Increase in spermine content coordinated with siderophore production in Paracoccus denitrificans

Bergeron, Raymond J.; Weimar, William R.

doi:10.1128/jb.173.7.2238-2243.1991

Cited by 8 publications

(9 citation statements)

References 44 publications

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“…In low pH medium and in the iron-limiting medium, no pavettamine was detected. For both conditions, induction of the production of polyamines in certain bacteria has been reported (Shah and Swiatlo, 2008;Bergeron and Weimar, 1991). Our results provide evidence that the endosymbiont isolates of Fadogia homblei are not capable of producing pavettamine under the investigated culture conditions in vitro, since our method could detect pavettamine at minimal concentration.…”

Section: The Endosymbiont Of Fadogia Homblei Revealed No In Vitro Prosupporting

confidence: 49%

Production of toxic pavettamine and pavettamine conjugates in the gousiekte-causing Fadogia homblei plant and its relation to the bacterial endosymbiont

Elst¹,

Wyk²,

Schultz³

et al. 2013

Phytochemistry

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Plant poisoning of livestock is responsible for considerable economic losses in southern Africa.Six plant species of the Rubiaceae family are known to cause gousiekte, a cardiac syndrome of ruminants induced by ingestion of the toxic compound pavettamine. Progress in understanding the aetiology of this disease is largely hampered by the variable toxicity of the plants and the -2 -absence of a quantification method for pavettamine. The pavettamine concentration in leaf samples of Fadogia homblei, a known gousiekte causing plant, was analyzed by massspectrometry. In the most apical leaf pair, the highest concentration of pavettamine was detected. Distal leaves contained progressively less pavettamine. Besides a significant amount of free pavettamine, most pavettamine was found to occur in a conjugated form. To which molecules the pavettamine is conjugated remains unknown as is the function of conjugated pavettamine in the development of gousiekte. All know gousiekte-causing plants contain symbiotic bacteria in their leaves; it was hypothesized that these bacteria might be involved in the production of pavettamine. However, analysis of in vitro cultures of the Fadogia homblei endosymbiont revealed no production of pavettamine. Pavettamine is therefore not produced by the bacteria alone. It is either the product of the interaction with the plant or solely produced by the host.

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Section: The Endosymbiont Of Fadogia Homblei Revealed No In Vitro Prosupporting

confidence: 49%

Production of toxic pavettamine and pavettamine conjugates in the gousiekte-causing Fadogia homblei plant and its relation to the bacterial endosymbiont

Elst¹,

Wyk²,

Schultz³

et al. 2013

Phytochemistry

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“…In agreement, significantly increased levels of spermidine, spermine and putrescine were detected in the metabolome of iron limited C. difficile cells (Supplementary Table S6). Already in the nineties an increase in polyamines in bacterial cell grown under iron-limited conditions was studied (Bergeron and Weimar, 1991). A similar close relationship between intracellular iron and polyamine content was described for cancer cells (Bae et al, 2018; Lane et al, 2018).…”

Section: Resultsmentioning

confidence: 99%

Iron Regulation in Clostridioides difficile

et al. 2018

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The response to iron limitation of several bacteria is regulated by the ferric uptake regulator (Fur). The Fur-regulated transcriptional, translational and metabolic networks of the Gram-positive, pathogen Clostridioides difficile were investigated by a combined RNA sequencing, proteomic, metabolomic and electron microscopy approach. At high iron conditions (15 μM) the C. difficile fur mutant displayed a growth deficiency compared to wild type C. difficile cells. Several iron and siderophore transporter genes were induced by Fur during low iron (0.2 μM) conditions. The major adaptation to low iron conditions was observed for the central energy metabolism. Most ferredoxin-dependent amino acid fermentations were significantly down regulated (had, etf, acd, grd, trx, bdc, hbd). The substrates of these pathways phenylalanine, leucine, glycine and some intermediates (phenylpyruvate, 2-oxo-isocaproate, 3-hydroxy-butyryl-CoA, crotonyl-CoA) accumulated, while end products like isocaproate and butyrate were found reduced. Flavodoxin (fldX) formation and riboflavin biosynthesis (rib) were enhanced, most likely to replace the missing ferredoxins. Proline reductase (prd), the corresponding ion pumping RNF complex (rnf) and the reaction product 5-aminovalerate were significantly enhanced. An ATP forming ATPase (atpCDGAHFEB) of the F0F1-type was induced while the formation of a ATP-consuming, proton-pumping V-type ATPase (atpDBAFCEKI) was decreased. The [Fe-S] enzyme-dependent pyruvate formate lyase (pfl), formate dehydrogenase (fdh) and hydrogenase (hyd) branch of glucose utilization and glycogen biosynthesis (glg) were significantly reduced, leading to an accumulation of glucose and pyruvate. The formation of [Fe-S] enzyme carbon monoxide dehydrogenase (coo) was inhibited. The fur mutant showed an increased sensitivity to vancomycin and polymyxin B. An intensive remodeling of the cell wall was observed, Polyamine biosynthesis (spe) was induced leading to an accumulation of spermine, spermidine, and putrescine. The fur mutant lost most of its flagella and motility. Finally, the CRISPR/Cas and a prophage encoding operon were downregulated. Fur binding sites were found upstream of around 20 of the regulated genes. Overall, adaptation to low iron conditions in C. difficile focused on an increase of iron import, a significant replacement of iron requiring metabolic pathways and the restructuring of the cell surface for protection during the complex adaptation phase and was only partly directly regulated by Fur.

