# Pyoverdine

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Pyoverdine Names Other names Pyoverdin Identifiers 3D model (JSmol) Interactive image ChEBI family: CHEBI:84046 PubChem CID 57012495 InChI InChI=1S/C56H88N18O22/c1-27(79)43-53(91)61-15-4-3-8-31(46(84)65-34(11-7-19-73(96)26-78)49(87)70-44(28(2)80)54(92)71-43)64-47(85)33(10-6-18-72(95)25-77)67-50(88)36(23-75)68-48(86)32(9-5-16-62-56(58)59)66-51(89)37(24-76)69-52(90)38-14-17-60-45-35(63-42(83)13-12-30(57)55(93)94)20-29-21-40(81)41(82)22-39(29)74(38)45/h20-22,25-28,30-34,36-38,43-45,60,75-76,79-82,95-96H,3-19,23-24,57H2,1-2H3,(H,61,91)(H,63,83)(H,64,85)(H,65,84)(H,66,89)(H,67,88)(H,68,86)(H,69,90)(H,70,87)(H,71,92)(H,93,94)(H4,58,59,62) Key: QIRRYPHVUMPBDX-UARRTFJPSA-N SMILES CC(C1C(=O)NC(C(=O)NCCCCC(C(=O)NC(C(=O)N1)CCCN(C=O)O)NC(=O)C(CCCN(C=O)O)NC(=O)C(CO)NC(=O)C(CCCN=C(N)N)NC(=O)C(CO)NC(=O)C2CCNC3N2C4=CC(=C(C=C4C=C3NC(=O)CCC(C(=O)O)N)O)O)C(C)O)O Properties Chemical formula C56H88N18O22 Molar mass 1365.424 g·mol−1 Appearance Solid Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Y verify (what is YN ?) Infobox references

Chemical compound

**Pyoverdines**[1] (alternatively, and less commonly, spelled as **pyoverdins**) are [fluorescent](/source/Fluorescence) [siderophores](/source/Siderophores) produced by certain [pseudomonads](/source/Pseudomonadaceae).[2][3] Pyoverdines are important [virulence factors](/source/Virulence_factor), and are required for [pathogenesis](/source/Pathogenesis) in many [biological models of infection](/source/Model_organism#Disease_models). Their contributions to bacterial pathogenesis include providing a crucial nutrient (i.e., [iron](/source/Iron)), regulation of other virulence factors (including [exotoxin A](/source/Pseudomonas_exotoxin) and the [protease](/source/Protease) PrpL),[4] supporting the formation of [biofilms](/source/Biofilm),[5] and are increasingly recognized for having [toxicity](/source/Toxin) themselves.[6][7][8]

Pyoverdines have also been investigated as "[Trojan Horse](/source/Trojan_Horse)" molecules for the delivery of [antimicrobials](/source/Antimicrobial) to otherwise [resistant bacterial strains](/source/Antimicrobial_resistance), as [chelators](/source/Chelation) that can be used for [bioremediation](/source/Bioremediation) of [heavy metals](/source/Heavy_metals), and as fluorescent reporters used to assay for the presence of iron and potentially other metals.[9]

Due to their bridging the gaps between [pathogenicity](/source/Pathogen), [iron metabolism](/source/Human_iron_metabolism), and fluorescence, pyoverdines have piqued the curiosity of scientists around the world for over 100 years.[*[citation needed](https://en.wikipedia.org/wiki/Wikipedia:Citation_needed)*]

## Biological functions

Like most siderophores, pyoverdine is synthesized and [secreted](/source/Secretion) into the environment when the [microorganism](/source/Microorganism) that produces it detects that [intracellular](/source/Intracellular) iron concentrations have fallen below a preset threshold. Although iron is the [fourth-most abundant element in the Earth's crust](/source/Abundance_of_elements_in_Earth's_crust), solubility of biologically relevant iron compounds is exceedingly low, and is generally insufficient for the needs of most (but not all) microorganisms. Siderophores, which are typically quite soluble and have exceptionally high [avidity](/source/Avidity) for [iron (III)](/source/Ferric) (the avidity of some siderophores for iron exceeds 1040 M-1 and many of the strongest avidities ever observed in nature are exhibited by siderophores for iron), help increase [bioavailability](/source/Bioavailability_(soil)) of iron by pulling it into aqueous solution.

In addition to this role, pyoverdine has a number of other functions, including regulating virulence,[4][5] limiting the growth of other bacterial species (and serving as a sort of antimicrobial) by limiting iron availability, and sequestering other metals and preventing their toxicity.

