its detection in real samples (serum, saliva, and tap water), in the presence of various interfering species. The excellent analytical performances underline the premises for an early diagnosis kit of bacterial infections based on electrochemical sensors.

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32

Ambrosi, Cecilia, Livia Leoni, and Paolo Visca. "Different Responses of Pyoverdine Genes to Autoinduction in Pseudomonas aeruginosa and the Group Pseudomonas fluorescens-Pseudomonas putida." Applied and Environmental Microbiology 68, no. 8 (August 2002): 4122–26. http://dx.doi.org/10.1128/aem.68.8.4122-4126.2002.

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ABSTRACT We investigated the regulation of the psbA and pvdA pyoverdine biosynthesis genes, which encode the l-ornithine N 5-oxygenase homologues in Pseudomonas strain B10 and Pseudomonas aeruginosa PAO1, respectively. We demonstrate that pyoverdineB10, as the end product of its biosynthetic pathway, is a key participant of the control circuit regulating its own production in Pseudomonas strain B10. In P. aeruginosa PAO1, however, pyoverdinePAO1 has no apparent role in the positive regulation of the pvdA gene.

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Voss, Jessica, Kambiz Taraz, and Herbert Budzikiewicz. "A Pyoverdin from the Antarctica Strain 51W of Pseudomonas fluorescens." Zeitschrift für Naturforschung C 54, no. 3-4 (April 1, 1999): 156–62. http://dx.doi.org/10.1515/znc-1999-3-403.

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From the strain 51W of Pseudomonas fluorescens living under extreme conditions at the Schirmacher Oasis (Antarctica) a pyoverdin was obtained. Its structure was elucidated by chemical degradation and spectroscopic methods. The NMR data of the pyoverdin and of its Ga(III) complex were compared. Appreciable influences of the metal on the chemical shifts of the atoms at its binding sites were observed. Thus the structural elements involved in the complexation can be identified and coinciding signals of amino acids occurring more than once in the peptide chain can be separated.

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Ambrosi, Cecilia, Federica Tiburzi, Francesco Imperi, Lorenza Putignani, and Paolo Visca. "Involvement of AlgQ in Transcriptional Regulation of Pyoverdine Genes in Pseudomonas aeruginosa PAO1." Journal of Bacteriology 187, no. 15 (August 1, 2005): 5097–107. http://dx.doi.org/10.1128/jb.187.15.5097-5107.2005.

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ABSTRACT In response to iron limitation, Pseudomonas aeruginosa produces the fluorescent siderophore pyoverdine. Transcription of pyoverdine biosynthetic (pvd) genes is driven by the iron starvation sigma factor PvdS, which is negatively regulated by the Fur-Fe(II) holorepressor. We studied the effect of AlgQ, the Escherichia coli Rsd orthologue, on pyoverdine production by P. aeruginosa PAO1. AlgQ is a global regulatory protein which activates alginate, ppGpp, and inorganic polyphosphate synthesis through a cascade involving nucleoside diphosphate kinase (Ndk). AlgQ is also capable of interacting with region 4 of RpoD. In a reconstituted E. coli system, PvdS-dependent transcription from the pvdA promoter was doubled by the multicopy algQ gene. The P. aeruginosa ΔalgQ mutant exhibited a moderate but reproducible reduction in pyoverdine production compared with wild-type PAO1, as a result of a decline in transcription of pvd genes. PvdS expression was not affected by the algQ mutation. Single-copy algQ fully restored pyoverdine production and expression of pvd genes in the ΔalgQ mutant, while ndk did not. An increased intracellular concentration of RpoD mimicked the ΔalgQ phenotype, whereas PvdS overexpression suppressed the algQ mutation. E. coli rsd could partially substitute for algQ in transcriptional modulation of pvd genes. We propose that AlgQ acts as an anti-sigma factor for RpoD, eliciting core RNA polymerase recruitment by PvdS and transcription initiation at pvd promoters. AlgQ provides a link between the pyoverdine and alginate regulatory networks. These systems have similarities in responsiveness and physiological function: both depend on alternative sigma factors, respond to nutrient starvation, and act as virulence determinants for P. aeruginosa.

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Peek, Mary E., Abhinav Bhatnagar, Nael A. McCarty, and Susu M. Zughaier. "Pyoverdine, the Major Siderophore inPseudomonas aeruginosa, Evades NGAL Recognition." Interdisciplinary Perspectives on Infectious Diseases 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/843509.

