Isolation and properties of a yellow-green fluorescent peptide from Azotobacter medium

Bulen, William A.; LeComte, Jack R.

doi:10.1016/0006-291x(62)90119-5

Cited by 49 publications

(25 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Pyoverdin from P. aeruginosa shares structural aspects with other bacterial yellow-green fluorescent peptides: pseudobactin from Pseudomonas strain B10 (37), pyoverdin from Pseudomonas fluorescens (28,32,33), pseudobactin 7SR1 from a plant-deleterious Pseudomonas strain (44), and azotobactin from A. vinelandii (5,15). The same dihydroxyquinoline derivative, responsible for the fluorescence of these compounds, is present in all these compounds with only minor structural differences.…”

Section: Resultsmentioning

confidence: 99%

“…This fluorescent siderophore produced by P. aeruginosa is a complex peptide containing two hydroxamate groups and a dihydroxyquinoline derivative (42) as its theorized chelating moieties. Yellow-green fluorescent peptides produced by other fluorescent Pseudomonas species and Azotobacter vinelandii (5,15,28,32,33,37,44) have similar spectral characteristics and extensive structural homology with pyoverdin.Recent investigations have suggested that iron acquisition by P. aeruginosa may play a role in its pathogenesis. The concentration of iron in culture medium has a significant effect on the production of the extracellular proteins, toxin A, alkaline protease, and elastase (3, 4).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Mapping of mutations in Pseudomonas aeruginosa defective in pyoverdin production

Ankenbauer¹,

Hanne²,

Cox³

1986

J Bacteriol

View full text Add to dashboard Cite

Twelve mutants of Pseudomonas aeruginosa PAO defective in pyoverdin production were isolated (after chemical and transposon mutagenesis) that were nonfluorescent and unable to grow on medium containing 400 ,uM ethylenediaminedi(o-hydroxyphenylacetic acid). Four mutants were unable to produce hydroxamate, six were hydroxamate positive, one was temperature sensitive for pyoverdin production, and another was unable to synthesize pyoverdin on succinate minimal medium but was capable of synthesizing pyoverdin when grown on Casamino Acids medium (Difco Laboratories, Detroit, Mich.). The mutations were mapped on the PAO chromosome. All the mutations affecting pyoverdin production were located at 65 to 70 min, between catAl and mtu-9002.Pathogenic bacteria require iron for growth in a mammalian host (6). To obtain iron from the host, bacteria must effectively compete with the iron-sequestering proteins transferrin and lactoferrin (1). Many microbes possess iron acquisition systems mediated by siderophores, lowmolecular-weight products capable of binding and delivering iron to the cell via high-affinity transport systems (31).Pseudomonas aeruginosa is a major cause of nosocomial infections which result in high mortality. P. aeruginosa is known to produce two siderophores, pyochelin (9, 10, 25) and pyoverdin (8,42). Pyochelin is a phenolic siderophore that has two sulfur-containing heterocyclic rings (9, 10). Pyoverdin, previously termed bacterial fluorescein (A. Turfreijer, Ph.D. thesis, University of Amsterdam, Amsterdam, The Netherlands, 1941), has long been thought to be involved in iron metabolism because of its hydroxamate character (16) and the inhibition of its production by iron (14,17,38). Only recently has the siderophore activity of pyoverdin been demonstrated (8) and its molecular structure elucidated (42). This fluorescent siderophore produced by P. aeruginosa is a complex peptide containing two hydroxamate groups and a dihydroxyquinoline derivative (42) as its theorized chelating moieties. Yellow-green fluorescent peptides produced by other fluorescent Pseudomonas species and Azotobacter vinelandii (5,15,28,32,33,37,44) have similar spectral characteristics and extensive structural homology with pyoverdin.Recent investigations have suggested that iron acquisition by P. aeruginosa may play a role in its pathogenesis. The concentration of iron in culture medium has a significant effect on the production of the extracellular proteins, toxin A, alkaline protease, and elastase (3, 4). Pyochelin has been shown to increase the lethality of P. aeruginosa during infections in mice (7). A mutant unable to synthesize pyoverdin had an extremely depressed growth rate compared with that of wild-type strains when grown in human serum and transferrin (2).Advances in P. aeruginosa genetics have allowed the map positions of several reported virulence factors to be determined. Use of the chromosome-mobilizing plasmid R68.45 * Corresponding author.(19), R-prime plasmids (21), and transposon-facilitated recombination (24) has m...

