Evidence map›Paper›PMID 23760277›Full record

ArticleThe Journal of biological chemistry2013

The Mycobacterium tuberculosis secreted protein Rv0203 transfers heme to membrane proteins MmpL3 and MmpL11.

Cedric P Owens, Nicholas Chim, Amanda B Graves, Christine A Harmston, Angelina Iniguez, Heidi Contreras, Matthew D Liptak, Celia W Goulding

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
4.6field-weighted citation impact, top 5% 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, 78 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Vitamin BMicrobiology spectrum · 2024
    Article
  5. Metabolic Rewiring ofMetabolites · 2024
    Review
  6. Review
  7. Article
  8. Molecular Mechanisms of MmpL3 Function and Inhibition.Microbial drug resistance (Larchmont, N.Y.) · 2023
    Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Structural and Molecular Dynamics ofACS infectious diseases · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 2 institutions in 1 country.

Cedric P OwensDepartment of Molecular Biology and Biochemistry, University of California at Irvine, Irvine, California 92697, USA.
Nicholas Chim
Amanda B Graves
Christine A Harmston
Angelina Iniguez
Heidi Contreras
Matthew D Liptak
Celia W Goulding
University of California, Irvine · USUniversity of Vermont · US

Funding

Structural And Biochemical Characterization Of A Novel Mycobacterial Heme UptakeR01AI081161 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI GOULDING, CELIA · 2009 to 2013
$1.8M
Biochemical and Proteomic Analyses of Mycobacterial Heme UptakeF31GM101945 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI CONTRERAS, HEIDI · 2012 to 2014
$98k
NIAID NIH HHS AI081161NIAID NIH HHS R01 AI081161NIGMS NIH HHS F31 GM101945NIGMS NIH HHS GM101945
6 · The paper itself

Abstract

Mycobacterium tuberculosis is the causative agent of tuberculosis, which is becoming an increasingly global public health problem due to the rise of drug-resistant strains. While residing in the human host, M. tuberculosis needs to acquire iron for its survival. M. tuberculosis has two iron uptake mechanisms, one that utilizes non-heme iron and another that taps into the vast host heme-iron pool. To date, proteins known to be involved in mycobacterial heme uptake are Rv0203, MmpL3, and MmpL11. Whereas Rv0203 transports heme across the bacterial periplasm or scavenges heme from host heme proteins, MmpL3 and MmpL11 are thought to transport heme across the membrane. In this work, we characterize the heme-binding properties of the predicted extracellular soluble E1 domains of both MmpL3 and MmpL11 utilizing absorption, electron paramagnetic resonance, and magnetic circular dichroism spectroscopic methods. Furthermore, we demonstrate that Rv0203 transfers heme to both MmpL3-E1 and MmpL11-E1 domains at a rate faster than passive heme dissociation from Rv0203. This work elucidates a key step in the mycobacterial uptake of heme, and it may be useful in the development of anti-tuberculosis drugs targeting this pathway.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesBiological TransportCarrier ProteinsCircular DichroismElectron Spin Resonance SpectroscopyElectrophoresis, Polyacrylamide GelHemeHemeproteinsHumansKineticsMembrane ProteinsMembrane Transport ProteinsMetalloporphyrinsModels, BiologicalBacterial ProteinsCarrier ProteinsHemeHemeproteinsMembrane ProteinsMembrane Transport ProteinsMetalloporphyrinsRecombinant Proteinszinc mesoporphyrinHemeHeme Uptake PathwayIronIron AcquisitionKineticsMycobacterium tuberculosisProtein DomainsTransport

Identifiers

PMID23760277
PMCPMC3724630
OpenAlexW1964734437

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.