GNPS - Siderophores produced by P tuberum
Ontology highlight
ABSTRACT:
INSTRUMENT(S): timsTOF Pro
ORGANISM(S): Paraburkholderia Tuberum (ncbitaxon:157910)
SUBMITTER: 
Laurent Bigler
PROVIDER: MSV000095895 | GNPS |
REPOSITORIES: GNPS
Similar Datasets
Project description:Bacterial superatant of Paraburkholderia tuberum was injected to LC-(+)ESI-MS/MS analysis with and without spiking of Fe(III). Apo-siderophores and Fe-siderophore complexes were observed.
| MSV000095895 | MassIVE
Project description:Siderophores are specialized molecules with different chemical structures, produced by bacteria and fungi to scavenge iron from the environment, a crucial nutrient for their growth and metabolism. These iron-chelating compounds enable bacteria to overcome iron limitation, a key factor in microbial survival and pathogenesis. Catecholate-type siderophores are primarily produced by bacteria, while hydroxamates are predominantly produced by fungi. The capacity of nine hydroxamate-type siderophores produced by fungi to serve as siderophores for iron acquisition by Pseudomonas aeruginosa, a human pathogen, has been investigated. Growth assays under iron limitation and 55Fe incorporation tests clearly highlighted that all nine siderophores promoted bacterial growth and facilitated iron transport. Additionally, the study aimed to identify the TonB-dependent transporters (TBDTs) responsible for iron import mediated by the tested siderophores. Mutant strains lacking genes encoding TBDTs were employed, revealing that iron is imported into P. aeruginosa cells solely by FpvB for the siderophores coprogen, triacetylfusarinine C, fusigen, ferrirhodin, and ferrirubin siderophores. Iron complexed by desferioxamine G is imported by two TBDTs, FpvB and FoxA. Ferricrocin-Fe and ferrichrycin-Fe complexes are imported by FpvB and FiuA. Lastly, rhodotorulic acid-Fe complexes are imported by FpvB, FiuA, and another unidentified TBDT. In conclusion, the data illustrate the effectiveness of hydroxamate-type siderophores in transporting iron into P. aeruginosa cells and provide insights into the intricate molecular mechanisms involved in iron acquisition, which have implications for understanding bacterial pathogenesis and developing potential therapeutic strategies.
2024-08-26 | PXD052483 | Pride
Project description:This project tested if siderophores are publig goods in Pseudomonas, and involved resequencing a well used siderophore mutant made by non-specific mutagenesis techniques
| PRJEB17787 | ENA
Project description:Bacteria access iron, a key nutrient, by producing siderophores or using siderophores produced by other microorganisms. The pathogen Pseudomonas aeruginosa produces two siderophores but is also able to pirate enterobactin (ENT), the siderophore produced by Escherichia coli. ENT-Fe complexes are imported across the outer membranes of P. aeruginosa by the two-outer membrane transporters PfeA and PirA. Iron is released from ENT in the P. aeruginosa periplasm by hydrolysis of ENT by the esterase PfeE. We show here that pfeE gene deletion renders P. aeruginosa unable to grow in the presence of ENT because it is unable to access iron via this siderophore. Two-species co-culture under iron-restricted conditions show that P. aeruginosa strongly represses the growth of E. coli as long it is able to produce its own siderophores. Both strains are present in similar proportions in the culture as long as the siderophore-deficient P. aeruginosa strain is able to use ENT produced by E. coli to access iron. If pfeE is deleted, E. coli has the upper hand in the culture and P. aeruginosa growth is repressed. Overall, these data show that PfeE is the Achilles heel of P. aeruginosa in communities with bacteria producing ENT.
2021-04-29 | PXD023712 | Pride
Project description:Iron is an essential nutrient for the opportunistic pathogen Pseudomonas aeruginosa, as for almost all living organisms. To access this element, the pathogen is able to express at least 15 different iron-uptake pathways, the vast majority involving small iron chelators called siderophores. Indeed, P. aeruginosa produces two siderophores, pyoverdine and pyochelin, but can also use many produced by other microorganisms. This implies that the bacterium expresses appropriate TonB-dependent transporters (TBDTs) at the outer membrane to import the ferric form of each of the siderophores used. These transporters are highly selective for a given ferri-siderophore complex or for siderophores with similar chemical structures. Here, we show that P. aeruginosa can also use rhizoferrin, staphyloferrin A, aerobactin, and schizokinen as siderophores to access iron. Growth assays in iron-restricted conditions and 55Fe uptake assays showed that the two alpha-carboxylate type siderophores rhizoferrin-Fe and staphyloferrin A-Fe are transported into P. aeruginosa cells by the TBDT ActA (PA3268). Among the mixed alpha-carboxylate/hydroxamate type siderophores, we found aerobactin-Fe to be transported by ChtA (as previously described) and schizokinen-Fe by ChtA and another unidentified TBDT.