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Mapping of mutations in Pseudomonas aeruginosa defective in pyoverdin production

Ankenbauer¹,

Hanne²,

Cox³

1986

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…Our own stand is to respect the valid name first introduced, which is pyoverdine (Elliott, 1958). The appelation "pyoverdine" has also been used (Menhart et al, 1991) to describe the closely related yellow-green fluorescent pigments produced by Azotobacter strains (Bulen and LeComte, 1962) and so far called azotobactins in regard to their siderophore functions. The choice of only one name, pyoverdine, to designate compounds belonging to the same family by their closely related structures and their identical biological function is strongly supported by the recent finding of one Pseudomonas strain which produces both pyoverdine-type and azotobactin-type related pigments (Hohlneicher et al, 1995).…”

Section: Detection Of Siderophoresmentioning

confidence: 99%

Iron Metabolism and Siderophores in Pseudomonas and Related Species

Meyer¹,

Stintzi²

1998

Pseudomonas

View full text Add to dashboard Cite

“…The known siderophores of A. vinelandii include the fluorescent compounds azotobactin D and azotobactin ␦ (13,14) and the catechol siderophores azotochelin (15), aminochelin (16), and protochelin (3). These five siderophores have been discovered and characterized over a span of about 30 years using primarily chemical assays (17), which allow the analysis of only one or a few siderophores at the same time due to limited sensitivity and separation power.…”

mentioning

confidence: 99%

The Siderophore Metabolome of Azotobacter vinelandii

Baars

Zhang

Morel

et al. 2016

Appl Environ Microbiol

View full text Add to dashboard Cite

In this study, we performed a detailed characterization of the siderophore metabolome, or "chelome," of the agriculturally important and widely studied model organism Azotobacter vinelandii. Using a new high-resolution liquid chromatography-mass spectrometry (LC-MS) approach, we found over 35 metal-binding secondary metabolites, indicative of a vast chelome in A. vinelandii. These include vibrioferrin, a siderophore previously observed only in marine bacteria. Quantitative analyses of siderophore production during diazotrophic growth with different sources and availabilities of Fe showed that, under all tested conditions, vibrioferrin was present at the highest concentration of all siderophores and suggested new roles for vibrioferrin in the soil environment. Bioinformatic searches confirmed the capacity for vibrioferrin production in Azotobacter spp. and other bacteria spanning multiple phyla, habitats, and lifestyles. Moreover, our studies revealed a large number of previously unreported derivatives of all known A. vinelandii siderophores and rationalized their origins based on genomic analyses, with implications for siderophore diversity and evolution. Together, these insights provide clues as to why A. vinelandii harbors multiple siderophore biosynthesis gene clusters. Coupled with the growing evidence for alternative functions of siderophores, the vast chelome in A. vinelandii may be explained by multiple, disparate evolutionary pressures that act on siderophore production.

show abstract

Isolation and properties of a yellow-green fluorescent peptide from Azotobacter medium

Cited by 49 publications

References 6 publications

Mapping of mutations in Pseudomonas aeruginosa defective in pyoverdin production

Mapping of mutations in Pseudomonas aeruginosa defective in pyoverdin production

Iron Metabolism and Siderophores in Pseudomonas and Related Species

The Siderophore Metabolome of Azotobacter vinelandii

Contact Info

Product

Resources

About