## Structure and characteristics

Although many (>100) forms of pyoverdine have been isolated and studied, they all have certain characteristics in common. Each pyoverdine molecule has three parts: a dihydroxyquinoline core, a 6-14 [amino acid](/source/Amino_acid) [peptide](/source/Peptide) that varies among [strains](/source/Strain_(biology)), and a side chain (usually composed of a 4-5 carbon α-[ketoacid](/source/Keto_acid) from the [Krebs/citric acid cycle](/source/Krebs_citric_acid_cycle)). The core of pyoverdine is responsible for several of its properties, including its well-known yellowish color and fluorescence.

### Structure

The dihydroxyquinoline core is composed of (1S)-5-amino-2,3-dihydro- 8,9-dihydroxy-1H-pyrimido[1,2-a][quinoline](/source/Quinoline)-1-carboxylic acid. This portion of the molecule is invariant amongst all observed pyoverdine molecules.

The core is modified by the addition of an amino acid chain composed of 6-14 amino acids. The chain of amino acids is built onto the [chromophore](/source/Chromophore) core, and is synthesized via [non-ribosomal peptide synthesis](/source/Non-ribosomal_peptide_synthesis).[10][11] As is common for non-ribsosomally synthesized peptides, pyoverdine frequently includes [D-form amino acids](/source/D_amino_acid) and non-standard amino acids, such as [*N*-5-formyl-*N*-5-hydroxyornithine](/source/Ornithine). The peptide chain may also be partially (or completely) cyclized. This peptide chain provides the other four aspects of the [hexadentate](/source/Denticity) interaction, usually through [hydroxamate](/source/Hydroxamic_acid) and/or [hydroxycarboxylate](https://en.wikipedia.org/w/index.php?title=Hydroxycarboxylate&action=edit&redlink=1) groups. This portion of the molecule is also crucial for interaction with the ferripyoverdine receptor (FpvA) that allows ferripyoverdine to be imported into the cell. The peptide chain produced by a given strain of *[Pseudomonas](/source/Pseudomonadaceae)* is currently thought to be invariant.

Little is known about the particular function or importance of the ketoacid side chain, but it is well known[12] that pyoverdine molecules with different ketoacids ([congeners](/source/Congener_(chemistry))) co-exist. Ketoacids that have been observed include [succinate](/source/Succinic_acid)/[succinamide](/source/Succinimide), [glutamate](/source/Glutamic_acid), [glutarate](/source/Glutaric_acid), [malate](/source/Malic_acid)/[malamide](https://en.wikipedia.org/w/index.php?title=Malamide&action=edit&redlink=1), and [α-ketoglutarate](/source/Alpha-Ketoglutaric_acid).