2023-09-21 | PXD043056 | Pride
Project description:<p>High-affinity iron (Fe) scavenging compounds, or siderophores, are widely employed by soil bacteria to survive scarcity in bioavailable Fe. Siderophore biosynthesis relies on cellular carbon metabolism, despite reported decrease in both carbon uptake and Fe-containing metabolic proteins in Fe-deficient cells. Given this paradox, the metabolic network required to sustain the Fe-scavenging strategy is poorly understood. Here, through multiple <sup>13</sup>C-metabolomics experiments with Fe-replete and Fe-limited cells, we uncover how soil <em>Pseudomonas</em> species reprogram their metabolic pathways to prioritize siderophore biosynthesis. Across the three species investigated (<em>Pseudomonas putida</em> KT2440, <em>Pseudomonas protegens</em> Pf-5, and <em>Pseudomonas putida</em> S12), siderophore secretion is higher during growth on gluconeogenic substrates than during growth on glycolytic substrates. In response to Fe limitation, we capture decreased flux toward the tricarboxylic acid (TCA) cycle during the metabolism of glycolytic substrates but, due to carbon recycling to the TCA cycle via enhanced anaplerosis, the metabolism of gluconeogenic substrates results in an increase in both siderophore secretion (up to threefold) and Fe extraction (up to sixfold) from soil minerals. During simultaneous feeding on the different substrate types, Fe deficiency triggers a hierarchy in substrate utilization, which is facilitated by changes in protein abundances for substrate uptake and initial catabolism. Rerouted metabolism further promotes favorable fluxes in the TCA cycle and the gluconeogenesis-anaplerosis nodes, despite decrease in several proteins in these pathways, to meet carbon and energy demands for siderophore precursors in accordance with increased proteins for siderophore biosynthesis. Hierarchical carbon metabolism thus serves as a critical survival strategy during the metal nutrient deficiency.</p><p><br></p><p><strong>Data availability:</strong></p><p>The proteomics data have been deposited into the ProteomeXchange Consortium via the PRIDE partner repository with the data set identifier <a href='https://www.ebi.ac.uk/pride/archive/projects/PXD013605' rel='noopener noreferrer' target='_blank'>PXD013605</a>.</p>
2020-12-05 | MTBLS1715 | MetaboLights
Project description:Iron is an essential nutrient for bacterial growth but poorly bioavailable. To scavenge ferric iron present in their environment, bacteria synthesize and secrete siderophores, small compounds with a high affinity for iron. Pyochelin (PCH) is one of the two siderophores produced by the opportunistic pathogen Pseudomonas aeruginosa. Once having captured a ferric iron, PCH-Fe is imported back into bacteria first by the outer membrane transporter FptA and afterwards by the inner membrane permease FptX. Here using molecular biology, 55Fe uptake assays and LC-MS/MS quantification of PCH in the different bacterial cell fractions, we show that (i) PCH (probably under its PCH-Fe form) is able to rich bacterial periplasm and cytoplasm when both FptA and FptX are expressed, and (ii) that PchHI (a heterodimeric ABC transporter) plays a role in the translocation of siderophore-free iron siderophore-free iron across the inner membrane into the cytoplasm. Consequently, probably the first fraction of PCH-Fe internalized by FptA may be transported further by FptX in the bacterial cytoplasm to activate the transcriptional regulator PchR, regulating the transcription of all genes of the PCH pathway. The further fractions of PCH-Fe transported by FptA may dissociate in the bacterial periplasm by an unknown mechanism, with the siderophore-free iron being transported into the cytoplasm by PchHI.
2022-03-15 | PXD026833 | Pride
Project description:The development of new antibiotics against Gram-negative bacteria has to deal with the low permeability of the outer membrane. This obstacle can be overcome by utilizing siderophore-dependent iron uptake pathways as gates for antibiotic uptake. Iron-chelating siderophores are actively imported by bacteria, and their conjugation to antibiotics allows smuggling the latter into bacterial cells. Synthetic siderophore mimetics based on MECAM and DOTAM cores, both chelating iron via catechol groups, have been recently applied as versatile carriers of functional cargo. In the present study, we show that MECAM and the MECAM-ampicillin conjugate 3 transport iron into Pseudomonas aeruginosa cells via the catechol-type outer membrane transporters PfeA and PirA, and DOTAM solely via PirA. Differential proteomics and RTqPCR showed that MECAM import induced the expression of pfeA, whereas 3 led to an increase in the expression of pfeA and ampc, a gene conferring ampicillin resistance. The presence of DOTAM did not induce the expression of pirA, but upregulated the expression two zinc transporters (cntO and PA0781), pointing out that bacteria become zinc starved in the presence of this compound. Kinetic experiments with radioactive 55Fe demonstrated that iron uptake was as efficient as with the natural prototype siderophore enterobactin. The study provides a mechanistic and functional validation for DOTAM- and MECAM-based artificial siderophore mimetics as vehicles for the delivery of cargo into Gram-negative bacteria.
2022-10-28 | PXD031065 | Pride
Project description:Iron deficiency is a yield-limiting factor and a worldwide problem for crop production in many agricultural regions, particularly in aerobic and calcareous soils. Graminaceous species, like maize, improve Fe acquisition through the release of phytosiderophores (PS) into the rhizosphere and the following uptake of Fe(III)-PS complexes through specific transporters. Transcriptional profile obtained by roots 12-d-old maize plants under Fe starvation for 1 week (Fe-deficient; 19-d-old plants) were compared with the transcriptional profile obtained by roots of 12-d-old maize plants grown in a nutrient solution containing 100 μM Fe-EDTA for 1 week (Fe-sufficient; 19-d-old plants).
2017-06-12 | GSE76829 | GEO
Project description:The plant pathogen Dickeya chrysanthemi EC16 (formerly known as Petrobacterium chrysanthemi EC16 and Erwinia chrysanthemi EC16) was found to produce a new triscatecholamide siderophore, cyclic trichrysobactin, the related catecholamide compounds, linear trichrysobactin and dichrysobactin, and the previously reported monomeric siderophore unit, chrysobactin. Chrysobactin is comprised of L-serine, D-lysine, and 2,3-dihydroxybenzoic acid (DHBA). Trichrysobactin is a cyclic trimer of chrysobactin joined by a triserine lactone backbone. The chirality of the ferric complex of cyclic trichrysobactin is found to be in the ? configuration, similar to Fe(III)-bacillibactin, which contains a glycine spacer between the DHBA and L-threonine components and is opposite that of Fe(III)-enterobactin, which contains DHBA ligated directly to L-serine.
| S-EPMC3126860 | biostudies-literature