Evidence map›Paper›PMID 20086155›Full record

ArticleAntimicrobial agents and chemotherapy2010

Neutrophil gelatinase-associated lipocalin expresses antimicrobial activity by interfering with L-norepinephrine-mediated bacterial iron acquisition.

Marcus Miethke, Arne Skerra

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 75 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Engineered Tissue Models to Decode Host-Microbiota Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  10. The Hunger Games:Frontiers in immunology · 2021
    Article
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  14. Interkingdom Cross-Talk in Times of Stress:Frontiers in immunology · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Review
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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

2 authors at 2 institutions in 1 country.

Marcus MiethkeMunich Center for Integrated Protein Science, CIPS-M, Lehrstuhl für Biologische Chemie, Technische Universität München, 85350 Freising-Weihenstephan, Germany.
Arne Skerra
Center for Integrated Protein Science Munich · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

l-norepinephrine (NE) is a neuroendocrine catecholamine that supports bacterial growth by mobilizing iron from a primary source such as holotransferrin to increase its bioavailability for cellular uptake. Iron complexes of NE resemble those of bacterial siderophores that are scavenged by human neutrophil gelatinase-associated lipocalin (NGAL) as part of the innate immune defense. Here, we show that NGAL binds iron-complexed NE, indicating physiological relevance for both bacterial and human iron metabolism. The fluorescence titration of purified recombinant NGAL with the Fe(III).(NE)(3) iron complex revealed high affinity for this ligand, with a K(D) of 50.6 nM. In contrast, the binding protein FeuA of Bacillus subtilis, which is involved in the bacterial uptake of triscatecholate iron complexes, has a K(D) for Fe(III).(NE)(3) of 1.6 muM, indicating that NGAL is an efficient competitor. Furthermore, NGAL was shown to inhibit the NE-mediated growth of both E. coli and B. subtilis strains that either are capable or incapable of producing their native siderophores enterobactin and bacillibactin, respectively. These experiments suggest that iron-complexed NE directly serves as an iron source for bacterial uptake systems, and that NGAL can function as an antagonist of this iron acquisition process. Interestingly, a functional FeuABC uptake system was shown to be necessary for NE-mediated growth stimulation as well as its NGAL-dependent inhibition. This study demonstrates for the first time that human NGAL not only neutralizes pathogen-derived virulence factors but also can effectively scavenge an iron-chelate complex abundant in the host.

Indexed as

Acute-Phase ProteinsAnti-Bacterial AgentsBacillus subtilisEpinephrineEscherichia coliEscherichia coli ProteinsHumansIn Vitro TechniquesIronLigandsLipocalin-2LipocalinsNorepinephrineProtein BindingProto-Oncogene ProteinsReceptors, Cell SurfaceAcute-Phase ProteinsAnti-Bacterial Agentscolicin receptor, E coliEpinephrineEscherichia coli ProteinsIronLCN2 protein, humanLigandsLipocalin-2LipocalinsNorepinephrineProto-Oncogene ProteinsReceptors, Cell SurfaceRecombinant ProteinsSiderophores

Identifiers

PMID20086155
PMCPMC2849382
OpenAlexW2110931665

What OpenQuestion holds

Textmetadata
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.