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Pseudomonas aeruginosais the most common pathogen that persists in the cystic fibrosis lungs. Bacteria such asP. aeruginosasecrete siderophores (iron-chelating molecules) and the host limits bacterial growth by producing neutrophil-gelatinase-associated lipocalin (NGAL) that specifically scavenges bacterial siderophores, therefore preventing bacteria from establishing infection.P. aeruginosaproduces a major siderophore known as pyoverdine, found to be important for bacterial virulence and biofilm development. We report that pyoverdine did not bind to NGAL, as measured by tryptophan fluorescence quenching, while enterobactin bound to NGAL effectively causing a strong response. The experimental data indicate that pyoverdine evades NGAL recognition. We then employed a molecular modeling approach to simulate the binding of pyoverdine to human NGAL using NGAL’s published crystal structures. The docking of pyoverdine to NGAL predicted nine different docking positions; however, neither apo- nor ferric forms of pyoverdine docked into the ligand-binding site in the calyx of NGAL where siderophores are known to bind. The molecular modeling results offer structural support that pyoverdine does not bind to NGAL, confirming the results obtained in the tryptophan quenching assay. The data suggest that pyoverdine is a stealth siderophore that evades NGAL recognition allowingP. aeruginosato establish chronic infections in CF lungs.

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Lenz, Christof, Cordula Amann, Gernot Briskot, Kambiz Taraz, and Herbert Budzikiewicz. "Succinopyoverdins - a New Variety of the Pyoverdin Chromophore." Zeitschrift für Naturforschung C 55, no. 3-4 (April 1, 2000): 146–52. http://dx.doi.org/10.1515/znc-2000-3-404.

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Abstract Pseudomonas spp. of the fluorescent group produce siderophores (so-called pyoverdins) consisting of a peptide chain attached to a pyrimidoquinoline ring system which is derived from a condensation product of L-Dab and D-Tyr. Commonly several related compounds are found to accompany the pyoverdins having the same peptide chain, but differing in the heterocyclic part. The structure elucidation of a new variety (succinopyoverdin) is described here.

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37

Hohnadel, D., and J. M. Meyer. "Specificity of pyoverdine-mediated iron uptake among fluorescent Pseudomonas strains." Journal of Bacteriology 170, no. 10 (1988): 4865–73. http://dx.doi.org/10.1128/jb.170.10.4865-4873.1988.

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Y Ramírez-Rueda, Román, and Marcos J. Salvador. "Phenotypic detection of quorum sensing inhibition in Pseudomonas aeruginosa pyoverdine and swarming by volatile organic products." Future Microbiology 15, no. 12 (August 2020): 1147–56. http://dx.doi.org/10.2217/fmb-2020-0033.

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Aim: To determine phenotypically the anti quorum-sensing (QS) activity of 30 volatile organic products (VOPs) through the inhibition of swarming motility and pyoverdine production in Pseudomonas aeruginosa. Materials & methods: Twenty-four essential oils and six small volatile organic compounds randomly selected were screened for their anti-QS activity by violacein inhibition on Chromobacterium violaceum. The VOPs with positive results were subsequently evaluated for swarming motility and pyoverdine production on P. aeruginosa determining the colony diameter and fluorescence under UV light, respectively. Results: Fifty percent of VOPs tested showed strong violacein inhibition, 40% presented anti-swarming activity and 33% inhibited pyoverdine production. Conclusion: Our data demonstrate that VOPs have a great potential to inhibit virulence factors mediated by QS in P. aeruginosa

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Michels, J., H. Benoni, G. Briskot, J. Lex, H. Schmickler, K. Taraz, H. Budzikiewicz, H. Korth, and G. Pulverer. "Isolierung und spektroskopische Charakterisierung des Pyoverdin-Chromophors sowie seines 5-Hydroxy-Analogen [1] / Isolation and Spectroscopic Characterization of the Pyoverdin Chromophore and of Its 5-Hydroxy Analogue [1]." Zeitschrift für Naturforschung C 46, no. 11-12 (December 1, 1991): 993–1000. http://dx.doi.org/10.1515/znc-1991-11-1211.

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Abstract The isolation of the common chromophore of the pyoverdins isolated from iron-deficient cultures of fluorescent Pseudomonas strains and of its 5-hydroxy analogue as well as the spectroscopic characterization of the two compounds is described.

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Greenwald, Jason, Gabrielle Zeder-Lutz, Agnès Hagege, Hervé Celia, and Franc Pattus. "The Metal Dependence of Pyoverdine Interactions with Its Outer Membrane Receptor FpvA." Journal of Bacteriology 190, no. 20 (July 18, 2008): 6548–58. http://dx.doi.org/10.1128/jb.00784-08.

