Iron Uptake Mechanism in Ferritin from Helicobacter pylori

2015 ◽  
pp. 238-249
Keyword(s):  
Helicobacter Pylori ◽  
Iron Uptake ◽  
Uptake Mechanism

A new mechanism for membrane iron transport in Pseudomonas aeruginosa

2002 ◽  
Vol 30 (4) ◽  
pp. 702-705 ◽  
Author(s):  
I.J. Schalk ◽  
M. A. Abdallah ◽  
F. Pattus
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Iron Uptake ◽  
Iron Transport ◽  
Membrane Receptor ◽  
Gram Negative Bacteria ◽  
Outer Membrane Receptor ◽  
Uptake Mechanism ◽  
Atp Binding Cassette Transporter ◽  
Biophysical Studies

Various biochemical and biophysical studies have demonstrated the existence of a novel iron-uptake mechanism in Pseudomonas aeruginosa, different from that generally described for ferrichrome and ferric-enterobactin in Escherichia coli. This new iron-uptake mechanism involves all the proteins generally reported to be involved in the uptake of ferric-siderophore complexes in Gram-negative bacteria (i.e. the outer membrane receptor, periplasmic binding protein and ATP-binding-cassette transporter), but differs in the behaviour of the siderophore. One of the key features of this process is the binding of iron-free pyoverdin to the outer membrane receptor FpvA in conditions of iron deficiency.

scholarly journals Is there a strategy I iron uptake mechanism in maize?

2018 ◽  
Vol 13 (4) ◽  
pp. e1161877 ◽  
Author(s):  
Suzhen Li ◽  
Xiaojin Zhou ◽  
Jingtang Chen ◽  
Rumei Chen
Keyword(s):  
Iron Uptake ◽  
Uptake Mechanism ◽  
Strategy I

Investigation of iron pools in cucumber roots by Mössbauer spectroscopy: direct evidence for the Strategy I iron uptake mechanism

Planta ◽  
2008 ◽  
Vol 229 (2) ◽  
pp. 271-278 ◽  
Author(s):  
Krisztina Kovács ◽  
Ernő Kuzmann ◽  
Enikő Tatár ◽  
Attila Vértes ◽  
Ferenc Fodor
Keyword(s):  
Mössbauer Spectroscopy ◽  
Iron Uptake ◽  
Direct Evidence ◽  
Mossbauer Spectroscopy ◽  
Uptake Mechanism ◽  
Mößbauer Spectroscopy ◽  
Cucumber Roots ◽  
Strategy I

ColV Plasmid-Mediated, Colicin V-Independent Iron Uptake System of Invasive Strains of Escherichia coli

1980 ◽  
Vol 29 (2) ◽  
pp. 411-416
Author(s):  
Peter H. Williams ◽  
Philip J. Warner
Keyword(s):  
Escherichia Coli ◽  
Iron Uptake ◽  
Chelating Agent ◽  
Uptake System ◽  
Uptake Mechanism ◽  
E Coli ◽  
Marked Enhancement ◽  
Bacterial Cell Membrane ◽  
Colicin V ◽  
K 12

Evidence is presented that ColV plasmid-mediated iron uptake, an important component of the virulence of invasive strains of Escherichia coli , is independent of colicin V synthesis and activity. A mutant of E. coli K-12 deficient in the biosynthesis of enterochelin (strain AN1937) was unable to grow on minimal agar containing the chelating agent α,α′-dipyridyl unless it was harboring the plasmid ColV-K30 (strain LG1315). Acquisition of the active plasmid-specified iron sequestering system was accompanied by marked enhancement of pathogenicity in experimental infections of mice. Mutants of strain LG1315 were isolated that were defective in iron uptake due to plasmid mutations. They were unchanged with respect to colicin production, but were significantly less virulent than the parent strain. Conversely, mutants isolated as defective in colicin V synthesis were normal for the plasmid-coded iron uptake mechanism and showed the same lethality for infected mice as did strain LG1315. Furthermore, mutations in strain AN1937 which render it resistant or tolerant to the bactericidal action of colicin V did not influence the uptake of iron into plasmid-carrying strains. Cross-feeding tests involving plasmid mutants defective in iron uptake identified two plasmid-specified components of the system, an extracellular iron-chelating compound and a nondiffusible product allowing transport of iron across the bacterial cell membrane.

Iron-Uptake System for the Antioxidant Ability of Helicobacter pylori Regulated by Ferric Uptake Regulator (FUR)

2011 ◽  
Vol 140 (5) ◽  
pp. S-468
Author(s):  
Hitoshi Tsugawa ◽  
Hidekazu Suzuki ◽  
Kenro Hirata ◽  
Juntaro Matsuzaki ◽  
Sawako Okada ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Iron Uptake ◽  
Uptake System ◽  
Ferric Uptake Regulator ◽  
Antioxidant Ability ◽  
Iron Uptake System

scholarly journals The fslE Homolog, FTL_0439 (fupA/B), Mediates Siderophore-Dependent Iron Uptake in Francisella tularensis LVS