Structure of the peptide backbone in various fluorescent Pseudomonas strains. Amino acid three-letter codes are used, along with Q=chromophore, DXxx=D-amino acid, aThr=allo-threonine, c=cyclic structure, cOHOrn=cyclo-hydroxyornithine, Dab=diaminobutyric acid, Ac=Acetyl, Fo=formyl OH=hydroxyl[13] Pseudomonad species Strain Structure of the pyoverdine peptide chain P. aeruginosa ATCC15692 (PAO1) Q-DSer-Arg-DSer-FoOHOrn-c(Lys-FoOHOrn-Thr-Thr) P. aeruginosa ATCC27853 Q-DSer-FoOHDOrn-Orn-Gly-aDThr-Ser-cOHOrn P. aeruginosa Pa6 Q-DSer-Dab-FoOHOrn-Gln-DGln-FoOHDOrn-Gly P. chlororaphis ATCC9446 Q-DSer-Lys-Gly-FoOHOrn-c(Lys-FoOHDOrn-Ser) P. fluorescens bv.I ATCC13525 Q-DSer-Lys-Gly-FoOHOrn-c(Lys-FoOHDOrn-Ser) P. fluorescens bv.I 9AW Q-DSer-Lys-OHHis-aDThr-Ser-cOHOrn P. fluorescens bv.III ATCC17400 Q-DAla-DLys-Gly-Gly-OHAsp-DGln/Dab-Ser-DAla-cOHOrn P. fluorescens bv.V 51W Q-DAla-DLys-Gly-Gly-OHDAsp-DGln-DSer-Ala-Gly-aDThr-cOHOrn P. fluorescens bv.V 1W Q-DSer-Lys-Gly-FoOHOrn-c(Lys-FoOHDOrn-Ser) P. fluorescens bv.V 10CW Q-DSer-Lys-Gly-FoOHOrn-c(Lys-FoOHDOrn-Ser) P. fluorescens bv.VI PL7 Q-DSer-AcOHDOrn-Ala-Gly-aDThr-Ala-cOHOrn P. fluorescens bv.VI PL8 Q-DLys-AcOHDOrn-Ala-Gly-aDThr-Ser-cOHOrn P. fluorescens 1.3 Q-DAla-DLys-Gly-Gly-OHAsp-DGln/Dab-Gly-Ser-cOHOrn P. fluorescens 18.1 Q-DSer-Lys-Gly-FoOHOrn-Ser-DSer-Gly-c(Lys-FoOHDOrn-Ser) P. fluorescens CCM 2798 Q-Ser-Dab-Gly-Ser-OHDAsp-Ala-Gly-DAla-Gly-cOHOrn P. fluorescens CFBP 2392 Q-DLys-AcOHDOrn-Gly-aDThr-Thr-Gln-Gly-DSer-cOHOrn P. fluorescens CHA0 Q-Asp-FoOHDOrn-Lys-c(Thr-Ala-Ala-FoOHDOrn-Lys) P. putida bv. B 9BW Q-DSer-Lys-OHHis-aDThr-Ser-cOHOrn P. putida CFBP 2461 Q-Asp-Lys-OHDAsp-Ser-aDThr-Ala-Thr-DLys-cOHOrn P. tolaasii NCPPB 2192 Q-DSer-Lys-Ser-DSer-Thr-Ser-AcOHOrn-Thr-DSer-cOHDOrn

### Characteristics

Amongst their other notable characteristics, pyoverdines exhibit bright, relatively photostable fluorescence with characteristic [excitation and emission spectra](/source/Fluorescence_spectroscopy) that are rapidly and strongly [quenched](/source/Quenching_(fluorescence)) upon binding their natural [ligand](/source/Ligand), iron. Excitation and [molar absorptivity](/source/Molar_absorptivity) show moderate [pH](/source/PH) dependence, but fluorescence is generally unaffected by [pH](/source/PH) variations. Unlike fluorescence, [spectroscopic](/source/Spectroscopy) absorption shows little [quenching](/source/Quenching_(fluorescence)) upon [iron-binding](/source/Chelation), suggesting that the mechanism for molecular relaxation is vibrational, rather than via [electromagnetic radiation](/source/Fluorescence).

Pyoverdine coordinates a [hexadentate](/source/Denticity) (i.e., six-part) chelation of iron that involves six different oxygen atoms (2 from the dihyodroxyquinoline core and 2 from each of 2 different amino acids in the backbone). This results in a very tightly coordinated [octahedral](/source/Octahedral_molecular_geometry) complex that efficiently prevents the ingress of [water](/source/Water) or other materials that may disrupt binding. Typically, [ferric iron](/source/Ferric) is removed from pyoverdine by [reduction](/source/Redox) to the [ferrous](/source/Ferrous) state, for which pyoverdine has a much lower (i.e., 109 M-1) avidity. This allows for the non-destructive removal of iron from pyoverdine. After reduction, the iron is "handed off" to other carriers that have increased affinity for ferrous iron, while the apopyoverdine is re-exported for continued use.

Pyoverdine is structurally similar to [azobactin](https://en.wikipedia.org/w/index.php?title=Azobactin&action=edit&redlink=1), from *[Azotobacter vinelandii](/source/Azotobacter_vinelandii)*, except that the latter possesses an extra urea ring.[13]

## Synthesis

### Biosynthesis

In *Pseudomonas aeruginosa* PAO1 there are 14 *pvd* genes involved in the biosynthesis of pyoverdine.[14]

Pyoverdine biosynthesis seems to be largely regulated through the activity of the alternate [sigma factor](/source/Sigma_factor) PvdS which, in turn, is regulated both by the Fur system and by the intracellular sequestration of PvdS at the [plasma membrane](/source/Cell_membrane) and away from the [nucleoid](/source/Nucleoid) by the repressor FpvI.

