Evidence map›Paper›PMID 22083713›Full record

ArticleInfection and immunity2012

The Neisseria meningitidis ZnuD zinc receptor contributes to interactions with epithelial cells and supports heme utilization when expressed in Escherichia coli.

Pradeep Kumar, Soma Sannigrahi, Yih-Ling Tzeng

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.9field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Virulence regulation in the fish pathogenFrontiers in cellular and infection microbiology · 2026
    Review
  2. Frontiers in cellular and infection microbiology · 2025
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. The Zinc Nutritional Immunity ofFrontiers in immunology · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Competition for zinc binding in the host-pathogen interaction.Frontiers in cellular and infection microbiology · 2013
    Review
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 1 institution in 1 country.

Pradeep KumarDepartment of Medicine, Emory University School of Medicine, Atlanta, Georgia, USA.
Soma Sannigrahi
Yih-Ling Tzeng
Emory University · US

Funding

Control of virulence in Neisseria meningitidisR01AI061031 · NIAID · EMORY UNIVERSITY · PI TZENG, YIH-LING · 2005 to 2009
$1.5M
NIAID NIH HHS R01 AI061031
6 · The paper itself

Abstract

Neisseria meningitidis employs redundant heme acquisition mechanisms, including TonB receptor-dependent and receptor-independent uptakes. The TonB-dependent zinc receptor ZnuD shares significant sequence similarity to HumA, a heme receptor of Moraxella catarrhalis, and contains conserved motifs found in many heme utilization proteins. We present data showing that, when expressed in Escherichia coli, ZnuD allowed heme capture on the cell surface and supported the heme-dependent growth of an E. coli hemA strain. Heme agarose captured ZnuD in enriched outer membrane fractions, and this binding was inhibited by excess free heme, supporting ZnuD's specific interaction with heme. However, no heme utilization defect was detected in the meningococcal znuD mutant, likely due to unknown redundant TonB-independent heme uptake mechanisms. Meningococcal replication within epithelial cells requires a functional TonB, and we found that both the znuD and tonB mutants were defective not only in survival within epithelial cells but also in adherence to and invasion of epithelial cells. Ectopic complementation rescued these phenotypes. Interestingly, while znuD expression was repressed by Zur with zinc as a cofactor, it also was induced by iron in a Zur-independent manner. A specific interaction of meningococcal Fur protein with the znuD promoter was demonstrated by electrophoretic mobility shift assay (EMSA). Thus, the meningococcal ZnuD receptor likely participates in both zinc and heme acquisition, is regulated by both Zur and Fur, and is important for meningococcal interaction with epithelial cells.

Indexed as

Amino Acid SequenceAnimalsBacterial AdhesionBacterial ProteinsCation Transport ProteinsCell Line, TumorEpithelial CellsEscherichia coliGene Expression Regulation, BacterialHemeHumansMembrane ProteinsMolecular Sequence AnnotationMutationNeisseria meningitidisPromoter Regions, GeneticBacterial ProteinsCation Transport ProteinsHemeMembrane ProteinstonB protein, BacteriaZincZnuD protein, Neisseria meningitidis

Identifiers

PMID22083713
PMCPMC3264319
OpenAlexW2107137243

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.