2010 ◽  
Vol 78 (10) ◽  
pp. 4276-4285 ◽  
Author(s):  
Bhaswati Sen ◽  
Alexis Meeker ◽  
Girija Ramakrishnan
Keyword(s):  
Francisella Tularensis ◽  
Iron Uptake ◽  
Virulent Strain ◽  
Iron Acquisition ◽  
Iron Limitation ◽  
Growth Defect ◽  
Uptake Mechanism ◽  
Independent Mechanism ◽  
Intraperitoneal Infection ◽  
Schu S4

ABSTRACT The Gram-negative pathogen Francisella tularensis secretes a siderophore to obtain essential iron by a TonB-independent mechanism. The fslABCDE locus, encoding siderophore-related functions, is conserved among different Francisella strains. In the virulent strain Schu S4, fslE is essential for siderophore utilization and for growth under conditions of iron limitation. In contrast, we found that deletion of fslE did not affect siderophore utilization by the attenuated live vaccine strain (LVS). We found that one of the fslE paralogs encoded in the LVS genome, FTL_0439 (fupA/B), was able to partially complement a Schu S4 ΔfslE mutant for siderophore utilization. We generated a deletion of fupA/B in LVS and in the LVS ΔfslE background. The ΔfupA/B mutant showed reduced growth under conditions of iron limitation. It was able to secrete but was unable to utilize siderophore. Mutation of both fupA/B and fslE resulted in a growth defect of greater severity. The ΔfupA/B mutants showed a replication defect in J774.1A cells and decreased virulence following intraperitoneal infection in mice. Complementation of the ΔfupA/B mutation in cis restored the ability to utilize siderophore and concomitantly restored virulence. Our results indicate that fupA/B plays a significant role in the siderophore-mediated iron uptake mechanism of LVS whereas fslE appears to play a secondary role. Variation in iron acquisition mechanisms may contribute to virulence differences between the strains.

FeoB is not required for ferrous iron uptake inCampylobacter jejuni

2003 ◽  
Vol 49 (11) ◽  
pp. 727-731 ◽  
Author(s):  
Brian H Raphael ◽  
Lynn A Joens
Keyword(s):  
Escherichia Coli ◽  
Helicobacter Pylori ◽  
Campylobacter Jejuni ◽  
Ferrous Iron ◽  
Iron Uptake ◽  
No Reduction ◽  
Amino Acid Identity ◽  
Acid Identity ◽  
E Coli ◽  
Magnesium Transporter

Among strains of Campylobacter jejuni, levels of ferrous iron (Fe2+) uptake was comparable. However, C. jejuni showed a lower level of ferrous iron uptake than Escherichia coli. Consistent with studies of E. coli, Fe2+uptake in C. jejuni was significantly enhanced by low Mg2+concentration. The C. jejuni genome sequence contains a single known ferrous iron uptake gene, feoB, whose product shares 50% amino acid identity to Helicobacter pylori FeoB and 29% identity to E. coli FeoB. However, Fe2+uptake could not be attributed to FeoB for several reasons. Site-directed mutations in feoB caused no defect in55Fe2+uptake. Among C. jejuni strains, various nucleotide alterations were found in feoB, indicating that some C. jejuni feoB genes are defective. In addition, uptake could not be attributed to the magnesium transporter CorA, since no reduction in55Fe2+uptake was observed in the presence of a CorA-specific inhibitor.Key words: Campylobacter jejuni, ferrous iron uptake, metal transport, FeoB.

scholarly journals Design and Synthesis of a Siderophore-Based Fluorescent Probe and Its Application in Selective Detection of Aeromonas

2021 ◽  
Author(s):  
Javier Cisneros-Sureda ◽  
Diego Rey-Varela ◽  
Jaime Rodríguez ◽  
Miguel Balado ◽  
Manuel L. Lemos ◽  
...  
Keyword(s):  
Fluorescent Probe ◽  
Iron Uptake ◽  
Pathogenic Bacteria ◽  
Click Reaction ◽  
Growth Promotion ◽  
Fish Farming ◽  
Uptake Mechanism ◽  
Design And Synthesis ◽  
Selective Labelling ◽  
Sulforhodamine B

Abstract Amonabactins, the siderophores produced by some pathogenic bacteria belonging to Aeromonas genus, can be used for the preparation of conjugates that can be imported into the cell using their specific transport machinery. Herein, we report the design and synthesis of a new amonabactin-based fluorescent probe by conjugation of the appropiate amonabactin analogue to sulforhodamine B (AMB-SRB) using a thiol-maleimide click reaction. Growth promotion assays and fluorescence microscopy studies demonstrated that AMB-SRB fluorescent probe was able to label the fish pathogenic bacterium A. salmonicida subsp. salmonicida through its outer membrane transport (OMT) protein FstC. The labelling of other Aeromonas species such as the human pathogenic A. hydrophila, indicates that this probe can be a very useful molecular tool for studying the amonabactin-dependent iron uptake mechanism. Furthermore, the selective labelling of A. salmonicida and other Aeromonas species in presence of other fish pathogenic bacteria, suggest the potential application of this probe for detection of Aeromonas in water and other fish farming samples through fluorescence assays.

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