Purification and Structural Characterization of Siderophore (Corynebactin) from Corynebacterium diphtheriae

@article{Zajdowicz2012PurificationAS,
  title={Purification and Structural Characterization of Siderophore (Corynebactin) from Corynebacterium diphtheriae},
  author={Sheryl L. W. Zajdowicz and Jon C. Haller and Amy E. Krafft and Stephen W. Hunsucker and Colin T. Mant and Mark W Duncan and Robert S. Hodges and David N M Jones and Randall K. Holmes},
  journal={PLoS ONE},
  year={2012},
  volume={7}
}
During infection, Corynebacterium diphtheriae must compete with host iron-sequestering mechanisms for iron. C. diphtheriae can acquire iron by a siderophore-dependent iron-uptake pathway, by uptake and degradation of heme, or both. Previous studies showed that production of siderophore (corynebactin) by C. diphtheriae is repressed under high-iron growth conditions by the iron-activated diphtheria toxin repressor (DtxR) and that partially purified corynebactin fails to react in chemical assays… 

Figures and Tables from this paper

Structural and functional delineation of aerobactin biosynthesis in hypervirulent Klebsiella pneumoniae
TLDR
In vivo heterologous production and in vitro reconstitution of aerobactin biosynthesis from hvKP was carried out, demonstrating the specificity, stereoselectivity, and kinetic throughput of the complete pathway.
Iron Acquisition and Iron-Dependent Gene Expression in Corynebacterium diphtheriae
TLDR
The ability of bacterial pathogens to acquire iron during infection of mammalian hosts is often an essential component of the disease process and mechanisms for acquiring iron from the host environment are essential for survival.
Citryl ornithine is an intermediate in a three-step biosynthetic pathway for rhizoferrin in Francisella.
TLDR
These findings support a three-step pathway for rhizoferrin production in Francisella; unlike the fungus Rhizopus delemar, where putrescine functions as a primary precursor for rhizerin, biosynthesis in Francis Bella preferentially starts with ornithine as the substrate for FslA-mediated condensation with citrate.
Identification of zinc and Zur-regulated genes in Corynebacterium diphtheriae
TLDR
The identification of zinc-regulated ABC transporters herein will facilitate future studies to characterize zinc transport in C. diphtheriae and advance knowledge of changes to Zur-dependent global gene expression in response to zinc.
Alternative pathways utilize or circumvent putrescine for biosynthesis of putrescine-containing rhizoferrin
TLDR
A natural product biosynthetic workaround that evolved to bypass a missing precursor and re-establish it in the final structure is revealed, shown here in vitro that FigA synthesizes N- citrylornithine, and FigC is an N-citrylORNithine decarboxylase that together synthesize rhizoferrin without using putrescine.
Biotechnological Potential of Streptomyces Siderophores as New Antibiotics.
TLDR
The possibility of using siderophores conjugated with antibiotics could be an alternative to overcome bacterial resistance to drugs and could improve their therapeutic efficacy.
Iron and Virulence in Francisella tularensis
TLDR
Current knowledge of iron acquisition in this organism is summarized and the critical role of these uptake systems in bacterial pathogenicity is summarized.
Ribonuclease J-Mediated mRNA Turnover Modulates Cell Shape, Metabolism and Virulence in Corynebacterium diphtheriae
TLDR
It is reported that C. diphtheriae DIP1463 encodes a predicted RnJ homolog, comprised of a conserved N-terminal β-lactamase domain, followed by β-CASP and C- terminal domains, which influences the expression of numerous factors vital to corynebacterial cell physiology and virulence.
Biosynthetic considerations of triscatechol siderophores framed on serine and threonine macrolactone scaffolds.
TLDR
The current understanding of the biosyntheses of the siderophores of enterobactin variants are summarized, placing them in contrast with the well-established biosynthesis of enterOBactin.
...
...

References

SHOWING 1-10 OF 61 REFERENCES
Siderophore-mediated iron transport in Bacillus subtilis and Corynebacterium glutamicum
Hexadentate bacillibactin is the siderophore of Bacillus subtilis and is structurally similar to the better known enterobactin of Gram-negative bacteria such as Escherichia coli. Although both are
Initial characterization of the ferric iron transport system of Corynebacterium diphtheriae.
TLDR
Strong inhibition of uptake by carbonyl cyanide m-chlorophenylhydrazone was consistent with the electrochemical proton gradient as the major energy source for iron transport, and inhibition by Hg2+ indicated that sulfhydryl groups were also important.
Analysis of a DtxR-Regulated Iron Transport and Siderophore Biosynthesis Gene Cluster in Corynebacterium diphtheriae
TLDR
A genetic locus associated with siderophore biosynthesis and transport in Corynebacterium diphtheriae is described, which demonstrated that expression of ciuA and ciuE is DtxR and iron regulated, and DNase I protection experiments confirmed the presence of D txR binding sites upstream from each of these genes.
Erwinia chrysanthemi requires a second iron transport route dependent of the siderophore achromobactin for extracellular growth and plant infection
TLDR
Interestingly, iron transport mediated by achromobactin or a closely related siderophore probably exists in other phytopathogenic bacterial species such as Pseudomonas syringae.
Characterization of staphyloferrin A biosynthetic and transport mutants in Staphylococcus aureus
TLDR
It is provided here that HtsABC, along with the FhuC ATPase, is required for the uptake of staphyloferrin A, a polycarboxylate siderophore, and crystal structure of apo‐HtsA was determined and identified a large positively charged region in the substrate‐binding pocket, in agreement with a role in binding of anionic staphylloferrins A.
Staphyloferrin A: a structurally new siderophore from staphylococci.
TLDR
DL-[5-14C]ornithine was incorporated into staphyloferrin A, demonstrating that ornithine is an intermediate in staphylloferrIn A biosynthesis.
Rhizoferrin: a complexone type siderophore of the Mucorales and entomophthorales (Zygomycetes).
TLDR
Evidence is presented that rhizoferrin, a novel polycarboxylate or complexone-type siderophore, originally isolated from Rhizopus microsporus, represents the common siderophile within the Zygomycetes, and could be detected by HPLC analysis in various families of the Mucorales.
Alpha-keto acids are novel siderophores in the genera Proteus, Providencia, and Morganella and are produced by amino acid deaminases
TLDR
The view that specific iron-carboxylate transport systems have evolved in members of the tribe Proteeae and are designed to recognize ferric complexes of both alpha-hydroxy acids and alpha-keto acids, of which the latter can easily be generated by L-amino acid deaminases in an amino acid-rich medium is supported.
...
...