Despite significant investigation, relatively little is known about the biosynthesis of pyoverdine. For example, It remains unclear whether the biosynthesis of pyoverdine takes place as individual components (i.e., the core, the peptide chain, and the ketoacid) or if the core and the other parts are condensed as a beginning molecule (possibly by the PvdL protein) and then modified by other enzymes afterward. For reasons that remain unclear, pyoverdine biosynthesis is strongly inhibited by the anti-cancer therapeutic [fluorouracil](/source/Fluorouracil),[15] particularly through its ability to disrupt RNA metabolism.[16] Although production of pyoverdines varies from strain to strain, fluorescent Pseudomonas species have been shown to produce between 200 and 500 mg/L when grown in iron-depleted conditions.[17][18]

#### Core

There is some dispute about the origin of the fluorescent chromophore core. Originally, it was widely thought to be synthesized by the *pvcABCD* [operon](/source/Operon), as deletion of portions of the *pvcC* and *pvcD* genes disrupts pyoverdine production.[19] Like other aspects of pyoverdine biosynthesis, the regulation of the *pvcABCD* is iron-dependent, and the loss of these genes' activity resulted in pyoverdine disruption.

A separate report suggests that *pvcABCD* may be responsible for the synthesis of paerucumarin (a pseudoverdine-related molecule) instead, and claims that loss of activity in the locus has no effect on pyoverdine production.[20] In addition, some fluorescent Pseudomonads lack apparent homologs of these genes, further calling into question whether this is the function of these genes.

This is consistent with reports that *pvdL* combines [coenzyme A](/source/Coenzyme_A) to a [myristic](/source/Myristic_acid) acid moiety, then adds a glutamate, [D-tyrosine](/source/Tyrosine), and [L-2,4-diaminobutyric acid](/source/L-2%2C4-diaminobutyric_acid) (DAB).[21] An alternate biosynthetic pathway suggests that *pvdL* incorporates glutamate, 2,4,5-trihydroxyphenylalanine and L-2,4-diaminobutyric acid instead.[22] This latter is supported by the identification of incorporation of a radiolabeled tyrosine into either pyoverdine or pseudoverdine.

This discrepancy remains unresolved.

#### Peptide chain

Several of the [genes](/source/Gene) responsible for pyoverdine biosynthesis (e.g., *pvdH, pvdA,* and *pvdF*) are involved in the generation of precursor and alternate amino acids necessary for various portions of the molecule.[23] Several others (e.g., *pvdI*, and *pvdJ*) are directly responsible for "stitching" together the peptide chain.[23] *pvdD* terminates the chain and releases the precursor into the [cytoplasm](/source/Cytoplasm), which is consistent with identification of pyoverdine-like molecules in the [cytoplasm](/source/Cytoplasm) with incompletely matured chromophores.[23]

#### Ketoacid

Currently, the best available evidence suggests that the ketoacid is originally attached to the chromophore core (as L-glutamate) when it is synthesized from D-tyrosine, L-2,4-diaminobutyric acid, and L-glutamate. It is unclear how this is later altered to the other congenerate (i.e., [a-ketoglutarate](/source/Alpha-Ketoglutaric_acid), [succinate](/source/Succinic_acid)/[succinamide](/source/Succinimide), etc.) forms.

#### Maturation and export

The localization of some of the Pvd proteins in the [periplasm](/source/Periplasm) and the outer membrane (such as PvdN, PvdO, PvdP, and PvdQ) have been interpreted to suggest that portions of the maturation of pyoverdine takes place in this location, perhaps after being transported into the [periplasm](/source/Periplasm) by PvdE, which is homologous to [ABC type exporters](/source/ATP-binding_cassette_transporter). How completely matured pyoverdine is exported from the cell remains unclear. Once completely matured, pyoverdine is exported from the [periplasm](/source/Periplasm) by PvdRT-OpmQ [efflux](/source/Efflux_(microbiology)) pump.

### Total chemical synthesis

A complete [organic synthesis](/source/Organic_synthesis) pathway for the pyoverdine produced by *[P. aeruginosa](/source/Pseudomonas_aeruginosa)* strain PAO1 has been reported[24] using [solid-phase peptide synthesis](/source/Solid-phase_peptide_synthesis). This protocol yielded pyoverdine at high yield (~48%) and is expected to substantially increase the ability of scientists to generate targeted derivatives on the pyoverdine scaffold and to facilitate the creation of siderophores with antimicrobial warheads.

