Evidence map›Paper›PMID 11705947›Full record

ArticleInfection and immunity2001

Potential role for extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum.

M M Timmerman, J P Woods

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 58 citations in OpenAlex.

  1. Gut microbes · 2025
    Article
  2. Journal of fungi (Basel, Switzerland) · 2019
    Review
  3. Histoplasma Capsulatum: Mechanisms for Pathogenesis.Current topics in microbiology and immunology · 2019
    Review
  4. Metals in fungal virulence.FEMS microbiology reviews · 2018
    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 1 institution in 1 country.

M M TimmermanDepartment of Medical Microbiology and Immunology, Microbiology Doctoral Training Program, University of Wisconsin, Madison 53706, USA.
J P Woods
University of Wisconsin–Madison · US

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
MOLECULAR PATHOGENESIS OF PULMONARY HISTOPLASMOSISR01HL055949 · NHLBI · UNIVERSITY OF WISCONSIN MADISON · PI WOODS, JON P. · 1995 to 2004
$1.7M
Histoplasma capsulatum Iron Acquisition and UtilizationR01AI052303 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI WOODS, JON P. · 2002 to 2006
$1.5M
NHLBI NIH HHS R01 HL055949NHLBI NIH HHS R01 HL55949NIAID NIH HHS R01 AI052303NIGMS NIH HHS T32 GM007215NIGMS NIH HHS T32 GM07215
6 · The paper itself

Abstract

The mammalian host specifically limits iron during Histoplasma capsulatum infection, and fungal acquisition of iron is essential for productive infection. H. capsulatum expresses several iron acquisition mechanisms under iron-limited conditions in vitro. These components include hydroxamate siderophores, extracellular glutathione-dependent ferric reductase enzyme, extracellular nonproteinaceous ferric reductant(s), and cell surface ferric reducing agent(s). We examined the relationship between these mechanisms and a potential role for the extracellular ferric reductase in utilization of environmental and host ferric compounds through the production of free, soluble Fe(II). Siderophores and ferric reducing agents were coproduced under conditions of iron limitation. The H. capsulatum siderophore dimerum acid and the structurally similar basidiomycete siderophore rhodotorulic acid acted as substrates for the ferric reductase, and rhodotorulic acid removed Fe(III) bound by transferrin. The mammalian Fe(III)-binding compounds hemin and transferrin served both as substrates for the ferric reductase and as iron sources for yeast-phase growth at neutral pH. In the case of transferrin, there was a correlation between the level of iron saturation and efficacy for both of these functions. Our data are not consistent with an entirely pH-dependent mechanism of iron acquisition from transferrin, as has been suggested to occur in the macrophage phagolysosome. The foreign siderophore ferrioxamine B also acted as a substrate for the ferric reductase, while the foreign siderophore ferrichrome did not. Both ferrioxamine and ferrichrome served as iron sources for yeast- and mold-phase growth, the latter presumably by some other acquisition mechanism(s).

Indexed as

FMN ReductaseBiological TransportEnvironmentFerric CompoundsGlutathioneHistoplasmaIronModels, BiologicalNADH, NADPH OxidoreductasesPiperazinesSiderophoresSubstrate Specificitydimerum acidferric citrate iron reductaseFerric CompoundsFMN ReductaseGlutathioneIronNADH, NADPH OxidoreductasesPiperazinesrhodotorulic acidSiderophores

Identifiers

PMID11705947
PMCPMC98861
OpenAlexW2140001930

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.