Evidence map›Paper›PMID 10629191›Full record

ArticleJournal of bacteriology2000

Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene.

W Zhu, D J Hunt, A R Richardson, I Stojiljkovic

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.9field-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

47 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Review
  3. HemU and TonB1 contribute to hemin acquisition inFrontiers in cellular and infection microbiology · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Putative Iron Acquisition Systems inMolecules (Basel, Switzerland) · 2018
    Article
  11. Draft Genome Sequence ofGenome announcements · 2017
    Article
  12. Review
  13. Article
  14. Ironing Out the Unconventional Mechanisms of Iron Acquisition and Gene Regulation inFrontiers in cellular and infection microbiology · 2017
    Review
  15. Article
  16. Review
  17. Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016
    Review
  18. Article
  19. Coupling heme and iron metabolism via ferritin H chain.Antioxidants & redox signaling · 2014
    Review
  20. Role and regulation of heme iron acquisition in gram-negative pathogens.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

4 authors at 1 institution in 1 country.

W ZhuDepartment of Microbiology, Emory School of Medicine, Atlanta, Georgia 30322, USA.
D J Hunt
A R Richardson
I Stojiljkovic
Emory University · US

Funding

MICROBIAL PATHOGEN GENOME PROJECT--NEISSERIA GONORRHOEAER01AI038399 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI DYER, DAVID W. · 1995 to 1998
–
NIAID NIH HHS AI38399NIAID NIH HHS AI472870-01A1
6 · The paper itself

Abstract

Heme compounds are an important source of iron for neisseriae. We have identified a neisserial gene, hemO, that is essential for heme, hemoglobin (Hb), and haptoglobin-Hb utilization. The hemO gene is located 178 bp upstream of the hmbR Hb receptor gene in Neisseria meningitidis isolates. The product of the hemO gene is homologous to enzymes that degrade heme; 21% of its amino acid residues are identical, and 44% are similar, to those of the human heme oxygenase-1. DNA sequences homologous to hemO were ubiquitous in commensal and pathogenic neisseriae. HemO genetic knockout strains of Neisseria gonorrhoeae and N. meningitidis were unable to use any heme source, while the assimilation of transferrin-iron and iron-citrate complexes was unaffected. A phenotypic characterization of a conditional hemO mutant, constructed by inserting an isopropyl-beta-D-thiogalactopyranoside (IPTG)-regulated promoter upstream of the ribosomal binding site of hemO, confirmed the indispensability of the HemO protein in heme utilization. The expression of HemO also protected N. meningitidis cells against heme toxicity. hemO mutants were still able to transport heme into the cell, since both heme and Hb could complement an N. meningitidis hemA hemO double mutant for growth. The expression of the HmbR receptor was reduced significantly by the inactivation of the hemO gene, suggesting that hemO and hmbR are transcriptionally linked. The expression of the unlinked Hb receptor, HpuAB, was not altered. Comparison of the polypeptide patterns of the wild type and the hemO mutant led to detection of six protein spots with an altered expression pattern, suggesting a more general role of HemO in the regulation of gene expression in Neisseriae.

Indexed as

Amino Acid SequenceBacterial ProteinsBase SequenceCloning, MolecularGene Expression Regulation, BacterialHemeHeme Oxygenase (Decyclizing)HemoglobinsHumansIronMolecular Sequence DataNeisseria gonorrhoeaeNeisseria meningitidisOpen Reading FramesPhenotypePhylogenyBacterial ProteinsHemeHeme Oxygenase (Decyclizing)HemoglobinsHmbR protein, Neisseria meningitidisIronPorphyrinsReceptors, Cell Surface

Identifiers

PMID10629191
PMCPMC94294
OpenAlexW2097600127

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.