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ABSTRACT To acquire iron, Pseudomonas aeruginosa secretes the fluorescent siderophore pyoverdine (Pvd), which chelates iron and shuttles it into the cells via the specific outer membrane transporter FpvA. We studied the role of iron and other metals in the binding and transport of Pvd by FpvA and conclude that there is no significant affinity between FpvA and metal-free Pvd. We found that the fluorescent in vivo complex of iron-free FpvA-Pvd is in fact a complex with aluminum (FpvA-Pvd-Al) formed from trace aluminum in the growth medium. When Pseudomonas aeruginosa was cultured in a medium that had been treated with a metal affinity resin, the in vivo formation of the FpvA-Pvd complex and the recycling of Pvd on FpvA were nearly abolished. The accumulation of Pvd in the periplasm of Pseudomonas aeruginosa was also reduced in the treated growth medium, while the addition of 1 μM AlCl3 to the treated medium restored the effects of trace metals observed in standard growth medium. Using fluorescent resonance energy transfer and surface plasmon resonance techniques, the in vitro interactions between Pvd and detergent-solubilized FpvA were also shown to be metal dependent. We demonstrated that FpvA binds Pvd-Fe but not Pvd and that Pvd did not compete with Pvd-Fe for FpvA binding. In light of our finding that the Pvd-Al complex is transported across the outer membrane of Pseudomonas aeruginosa, a model for siderophore recognition based on a metal-induced conformation followed by redox selectivity for iron is discussed.

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Viducic, Darija, Tsuneko Ono, Keiji Murakami, Mikiko Katakami, Heni Susilowati, and Yoichiro Miyake. "rpoN Gene of Pseudomonas aeruginosa Alters Its Susceptibility to Quinolones and Carbapenems." Antimicrobial Agents and Chemotherapy 51, no. 4 (January 29, 2007): 1455–62. http://dx.doi.org/10.1128/aac.00348-06.

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ABSTRACT The alternative sigma factor σ54 has been implicated in diverse functions within the cells. In this study, we have constructed an rpoN mutant of Pseudomonas aeruginosa and investigated its importance as a target for antimicrobial agents, such as quinolones and carbapenems. The stationary-phase cells of the rpoN mutant displayed a survival rate approximately 15 times higher than that of the wild-type cells in the presence of quinolones and carbapenems. The stationary phase led to substantial production of pyoverdine by the P. aeruginosa rpoN mutant. Pyoverdine synthesis correlated with decreased susceptibility to antimicrobial agents. Quantitative real-time PCR revealed that stationary-phase cells of the rpoN mutant grown without an antimicrobial agent had approximately 4- to 140- and 2- to 14-fold-higher levels of transcripts of the pvdS and vqsR genes, respectively, than the wild-type strain. In the presence of an antimicrobial agent, levels of pvdS and vqsR transcripts were elevated 400- and 5-fold, respectively, in comparison to the wild-type levels. Flow cytometry assays using a green fluorescent protein reporter demonstrated increased expression of the vqsR gene in the rpoN mutant throughout growth. A pvdS mutant of P. aeruginosa, deficient in pyoverdine production, was shown to be susceptible to biapenem. These findings suggest that rpoN is involved in tolerance to antimicrobial agents in P. aeruginosa and that its tolerant effect is partly dependent on increased pyoverdine production and vqsR gene expression.

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Sosnin, E. A., O. S. Zhdanova, E. R. Kashapova, and V. Ya Artyukhov. "Pyoverdine as a fluorescent marker of antibiotic sensitivity of Pseudomonas Aeruginosa." Optics and Spectroscopy 117, no. 6 (December 2014): 1018–24. http://dx.doi.org/10.1134/s0030400x14110204.

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Kisaalita, William S., Patricia J. Slininger, and Rodney J. Bothast. "Defined media for optimal pyoverdine production by Pseudomonas fluorescens 2-79." Applied Microbiology and Biotechnology 39, no. 6 (August 1993): 750–55. http://dx.doi.org/10.1007/bf00164461.

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Galet, Justine, Aurélie Deveau, Laurence Hôtel, Pascale Frey-Klett, Pierre Leblond, and Bertrand Aigle. "Pseudomonas fluorescens Pirates both Ferrioxamine and Ferricoelichelin Siderophores from Streptomyces ambofaciens." Applied and Environmental Microbiology 81, no. 9 (February 27, 2015): 3132–41. http://dx.doi.org/10.1128/aem.03520-14.

