Evidence map›Paper›PMID 20952578›Full record

ArticleJournal of bacteriology2010

Role of porins in iron uptake by Mycobacterium smegmatis.

Christopher M Jones, Michael Niederweis

Abstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. ThemBio · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. TargetingRSC medicinal chemistry · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Frontiers in microbiology · 2018
    Article
  18. Article
  19. Iron Starvation Conditions UpregulateFrontiers in cellular and infection microbiology · 2017
    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

2 authors at 1 institution in 1 country.

Christopher M JonesDepartment of Microbiology, University of Alabama at Birmingham, 609 Bevill Biomedical Research Building, 845 19th Street South, Birmingham, Alabama 35294, USA.
Michael Niederweis
University of Alabama at Birmingham · US

Funding

BASIC MECHANISMS IN AIDS PATHOGENESIST32AI007493 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MORROW, CASEY D · 1995 to 2014
$4.2M
Porins of Mycobacterium tuberculosisR01AI063432 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NIEDERWEIS, MICHAEL · 2005 to 2009
$1.7M
NIAID NIH HHS R01 AI063432NIAID NIH HHS T32 AI007493NIAID NIH HHS T32AI007493
6 · The paper itself

Abstract

Many bacteria rely on siderophores to extract iron from the environment. However, acquisition of iron-loaded siderophores is dependent on high-affinity uptake systems that are not produced under high-iron conditions. The fact that bacteria are able to maintain iron homeostasis in the absence of siderophores indicates that alternative iron acquisition systems exist. It has been speculated that such low-affinity uptake of iron in Gram-negative bacteria includes diffusion of iron ions or chelates across the outer membrane through porins. The outer membrane of the saprophytic Mycobacterium smegmatis contains the Msp family of porins, which enable the diffusion of small and hydrophilic solutes, such as monosaccharides, amino acids, and phosphate. However, it is unknown how cations cross the outer membrane of mycobacteria. Here, we show that the Msp porins of M. smegmatis are involved in the acquisition of soluble iron under high-iron conditions. Uptake of ferric ions by a triple porin mutant was reduced compared to wild-type (wt) M. smegmatis. An intracellular iron reporter indicated that derepression of iron-responsive genes occurs at higher iron concentrations in the porin mutant. This was consistent with the finding that the porin mutant produced more siderophores under low-iron conditions than wt M. smegmatis. In contrast, uptake of the exochelin MS, the main siderophore of M. smegmatis, was not affected by the lack of porins, indicating that a specific outer membrane siderophore receptor exists. These results provide, to our knowledge, the first experimental evidence that general porins are indeed the outer membrane conduit of low-affinity iron acquisition systems in bacteria.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsBiological TransportFerric CompoundsGene Expression Regulation, BacterialIronMutationMycobacterium smegmatisPorinsRepressor ProteinsSiderophoresBacterial Outer Membrane ProteinsBacterial Proteinsferric citrateFerric CompoundsIdeR protein, Mycobacterium tuberculosisIronPorinsRepressor ProteinsSiderophores

Identifiers

PMID20952578
PMCPMC3008526
OpenAlexW2014443241

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.