Disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, haemin and haemoglobin as iron sources The GenBank accession number for the sequence reported in this paper is AF087669.

Nicholson, Mary L.; Beall, Bernard

doi:10.1099/00221287-145-9-2453

Cited by 27 publications

(28 citation statements)

References 49 publications

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“…The growth yield of the tonB strain was decreased in iron-restricted medium lacking norepinephrine compared to those of the wild-type and complemented mutant strains. This result likely reflects the contribution of alcaligin-mediated acquisition of transferrin-iron to the growth of B. bronchiseptica, since ferric alcaligin transport is TonB dependent (39). Mutational analysis of putative TonB-dependent receptor genes.…”

Section: Resultsmentioning

confidence: 99%

Norepinephrine Mediates Acquisition of Transferrin-Iron in Bordetella bronchiseptica

Anderson

Armstrong

2008

J Bacteriol

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Previous research demonstrated that the sympathoadrenal catecholamine norepinephrine could promote the growth of Bordetella bronchiseptica in iron-restricted medium containing serum. In this study, norepinephrine was demonstrated to stimulate growth of this organism in the presence of partially iron-saturated transferrin but not lactoferrin. Although norepinephrine is known to induce transcription of the Bordetella bfeA enterobactin catechol xenosiderophore receptor gene, neither a bfeA mutant nor a bfeR regulator mutant was defective in growth responsiveness to norepinephrine. However, growth of a tonB mutant strain was not enhanced by norepinephrine, indicating that the response to this catecholamine was the result of high-affinity outer membrane transport. The B. bronchiseptica genome encodes a total of 19 known and predicted iron transport receptor genes, none of which, when mutated individually, were found to confer a defect in norepinephrinemediated growth stimulation in the presence of transferrin. Labeling experiments demonstrated a TonBdependent increase in cell-associated iron levels when bacteria grown in the presence of 55 Fe-transferrin were exposed to norepinephrine. In addition, TonB was required for maximum levels of cell-associated norepinephrine. Together, these results demonstrate that norepinephrine facilitates B. bronchiseptica iron acquisition from the iron carrier protein transferrin and this process may represent a mechanism by which some bacterial pathogens obtain this essential nutrient in the host environment.

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Section: Resultsmentioning

confidence: 99%

Norepinephrine Mediates Acquisition of Transferrin-Iron in Bordetella bronchiseptica

Anderson

Armstrong

2008

J Bacteriol

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“…Thus, it is likely that the siderophoremediated iron binding may function upstream of and provide free iron to the oxidase-permease iron uptake system. It has been reported that disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, hemin, and hemoglobin as iron sources (30). Thus, it is possible that the siderophore uptake mechanism is related to the use of hemoglobin iron by C. albicans.…”

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confidence: 99%

Characterization and Functional Analysis of the Siderophore-Iron Transporter CaArn1p in Candida albicans

Bai

Zheng

et al. 2002

Journal of Biological Chemistry

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Siderophores are small organic compounds with high affinity for ferric iron. Microorganisms commonly acquire iron via siderophore secretion and uptake. Here we report the characterization of the siderophore transporter CaArn1p in the fungal pathogen Candida albicans. Deletion of CaARN1 reduced the ability of C. albicans to use iron bound to the hydroxamate-type siderophore ferrichrome and abolished it when two high-affinity iron permease genes (CaFTR1 and CaFTR2) were also deleted, indicating a role of CaArn1p as well as the permeases in ferrichrome-iron uptake. Caarn1⌬ (but not Caftr1⌬Caftr2⌬) assimilated iron from another hydroxamate-type siderophore, ferrioxamine B, suggesting that iron uptake from this compound depends on the permeases, but not on CaArn1p. Northern blot analysis revealed that the transcription repressor CaTup1p repressed CaARN1 expression under iron-replete conditions via the DNA-binding protein Rfg1p. Green fluorescent protein-tagged CaArn1p was observed predominantly in the plasma membrane, with some in the cytoplasm as distinct spots. The number of these spots increased with the increase in ferrichrome concentration, suggesting that CaArn1p internalization might be a mechanism for ferrichrome-iron uptake or for recycling the transporter. Caarn1⌬ did not show reduced virulence when injected into the blood stream of mice, implying that CaArn1p is not required for iron uptake along this route of infection.

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“…In response to iron starvation, they produce the macrocyclic dihydroxamate siderophore alcaligin (15,53) and also use a variety of heterologous siderophores, including enterobactin (7), ferrichrome, and desferrioxamine B (6), for iron retrieval. These organisms can also obtain iron from host sources transferrin (60,61), lactoferrin (61), heme (1,55), and hemoglobin (55).…”

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confidence: 99%

The Bordetella bhu Locus Is Required for Heme Iron Utilization

2001

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Bordetella pertussis and Bordetella bronchiseptica are capable of obtaining iron from hemin and hemoglobin. Genes encoding a putative bacterial heme iron acquisition system (bhu, for Bordetella heme utilization) were identified in a B. pertussis genomic sequence database, and the corresponding DNA was isolated from a virulent strain of B. pertussis. A B. pertussis bhuR mutant, predicted to lack the heme outer membrane receptor, was generated by allelic exchange. In contrast to the wild-type strain, bhuR mutant PM5 was incapable of acquiring iron from hemin and hemoglobin; genetic complementation of PM5 with the cloned bhuRSTUV genes restored heme utilization to wild-type levels. In parallel studies, B. bronchiseptica bhu sequences were also identified and a B. bronchiseptica bhuR mutant was constructed and confirmed to be defective in heme iron acquisition. The wild-type B. bronchiseptica parent strain grown under low-iron conditions produced the presumptive BhuR protein, which was absent in the bhuR mutant. Furthermore, production of BhuR by iron-starved B. bronchiseptica was markedly enhanced by culture in hemin-supplemented medium, suggesting that these organisms sense and respond to heme in the environment. Analysis of the genetic region upstream of the bhu cluster identified open reading frames predicted to encode homologs of the Escherichia coli ferric citrate uptake regulators FecI and FecR. These putative Bordetella regulators may mediate heme-responsive positive transcriptional control of the bhu genes.

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Disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, haemin and haemoglobin as iron sources The GenBank accession number for the sequence reported in this paper is AF087669.

Cited by 27 publications

References 49 publications

Norepinephrine Mediates Acquisition of Transferrin-Iron in Bordetella bronchiseptica

Norepinephrine Mediates Acquisition of Transferrin-Iron in Bordetella bronchiseptica

Characterization and Functional Analysis of the Siderophore-Iron Transporter CaArn1p in Candida albicans

The Bordetella bhu Locus Is Required for Heme Iron Utilization

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