Evidence map›Paper›PMID 22458330›Full record

ArticleMolecular microbiology2012

Involvement of multiple distinct Bordetella receptor proteins in the utilization of iron liberated from transferrin by host catecholamine stress hormones.

Sandra K Armstrong, Timothy J Brickman, Ryan J Suhadolc

Abstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Norepinephrine derepresses the Fur regulon ofJournal of bacteriology · 2026
    Article
  2. Article
  3. Frontiers in cellular and infection microbiology · 2023
    Article
  4. Review
  5. Article
  6. Review
  7. DisruptingMicroorganisms · 2020
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Sandra K ArmstrongDepartment of Microbiology, University of Minnesota Medical School, 925 Mayo Memorial Building, 420 Delaware Street, S.E., Minneapolis, MN 55455-0312, USA. armst018@umn.edu
Timothy J Brickman
Ryan J Suhadolc
University of Minnesota · USUniversity of Minnesota Medical Center · US

Funding

IRON ACQUISITION IN BORDETELLA PERTUSSISR01AI031088 · NIAID · UNIVERSITY OF MINNESOTA TWIN CITIES · PI ARMSTRONG, SANDRA KAY · 1998 to 2014
$3.2M
Iron acquistion in Bordetella pertussisR21AI031088 · NIAID · UNIVERSITY OF MINNESOTA TWIN CITIES · PI ARMSTRONG, SANDRA KAY · 2003 to 2003
$221k
IRON ACQUISITION IN BORDETELLA PERTUSSISR29AI031088 · NIAID · EAST CAROLINA UNIVERSITY · PI ARMSTRONG, SANDRA KAY · 1991 to 1995
–
NIAID NIH HHS AI-31088NIAID NIH HHS R01 AI031088NIAID NIH HHS R21 AI031088
6 · The paper itself

Abstract

Bordetella bronchiseptica is a pathogen that can acquire iron using its native alcaligin siderophore system, but can also use the catechol xenosiderophore enterobactin via the BfeA outer membrane receptor. Transcription of bfeA is positively controlled by a regulator that requires induction by enterobactin. Catecholamine hormones also induce bfeA transcription and B. bronchiseptica can use the catecholamine noradrenaline for growth on transferrin. In this study, B. bronchiseptica was shown to use catecholamines to obtain iron from both transferrin and lactoferrin in the absence of siderophore. In the presence of siderophore, noradrenaline augmented transferrin utilization by B. bronchiseptica, as well as siderophore function in vitro. Genetic analysis identified BfrA, BfrD and BfrE as TonB-dependent outer membrane catecholamine receptors. The BfeA enterobactin receptor was found to not be involved directly in catecholamine utilization; however, the BfrA, BfrD and BfrE catecholamine receptors could serve as receptors for enterobactin and its degradation product 2,3-dihydroxybenzoic acid. Thus, there is a functional link between enterobactin-dependent and catecholamine-dependent transferrin utilization. This investigation characterizes a new B. bronchiseptica mechanism for iron uptake from transferrin that uses host stress hormones that not only deliver iron directly to catecholamine receptors, but also potentiate siderophore activity by acting as iron shuttles.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsBordetella bronchisepticaBordetella InfectionsCatecholaminesHormonesHost-Pathogen InteractionsHumansIronLactoferrinMembrane ProteinsReceptors, CatecholamineSiderophoresTransferrinBacterial Outer Membrane ProteinsBacterial ProteinsCatecholaminesHormonesIronLactoferrinMembrane ProteinsReceptors, CatecholamineSiderophorestonB protein, BacteriaTransferrin

Identifiers

PMID22458330
PMCPMC3331950
OpenAlexW1893316466

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.