Norepinephrine Mediates Acquisition of Transferrin-Iron in
            <i>Bordetella bronchiseptica</i>

Anderson, Mark T.; Armstrong, Sandra K.

doi:10.1128/jb.00086-08

Cited by 54 publications

(68 citation statements)

References 58 publications

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“…Here we uncovered the molecular basis for an alternate mechanism for holotransferrin iron extraction, ob- served only in the absence of staphyloferrin production. This second mechanism capitalizes on the recently characterized phenomenon of holotransferrin iron liberation through complex formation with mammalian catecholamine stress hormones (2,5,10,19,54). Catecholamine iron was shown to promote the growth of Bacillus and E. coli on holotransferrin at concentrations comparable to those tested in this study (5,40).…”

Section: Discussionmentioning

confidence: 97%

“…Catecholamines interact with Fe(III) in transferrin and promote its reduction to Fe(II) (54), effectively removing iron from this important innate immune protein. As a result, catecholamine hormones have been shown to enhance growth of pathogenic bacteria in serum (2,19,39,54). It is also known that they can stimulate the growth of S. epidermidis on transferrin (36,46), although a similar effect was not noted for S. aureus (46).…”

Section: Fig 1 Growth Of S Aureusmentioning

confidence: 91%

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Staphylococcus aureus Transporters Hts, Sir, and Sst Capture Iron Liberated from Human Transferrin by Staphyloferrin A, Staphyloferrin B, and Catecholamine Stress Hormones, Respectively, and Contribute to Virulence

et al. 2011

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Staphylococcus aureus is a frequent cause of bloodstream, respiratory tract, and skin and soft tissue infections. In the bloodstream, the iron-binding glycoprotein transferrin circulates to provide iron to cells throughout the body, but its iron-binding properties make it an important component of innate immunity. It is well established that siderophores, with their high affinity for iron, in many instances can remove iron from transferrin as a means to promote proliferation of bacterial pathogens. It is also established that catecholamine hormones can interfere with the iron-binding properties of transferrin, thus allowing infectious bacteria access to this iron pool. The present study demonstrates that S. aureus can use either of two carboxylate-type siderophores, staphyloferrin A and staphyloferrin B, via the transporters Hts and Sir, respectively, to access the transferrin iron pool. Growth of staphyloferrin-producing S. aureus in serum or in the presence of holotransferrin was not enhanced in the presence of catecholamines. However, catecholamines significantly enhanced the growth of staphyloferrin-deficient S. aureus in human serum or in the presence of human holotransferrin. It was further demonstrated that the Sst transporter was essential for this activity as well as for the utilization of bacterial catechol siderophores. The substrate binding protein SstD was shown to interact with ferrated catecholamines and catechol siderophores, with low to submicromolar affinities. Experiments involving mice challenged intravenously with wild-type S. aureus and isogenic mutants demonstrated that the combination of Hts, Sir, and Sst transport systems was required for full virulence of S. aureus.

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Section: Discussionmentioning

confidence: 97%

Section: Fig 1 Growth Of S Aureusmentioning

confidence: 91%

Staphylococcus aureus Transporters Hts, Sir, and Sst Capture Iron Liberated from Human Transferrin by Staphyloferrin A, Staphyloferrin B, and Catecholamine Stress Hormones, Respectively, and Contribute to Virulence

et al. 2011

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“…After the PCR product was cloned into pGEM-T Easy, yielding pGEMLbtUHis, an EcoRI fragment containing lbtU::His 6 was excised and cloned into EcoRI-digested pMMB2002. The resultant plasmid, pLbtUHis 6 , had lbtU::His 6 cloned under the control of an IPTG-inducible Ptac promoter. Plasmid pLbtUHis 6 was electroporated into 130b and mutant NU383, and Cm r transformants were isolated on antibiotic-containing BCYE agar.…”

Section: Methodsmentioning

confidence: 99%

“…The resultant plasmid, pLbtUHis 6 , had lbtU::His 6 cloned under the control of an IPTG-inducible Ptac promoter. Plasmid pLbtUHis 6 was electroporated into 130b and mutant NU383, and Cm r transformants were isolated on antibiotic-containing BCYE agar.…”