## Mechanisms of virulence

Pyoverdine has been reported to be required for virulence in a variety of [disease models](/source/Model_organism#Disease_models), including *[C. elegans](/source/Caenorhabditis_elegans)* and [various models of murine infection](/source/Mouse) (e.g., burn models, pneumonia models, etc.).[6][15][25][26]

As noted above, pyoverdine contributes in several fashions to general virulence, including regulating the production of itself, exotoxin A (which stalls translation), and the protease PrpL.[4] There is also evidence that, although not essential for its formation, pyoverdine contributes to the production and development of biofilms that are important for virulence.[5]

Finally, pyoverdine is associated with several types of toxicity in its own right. In 2001, Albesa and colleagues reported that pyoverdine purified from a strain of *[P. fluorescens](/source/Pseudomonas_fluorescens)* exhibited profound [cytotoxicity](/source/Cytotoxicity) to mammalian [macrophages](/source/Macrophage) and that this effect was at least partially dependent upon [reactive oxygen species](/source/Reactive_oxygen_species).[27] Later, Kirienko and colleagues determined that pyoverdine is both necessary and sufficient for killing *[C. elegans](/source/Caenorhabditis_elegans),* that enters host cells, destabilizes [mitochondrial dynamics](/source/Mitochondrial_fusion), and induces a [hypoxic response](/source/Hypoxia_(medical)).[6][7] Exposure triggers a response that is consistent with [hypoxia](/source/Hypoxia_(medical)) that depends on the [HIF-1](/source/Hypoxia-inducible_factors) protein, suggesting that the host perceives a condition where it lacks the molecular tools for generating [ATP](/source/Adenosine_triphosphate) [(generally, iron, oxygen, and cellular reducing equivalents)](/source/Glycolysis).[6][7]

## Role in microbial cooperation

Once pyoverdine is secreted, it diffuses freely in the environment. Iron-bound pyoverdine (also known as ferripyoverdine) can be taken up by any bacterial cell with the appropriate [receptor](/source/Receptor_(biochemistry)), although this varies between strains.[28] Importantly, this creates a common good which can be exploited by 'cheaters' which retain the ability to use pyoverdine but have stopped making it. Since pyoverdine production is energetically costly, this can create a fitness advantage in cells that are not synthesizing it.[29][30][31][32] Consequently, pyoverdine has become a model trait to study [microbial cooperation](/source/Microbial_cooperation) and exploitation.[33][34]

In *[P. aeruginosa](/source/Pseudomonas_aeruginosa)*, pyoverdine non-producing "cheat" bacteria have been shown to i) evolve readily from a producing ancestor;[35] and ii) outcompete cooperating strains in mixed culture in a density- and frequency-dependent manner.[36][37] Since pyoverdine usage relies on passive [diffusion](/source/Diffusion) and pyoverdine production is metabolically costly, environmental conditions are known to influence the likelihood of successful exploitation. The competitive advantage of pyoverdine non-producers over producers in mixed culture was shown to be maximized when environments are well-mixed and molecules diffuse readily (low spatial structure) and when the costs and benefits of pyoverdine production are high, i.e. when iron is strongly limited.[31][38] Most studies on pyoverdine cooperation and cheating have been conducted using clinical isolates, but siderophore exploitation was recently also demonstrated in natural *[Pseudomonas](/source/Pseudomonas)* isolates from non-clinical samples.[39][40]

## Nomenclature

Currently, no widespread and systematic nomenclature is used to differentiate pyoverdine structures. A system was proposed in 1989,[41] consisting of Pyoverdine Type I, Type IIa, Type IIb, and Type III. At the time, only a few pyoverdine structures were known, and it was anticipated that much less variation would occur than has been seen. As a consequence of the tremendous heterogeneity observed in the peptide backbone, and the observation of congeners (pyoverdines from a single strain differing only in their ketoacid portions), nomenclature of pyoverdines remains rather tenuous and no single system has garnered universal acceptance.

## History

- 1850s: [Sédillot](/source/Charles-Emmanuel_S%C3%A9dillot) notes a blue-green discharge from surgical wound dressings.

- 1860: Pyoverdine (although not so named) was extracted from wound dressings by [Fordos](/source/Mathurin-Joseph_Fordos).

- 1862: Lucke associates pyoverdine with bacilli observed under microscope.

- 1882: *[Pseudomonas aeruginosa](/source/Pseudomonas_aeruginosa)* grown for first time in pure culture by Carle Gessard, reported in "On the Blue and Green Coloration of Bandages". Gessard names the organism *Bacillus aeruginosa*, after "aerugo", the Latin word for [verdigris](/source/Verdigris).

