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Growth promotion was tested using M. smegmatis wild type strain, an exochelin-deficient mutant, and M. fortuitum employing a broad variety of xenosiderophores including hydroxamates, catecholates and a-hydroxy carboxylic acids. The experiments revealed that utilization of siderophore-bound iron is substrate specific suggesting high-affinity siderophore receptor and transport systems. Concentration-dependent...
The outer membrane receptor for ferrioxamines (FoxA Erw ) of Erwinia herbicola (Pantoea agglomerans) was cloned from a cosmid gene bank and partially sequenced. A comparison of the partial amino acid sequence of FoxA with the amino acid sequence of FoxA Yer from Yersinia enterocolitica revealed a high sequence homology. A functional analysis of FoxA and FoxA receptors cloned into a Fhu-negative background...
From the culture medium of Ralstonia (formerly Burkholderia or Pseudomonas) pickettii DSM 6297 grown under iron-limited conditions an iron complexing compound (siderophore) could be isolated. The structure of the isolated polycarboxylate siderophore was determined by spectroscopic methods as S,S-rhizoferrin, the enantiomer of R,R-rhizoferrin produced by fungi (Zygomycetes). Transport experiments with...
Transport and metabolization of iron bound to the fungal siderophore rhizoferrin was analyzed by transport kinetics, Mössbauer and EPR spectroscopy. Saturation kinetics (vmax=24.4 pmol/(mg min), Km=64.4μM) and energy dependence excluded diffusion and provided evidence for a rhizoferrin transport system in M. smegmatis. Based on the spectroscopic techniques indications for intracellular presence...
While in fungi iron transport via hydroxamate siderophores has been amply proven, iron transport via enterobactin is largely unknown. Enterobactin is a catecholate-type siderophore produced by several enterobacterial genera grown in severe iron deprivation. By using the KanMX disruption module in vector pUG6 in a fet3Δ background of Saccharomyces cerevisiae we were able to disrupt the gene YOL158c Sce...
Uptake of iron complexes into the Gram-negative bacterial cell requires highly specific outer membrane receptors and specific ATP-dependent (ATP-Binding-Cassette (ABC)) transport systems located in the inner membrane. The latter type of import system is characterized by a periplasmic binding protein (BP), integral membrane proteins, and membrane-associated ATP-hydrolyzing proteins. In Gram-positive...
DMT1 has four names, transports as many as eight metals, may have four or more isoforms and carries out its transport for multiple purposes. This review is a start at sorting out these multiplicities. A G185R mutation results in diminished gastrointestinal iron uptake and decreased endosomal iron exit in microcytic mice and Belgrade rats. Comparison of mutant to normal rodents is one analytical tool...
Many gram-negative bacteria produce and excrete siderophores, which complex iron with high affinity in the environment. The ferric siderophore complexes are transported across the outer membrane by receptor proteins. This process requires energy and is TonB dependent and must involve conformational changes in the receptor proteins to allow the transport of the ferric siderophores from the extracellular...
The mechanism of TonB dependent siderophore uptake through outer membrane transporters in Gram-negative bacteria is poorly understood. In an effort to expand our knowledge of the interaction between TonB and the outer membrane transporters, we have cloned and expressed the FepA cork domain (11–154) from Salmonella typhimurium and characterized its interaction with the periplasmic C-terminal domain...
During recent years new systems involved in iron transport were identified in the old workhorse Escherichia coli (and in other enterobacteria). This came as a bit of a surprise because one might think transport of this essential trace element was already thoroughly studied. Moreover, it appears that iron homeostasis consists not only of uptake but also of efflux of this potentially toxic redox-active...
In Yersinia pestis, the Yfe and Feo systems likely function to transport ferrous iron. Both FeoA and FeoB are essential for iron acquisition activity while FeoC is not. Mutations in yfe and feo had an additive effect on microaerophilic growth under iron-chelating conditions. Y. pestis cells lacking the Ybt siderophore-dependent system, the Yfe or the Feo system grow normally in J774A.1 cells. However,...
The TonB system of Escherichia coli (and most other Gram-negative bacteria) is distinguished by its importance to iron acquisition, its contribution to bacterial pathogenesis, and a unique and mysterious mechanism of action. This system somehow gathers the potential energy of the cytoplasmic membrane (CM) proton gradient and delivers it to active transporters in the outer membrane (OM). Our understanding...
The fish pathogen Vibrio anguillarum is the causative agent of a fatal hemorrhagic septicemia in salmonid fish. Many serotype O1 strains harbors a 65 Kbp plasmid (pJM1 encoding an iron sequestering system essential for virulence. The genes involved in the biosynthesis of the indigenous siderophore anguibactin are encoded by both the pJM1 plasmid and the chromosome, while those involved in the transport...
TonB is a protein prevalent in a large number of Gram-negative bacteria that is believed to be responsible for the energy transduction component in the import of ferric iron complexes and vitamin B12 across the outer membrane. We have analyzed all the TonB proteins that are currently contained in the Entrez database and have identified nine different clusters based on its conserved 90-residue C-terminal...
The transferrins are a family of proteins that bind free iron in the blood and bodily fluids. Serum transferrins function to deliver iron to cells via a receptor-mediated endocytotic process as well as to remove toxic free iron from the blood and to provide an anti-bacterial, low-iron environment. Lactoferrins (found in bodily secretions such as milk) are only known to have an anti-bacterial function,...
Shigella spp. have transport systems for both ferric and ferrous iron. The iron can be taken up as free iron or complexed to a variety of carriers. All Shigella species have both the Feo and Sit systems for acquisition of ferrous iron, and all have at least one siderophore-mediated system for transport of ferric iron. Several of the transport systems, including Sit, Iuc/IutA (aerobactin synthesis...
TtpC is a fourth required protein in the TonB2 energy transduction system in Vibrio anguillarum. TtpC is necessary for iron transport mediated by the TonB2 system and is highly conserved in all pathogenic vibrio species studied to date as well as several marine organisms. We show here that the TtpC proteins from selected pathogenic vibrio species can function with the TonB2 system of V. anguillarum...
The mechanism of iron transport in Francisella is still a puzzle since none of the sequenced Francisella strains appears to encode a TonB protein, the energy transducer of the proton motive force necessary to act on the bacterial outer membrane siderophore receptor to allow the internalization of iron. In this work we demonstrate using kinetic experiments of radioactive Fe3+ utilization, that iron...
The viability of iron(III/II) reduction as the initial step in the in vivo release of iron from its thermodynamically stable siderophore complex is explored.
The recent rise in drug resistance found amongst community acquired infections has sparked renewed interest in developing antimicrobial agents that target resistant organisms and limit the natural selection of immune variants. Recent discoveries have shown that iron uptake systems in bacteria and fungi are suitable targets for developing such therapeutic agents. The use of siderophore-drug conjugates...
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