ArticleInfection and immunity2002
BhuR, a virulence-associated outer membrane protein of Bordetella avium, is required for the acquisition of iron from heme and hemoproteins.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Reduced and Nonreduced Genomes inmSystems · 2022Article
- Transcriptional and posttranscriptional regulation of Shigella shuT in response to host-associated iron availability and temperature.MicrobiologyOpen · 2017Article
- Involvement of Iron-Containing Proteins in Genome Integrity in Arabidopsis Thaliana.Genome integrity · 2015Review
- RNA-mediated thermoregulation of iron-acquisition genes in Shigella dysenteriae and pathogenic Escherichia coli.PloS one · 2013Article
- Comprehensive antigen screening identifies Moraxella catarrhalis proteins that induce protection in a mouse pulmonary clearance model.PloS one · 2013Article
- Expression of BfrH, a putative siderophore receptor of Bordetella bronchiseptica, is regulated by iron, Fur1, and the extracellular function sigma factor EcfI.Infection and immunity · 2010Article
- Temporal signaling and differential expression of Bordetella iron transport systems: the role of ferrimones and positive regulators.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2009Review
- The heme sensor system of Staphylococcus aureus.Contributions to microbiology · 2009Review
- Function, regulation, and transcriptional organization of the hemin utilization locus of Bartonella quintana.Infection and immunity · 2009Article
- Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus.The Journal of biological chemistry · 2008Article
- Brucella abortus requires the heme transporter BhuA for maintenance of chronic infection in BALB/c mice.Infection and immunity · 2007Article
- Passively released heme from hemoglobin and myoglobin is a potential source of nutrient iron for Bordetella bronchiseptica.Infection and immunity · 2007Article
- Characterization of a highly conserved island in the otherwise divergent Bordetella holmesii and Bordetella pertussis genomes.Journal of bacteriology · 2006Article
- Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction.Journal of bacteriology · 2006Article
- Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity.Journal of bacteriology · 2005Article
- Transcriptional control of the rhuIR-bhuRSTUV heme acquisition locus in Bordetella avium.Infection and immunity · 2005Article
- RhuR, an extracytoplasmic function sigma factor activator, is essential for heme-dependent expression of the outer membrane heme and hemoprotein receptor of Bordetella avium.Infection and immunity · 2004Article
- Integration of environmental signals controls expression of Bordetella heme utilization genes.Journal of bacteriology · 2004Article
- Heme-responsive transcriptional activation of Bordetella bhu genes.Journal of bacteriology · 2003Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Iron (Fe) is an essential element for most organisms which must be obtained from the local environment. In the case of pathogenic bacteria, this fundamental element must be acquired from the fluids and tissues of the infected host. A variety of systems have evolved in bacteria for efficient acquisition of host-bound Fe. The gram-negative bacterium Bordetella avium, upon colonization of the avian upper respiratory tract, produces a disease in birds that has striking similarity to whooping cough, a disease caused by the obligate human pathogen Bordetella pertussis. We describe a B. avium Fe utilization locus comprised of bhuR and six accessory genes (rhuIR and bhuSTUV). Genetic manipulations of B. avium confirmed that bhuR, which encodes a putative outer membrane heme receptor, mediates efficient acquisition of Fe from hemin and hemoproteins (hemoglobin, myoglobin, and catalase). BhuR contains motifs which are common to bacterial heme receptors, including a consensus FRAP domain, an NPNL domain, and two TonB boxes. An N-terminal 32-amino-acid segment, putatively required for rhuIR-dependent regulated expression of bhuR, is present in BhuR but not in other bacterial heme receptors. Two forms of BhuR were observed in the outer membrane of B. avium: a 91-kDa polypeptide consistent in size with the predicted mature protein and a smaller 82-kDa polypeptide which lacks the 104 amino acids found at the N terminus of the 91-kDa form. A mutation in hemA was engineered in B. avium to demonstrate that the bacterium transports heme into the cytoplasm in a BhuR-dependent manner. The role of BhuR in virulence was established in turkey poults by use of a competitive-infection model.
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