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ABSTRACTIron is essential in many biological processes. However, its bioavailability is reduced in aerobic environments, such as soil. To overcome this limitation, microorganisms have developed different strategies, such as iron chelation by siderophores. Some bacteria have even gained the ability to detect and utilize xenosiderophores, i.e., siderophores produced by other organisms. We illustrate an example of such an interaction between two soil bacteria,Pseudomonas fluorescensstrain BBc6R8 andStreptomyces ambofaciensATCC 23877, which produce the siderophores pyoverdine and enantiopyochelin and the siderophores desferrioxamines B and E and coelichelin, respectively. During pairwise cultures on iron-limiting agar medium, no induction of siderophore synthesis byP. fluorescensBBc6R8 was observed in the presence ofS. ambofaciensATCC 23877. Cocultures with aStreptomycesmutant strain that produced either coelichelin or desferrioxamines, as well as culture in a medium supplemented with desferrioxamine B, resulted in the absence of pyoverdine production; however, culture with a double mutant deficient in desferrioxamines and coelichelin production did not. This strongly suggests thatP. fluorescensBBbc6R8 utilizes the ferrioxamines and ferricoelichelin produced byS. ambofaciensas xenosiderophores and therefore no longer activates the production of its own siderophores. A screening of a library ofP. fluorescensBBc6R8 mutants highlighted the involvement of the TonB-dependent receptor FoxA in this process: the expression offoxAand genes involved in the regulation of its biosynthesis was induced in the presence ofS. ambofaciens. In a competitive environment, such as soil, siderophore piracy could well be one of the driving forces that determine the outcome of microbial competition.

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Taraz, K., D. Seinsche, and H. Budzikiewicz. "Pseudobactin-und Pseudobactin A-Varianten: Neue Peptidsiderophore vom Pyoverdin-Typ aus Pseudomonas fluovescens "E2" / Variants of Pseudobactin and Pseudobactin A: New Pyoverdin Type Peptide Siderophores from Pseudomonas fluorescens "E2"." Zeitschrift für Naturforschung C 46, no. 7-8 (August 1, 1991): 522–26. http://dx.doi.org/10.1515/znc-1991-7-804.

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Abstract From a strain of Pseudomonas fluorescens pseudobactin and several related compounds were isolated and their structures were elucidated. In this way a reference compound (5) could be obtained for the unambiguous determination of the absolute configuration of C-1 of the pyoverdin chromophore in newly isolated representatives of this class.

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Barelmann, Insa, Kambiz Taraz, Herbert Budzikiewicz, Valérie Geoffroy, and Jean-Marie Meyer. "The Structures of the Pyoverdins from Two Pseudomonas fluorescens Strains Accepted Mutually by Their Respective Producers." Zeitschrift für Naturforschung C 57, no. 1-2 (February 1, 2002): 9–16. http://dx.doi.org/10.1515/znc-2002-1-202.

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From Pseudomonas fluorescens PL7 and PL8 structurally related pyoverdins were isolated and their primary structures were elucidated by spectroscopic methods and degradation reactions. Despite of some structural differences both Fe(III) complexes are taken up by either strain with a high rate. The implications regarding the recognition at the cell surface are discussed.

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Ongena, Marc, Philippe Jacques, Philippe Thonart, Inga Gwose, Diana Urı́a Fernández, Mathias Schäfer, and Herbert Budzikiewicz. "The pyoverdin of Pseudomonas fluorescens BTP2, a novel structural type." Tetrahedron Letters 42, no. 34 (August 2001): 5849–51. http://dx.doi.org/10.1016/s0040-4039(01)01077-2.

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Hussien, Shimaa S., Osman A. Desouky, Mahmoud E. F. Abdel-Haliem, and Abdou A. El-Mougith. "Uranium (VI) Complexation with Siderophores-pyoverdine Produced by Pseudomonas Fluorescens SHA 281." International Journal of Nuclear Energy Science and Engineering 3, no. 4 (2013): 95. http://dx.doi.org/10.14355/ijnese.2013.0304.03.

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McKellar, R. C., and H. Cholette. "Production of Extracellular Enzymes by a Pyoverdine-Deficient Mutant of Pseudomonas Fluorescens." Canadian Institute of Food Science and Technology Journal 20, no. 5 (December 1987): 324. http://dx.doi.org/10.1016/s0315-5463(87)71316-9.

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Meyer, Jean-Marie. "Pyoverdines: pigments, siderophores and potential taxonomic markers of fluorescent Pseudomonas species." Archives of Microbiology 174, no. 3 (August 30, 2000): 135–42. http://dx.doi.org/10.1007/s002030000188.

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Journal articles on the topic 'Pyoverdine Pseudomonas fluorescen'

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