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“…Certain catechol-type siderophores, such as agrobactin (37), vibriobactin (20), and parabactin (47) also contain polyamines, and in Paracococcus denitrificans, along with parabactin siderophore production, spermine production increases by an order of magnitude in response to iron starvation, although spermidine and not spermine donates its triamine backbone to the siderophore (5).…”

Section: Discussionmentioning

confidence: 99%

The ornithine decarboxylase gene odc is required for alcaligin siderophore biosynthesis in Bordetella spp.: putrescine is a precursor of alcaligin

Brickman

Armstrong

1996

J Bacteriol

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Chromosomal insertions defining Bordetella bronchiseptica siderophore phenotypic complementation group III mutants BRM3 and BRM5 were found to reside approximately 200 to 300 bp apart by restriction mapping of cloned genomic regions associated with the insertion markers. DNA hybridization analysis using B. bronchiseptica genomic DNA sequences flanking the cloned BRM3 insertion marker identified homologous Bordetella pertussis UT25 cosmids that complemented the siderophore biosynthesis defect of the group III B. bronchiseptica mutants. Subcloning and complementation analysis localized the complementing activity to a 2.8-kb B. pertussis genomic DNA region. Nucleotide sequencing identified an open reading frame predicted to encode a polypeptide exhibiting strong similarity at the primary amino acid level with several pyridoxal phosphate-dependent amino acid decarboxylases. Alcaligin production was fully restored to group III mutants by supplementation of iron-depleted culture media with putrescine (1,4-diaminobutane), consistent with defects in an ornithine decarboxylase activity required for alcaligin siderophore biosynthesis. Concordantly, the alcaligin biosynthesis defect of BRM3 was functionally complemented by the heterologous Escherichia coli speC gene encoding an ornithine decarboxylase activity. Enzyme assays confirmed that group III B. bronchiseptica siderophore-deficient mutants lack an ornithine decarboxylase activity required for the biosynthesis of alcaligin. Siderophore production by an analogous mutant of B. pertussis constructed by allelic exchange was undetectable. We propose the designation odc for the gene defined by these mutations that abrogate alcaligin siderophore production. Putrescine is an essential precursor of alcaligin in Bordetella spp.Nutritional iron limitation, mediated primarily by specific host iron-binding glycoproteins, is a front-line host defense against disease-causing infectious agents. Strategies aimed at defeating host iron restriction may involve the action of lowmolecular-mass, high-affinity, ferric iron-specific chelators of microbial origin, termed siderophores, that are synthesized coordinately with their cognate surface receptors and transport machinery in response to iron starvation (28). The role of siderophores in microbial pathogenesis is well established (29,53,54).Bordetella pertussis, the causative agent of human whooping cough or pertussis, and Bordetella bronchiseptica, the agent of swine atrophic rhinitis and kennel cough in dogs, are mucosal pathogens that colonize the upper respiratory tracts of their mammalian hosts. In the first reported molecular genetic studies of Bordetella iron acquisition systems, Armstrong and Clements (3) described the isolation of B. bronchiseptica mutants deficient in siderophore activity following transposon mutagenesis. DNA hybridization analysis using DNA probe sequences flanking the transposon insertions established the existence of homologs of B. bronchiseptica siderophore genes in B. pertussis. Reciprocal cross-feeding ex...

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Increase in spermine content coordinated with siderophore production in Paracoccus denitrificans

Cited by 8 publications

References 44 publications

Production of toxic pavettamine and pavettamine conjugates in the gousiekte-causing Fadogia homblei plant and its relation to the bacterial endosymbiont

Production of toxic pavettamine and pavettamine conjugates in the gousiekte-causing Fadogia homblei plant and its relation to the bacterial endosymbiont

Iron Regulation in Clostridioides difficile

The ornithine decarboxylase gene odc is required for alcaligin siderophore biosynthesis in Bordetella spp.: putrescine is a precursor of alcaligin

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