Section: Methodsmentioning

confidence: 99%

Legionella pneumophila LbtU Acts as a Novel, TonB-Independent Receptor for the Legiobactin Siderophore

et al. 2011

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Gram-negative Legionella pneumophila produces a siderophore (legiobactin) that promotes lung infection. We previously determined that lbtA and lbtB are required for the synthesis and secretion of legiobactin. DNA sequence and reverse transcription-PCR (RT-PCR) analyses now reveal the presence of an iron-repressed gene (lbtU) directly upstream of the lbtAB-containing operon. In silico analysis predicted that LbtU is an outer membrane protein consisting of a 16-stranded transmembrane ␤-barrel, multiple extracellular domains, and short periplasmic tails. Immunoblot analysis of cell fractions confirmed an outer membrane location for LbtU. Although replicating normally in standard media, lbtU mutants, like lbtA mutants, were impaired for growth on iron-depleted agar media. While producing typical levels of legiobactin, lbtU mutants were unable to use supplied legiobactin to stimulate growth on iron-depleted media and displayed an inability to take up iron. Complemented lbtU mutants behaved as the wild type did. The lbtU mutants were also impaired for infection in a legiobactin-dependent manner. Together, these data indicate that LbtU is involved in the uptake of legiobactin and, based upon its location, is most likely the Legionella siderophore receptor. The sequence and predicted two-dimensional (2D) and 3D structures of LbtU were distinct from those of all known siderophore receptors, which generally contain a 22-stranded ␤-barrel and an extended N terminus that binds TonB in order to transduce energy from the inner membrane. This observation coupled with the fact that L. pneumophila does not encode TonB suggests that LbtU is a new type of receptor that participates in a form of iron uptake that is mechanistically distinct from the existing paradigm.

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“…Additionally, B. pertussis and B. bronchiseptica can use the xenosiderophores enterobactin (14), ferrichrome, and desferrioxamine B (13); B. bronchiseptica can also use aerobactin, ferrichrysin, ferricrocin, ferrirubin, protochelin, schizokinen, vicibactin, and pyoverdin (71). The three Bordetella species have from 14 to 19 predicted TonB-dependent receptormediated transport systems (5,66), but only the alcaligin, enterobactin, and heme utilization systems have been characterized to date. Expression of each of these systems is repressed by Fur and is also activated under iron starvation conditions by mechanisms involving dedicated positive regulators that require the cognate iron source as the inducer (3,16,23,87,88).…”

mentioning

confidence: 99%

Transcriptional Profiling of the Iron Starvation Response in Bordetella pertussis Provides New Insights into Siderophore Utilization and Virulence Gene Expression

et al. 2011

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Serological studies of patients with pertussis and the identification of antigenic Bordetella pertussis proteins support the hypothesis that B. pertussis perceives an iron starvation cue and expresses multiple iron source utilization systems in its natural human host environment. Furthermore, previous studies using a murine respiratory tract infection model showed that several of these B. pertussis iron systems are required for colonization and persistence and are differentially expressed over the course of infection. The present study examined genome-wide changes in B. pertussis gene transcript abundance in response to iron starvation in vitro. In addition to known iron source utilization genes, we identified a previously uncharacterized iron-repressed cytoplasmic membrane transporter system, fbpABC, that is required for the utilization of multiple structurally distinct siderophores including alcaligin, enterobactin, ferrichrome, and desferrioxamine B. Expression of type III secretion system genes was also found to be upregulated during iron starvation in both B. pertussis strain Tohama I and Bordetella bronchiseptica strain RB50. In a survey of type III secretion system protein production by an assortment of B. pertussis laboratory-adapted and low-passage clinical isolate strains, iron limitation increased the production and secretion of the type III secretion system-specific translocation apparatus tip protein Bsp22 in all Bvg-proficient strains. These results indicate that iron starvation in the infected host is an important environmental cue influencing not only Bordetella iron transport gene expression but also the expression of other important virulence-associated genes.

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Norepinephrine Mediates Acquisition of Transferrin-Iron in Bordetella bronchiseptica

Cited by 54 publications

References 58 publications

Staphylococcus aureus Transporters Hts, Sir, and Sst Capture Iron Liberated from Human Transferrin by Staphyloferrin A, Staphyloferrin B, and Catecholamine Stress Hormones, Respectively, and Contribute to Virulence

Staphylococcus aureus Transporters Hts, Sir, and Sst Capture Iron Liberated from Human Transferrin by Staphyloferrin A, Staphyloferrin B, and Catecholamine Stress Hormones, Respectively, and Contribute to Virulence

Legionella pneumophila LbtU Acts as a Novel, TonB-Independent Receptor for the Legiobactin Siderophore

Transcriptional Profiling of the Iron Starvation Response in Bordetella pertussis Provides New Insights into Siderophore Utilization and Virulence Gene Expression

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