- 1889: [Bouchard](/source/Charles_Jacques_Bouchard) observes that injection of a rabbit infected with *[Bacillus anthracis](/source/Bacillus_anthracis)* (causative agent of [anthrax](/source/Anthrax)) with *[P. aeruginosa](/source/Pseudomonas_aeruginosa)* prevents formation of anthrax.

- 1889: Bouchard discovers that pyoverdine [fluoresces](/source/Fluorescence) under [ultraviolet light](/source/Ultraviolet).

- 1948, 1952: First observations that concentrations of iron and pyoverdine are reciprocal.

- 1978: Meyer and colleagues make first demonstration of role for pyoverdine in iron acquisition.

- 1980s–1990s: First structures and regulation of proverdine worked out

- 1999: First determination that pyoverdine fluorescence is [quenched](/source/Quenching_(fluorescence)) by iron binding.

## Other uses

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## Pseudoverdine

A compound related to pyoverdine, called pseudoverdine (formally known as 3-formylamino-6,7-dihydroxycoumarin) is also produced by some fluorescent Pseudomonads.[42] It is thought that pseudoverdine and pyoverdine may arise from a common precursor, 2,4,5-trihydroxyphenylalanine, which may condense with L-2,4-diaminobutyric acid to initiate pyoverdine production.[42]

Pseudoverdine is relatively similar to pyoverdine in its fluorescence and other [spectroscopic](/source/Spectroscopy) properties, and its ability to chelate ferric iron, albeit at much lower [affinity](/source/Chemical_affinity).[42] Unlike pyoverdine, it is incapable of [transporting](/source/Active_transport) iron into [cells](/source/Cell_(biology)), likely due to the absence of the peptide chain.[42] Another dissimilarity is that pseudoverdine does not appear to be [regulated](/source/Regulation_of_gene_expression) by the same processes as pyoverdine.[42]

## References

1. **[^](#cite_ref-1)** For the purposes of this page, pyoverdine will generally refer (unless otherwise noted) to the pyoverdine produced by *Pseudomonas aeruginosa* strain PAO1. It has been subjected to the most extensive study and can be considered the prototypical siderophore.

1. **[^](#cite_ref-2)** S. Wendenbaum; P. Demange; A. Dell; J. M. Meyer; M. A. Abdallah (1983). "The structure of pyoverdine Pa, the siderophore of Pseudomonas aeruginosa". *Tetrahedron Letters*. **24** (44): 4877–4880. [doi](/source/Doi_(identifier)):[10.1016/S0040-4039(00)94031-0](https://doi.org/10.1016%2FS0040-4039%2800%2994031-0).

1. **[^](#cite_ref-3)** Menhart, N.; Thariath, A.; Viswanatha, T. (1991). "Characterization of the pyoverdines of Azotobacter vinelandii ATCC 12837 with regard to heterogeneity". *Biology of Metals*. **4** (4): 223–32. [doi](/source/Doi_(identifier)):[10.1007/bf01141185](https://doi.org/10.1007%2Fbf01141185). [PMID](/source/PMID_(identifier)) [1838001](https://pubmed.ncbi.nlm.nih.gov/1838001). [S2CID](/source/S2CID_(identifier)) [8712926](https://api.semanticscholar.org/CorpusID:8712926).

1. ^ [***a***](#cite_ref-:2_4-0) [***b***](#cite_ref-:2_4-1) [***c***](#cite_ref-:2_4-2) Lamont, Iain L.; Beare, Paul A.; Ochsner, Urs; Vasil, Adriana I.; Vasil, Michael L. (2002-05-14). ["Siderophore-mediated signaling regulates virulence factor production in Pseudomonasaeruginosa"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC124530). *Proceedings of the National Academy of Sciences of the United States of America*. **99** (10): 7072–7077. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...99.7072L](https://ui.adsabs.harvard.edu/abs/2002PNAS...99.7072L). [doi](/source/Doi_(identifier)):[10.1073/pnas.092016999](https://doi.org/10.1073%2Fpnas.092016999). [ISSN](/source/ISSN_(identifier)) [0027-8424](https://search.worldcat.org/issn/0027-8424). [PMC](/source/PMC_(identifier)) [124530](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC124530). [PMID](/source/PMID_(identifier)) [11997446](https://pubmed.ncbi.nlm.nih.gov/11997446).

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Adapted from the Wikipedia article [Pyoverdine](https://en.wikipedia.org/wiki/Pyoverdine) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Pyoverdine?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.