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ABSTRACT: Micro Ferric Citrate

PROVIDER: PRJNA635162 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11851754.fastq.gz	Fastqsanger.gz
	SRR11851755.fastq.gz	Fastqsanger.gz
	SRR11851756.fastq.gz	Fastqsanger.gz
	SRR11851757.fastq.gz	Fastqsanger.gz

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Ferric Citrate Uptake is a Virulence Factor in Uropathogenic Escherichia coli

Project description:More than half of women will experience a urinary tract infection (UTI) with uropathogenic Escherichia coli (UPEC) causing ~80% of uncomplicated cases. Iron acquisition systems are essential for uropathogenesis, and UPEC encode functionally redundant iron acquisition systems, underlining their importance. However, a recent UPEC clinical isolate, HM7 lacks this functional redundancy and instead encodes a sole siderophore, enterobactin. To determine if E. coli HM7 possesses unidentified iron acquisition systems, we performed RNA-sequencing under iron-limiting conditions and demonstrated the ferric citrate uptake system (fecABCDE and fecIR) was highly upregulated. Importantly, there are high levels of citrate within urine, some of which is bound to iron, and the fec system is highly enriched in UPEC isolates compared to commensal or fecal strains. Therefore, we hypothesized that HM7 and other similar strains use the fec system to acquire iron in the host. Deletion of both enterobactin biosynthesis and ferric citrate uptake (ΔentB/ΔfecA) abrogates use of ferric citrate as an iron source and fecA provides an advantage in pooled human urine in absence of enterobactin. However, in a UTI mouse model, fecA is a fitness factor independent of enterobactin production, likely due to the action of host Lipocalin-2 chelating ferrienterobactin. These findings indicate that ferric citrate uptake is used as an iron source when siderophore efficacy is limited, such as in the host during UTI. Defining these novel compensatory mechanisms and understanding the nutritional hierarchy of preferred iron sources within the urinary tract are important in the search for new approaches to combat UTI.

2021-11-06 | GSE188170 | GEO

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Project description:We report the RNA-seq based analyses of the transcriptional changes in the Aedes aegypti midguts transcriptome 24,48 hours after blood feeding with or without 250 um ferric ammonium citrate.

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Adaptation of Geobacter sulfurreducens to Overcome the Loss of a Key Periplasmic c-Type Cytochrome

Project description:ppcA is a member of a family of small, periplamic c-type cytochromes in Geobact sulfurreducens. The ppcA mutant displays displays a growth defect on ferric citrate medium, but the mutant has been adapted to grow to near wild-type levels on ferric citrate. The aim of this study was to elucidate gene expression changes responsible for this adaptive growth. Keywords: cell type comparison Three biological replicates were hybridized in duplicate on 12K Combimatrix sense-detecting arrays, the experiment (ppcA mutant) was labeled with Cy5, and the control (wildtype) was labeled with Cy3.

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Ferric Citrate Uptake is a Virulence Factor in Uropathogenic Escherichia coli

Project description:Ferric Citrate Uptake is a Virulence Factor in Uropathogenic Escherichia coli

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Escherichia coli S2P family intramembrane protease RseP is engaged in the regulated sequential cleavages of FecR in the ferric citrate signaling

Project description:Escherichia coli RseP, a member of the S2P family intramembrane proteases, is involved in the activation of the σE extracytoplasmic stress response and the elimination of remnant signal peptides. It remains however unclear whether RseP has additional cellular functions. In this study, we attempted to identify new RseP substrates to explore still unknown physiological roles of this protease. Our mass spectrometry-based quantitative proteomic analysis revealed that the levels of the several Fec system proteins encoded by the fecABCDE operon (fec operon) were significantly decreased in an RseP-deficient strain. The Fec system is responsible for the uptake of ferric citrate, and the transcription of the fec operon is controlled by FecI, an alternative sigma factor, and its regulator FecR, a single-pass transmembrane protein. The assays with the fec operon expression reporter demonstrated that the proteolytic activity of RseP is essential for the ferric citrate-dependent up-regulation of the fec operon. Analysis using the FecR protein and FecR-derived model proteins showed that FecR undergoes sequential processing at the membrane and that RseP participates in the last step of this sequential processing to generate the N-terminal cytoplasmic fragment of FecR that acts in transcription of the fec operon with FecI. Ferric citrate signal-dependent generation of this cleavage product is the essential and sufficient role of RseP in the transcriptional activation of the fec operon. Our study unveiled a novel physiological role of E. coli RseP, intramembrane proteolysis of FecR, which is essential for the regulation of iron uptake by the ferric citrate transport system.

2021-04-14 | PXD023797 | JPOST Repository

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