Evidence map›Paper›PMID 10569756›Full record

ArticleInfection and immunity1999

Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum.

M M Timmerman, J P Woods

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

25 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Journal of fungi (Basel, Switzerland) · 2019
    Review
  5. Histoplasma Capsulatum: Mechanisms for Pathogenesis.Current topics in microbiology and immunology · 2019
    Review
  6. Metals in fungal virulence.FEMS microbiology reviews · 2018
    Review
  7. The Fungal PathogenFrontiers in microbiology · 2017
    Article
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  15. 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, Wisconsin 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
NHLBI NIH HHS R01 HL055949NIGMS NIH HHS T32 GM007215NIGMS NIH HHS T32GM07215
6 · The paper itself

Abstract

For the fungus Histoplasma capsulatum, and for other microbial pathogens, iron is an essential nutrient. Iron sequestration in response to infection is a demonstrated host defense mechanism; thus, iron acquisition may be considered an important pathogenic determinant. H. capsulatum is known to secrete Fe(III)-binding hydroxamate siderophores, which is one common microbial process for acquiring iron. Here, we report H. capsulatum ferric reduction activities in whole yeast cells and in both high- and low-molecular-weight fractions of culture supernatants. Each of these activities was induced or derepressed by growth under iron-limiting conditions, a phenomenon often associated with specific iron acquisition mechanisms. The high-molecular-weight culture supernatant activity was enhanced by the addition of reduced glutathione, was proteinase K sensitive and heat labile, and could utilize ferric chloride, ferric citrate, and human holotransferrin as substrates. The low-molecular-weight culture supernatant activity was resistant to proteinase K digestion. These results are consistent with the expression by H. capsulatum of both enzymatic ferric reductase and nonproteinaceous ferric reductant, both of which are regulated by iron availability. Such components could be involved in fungal acquisition of iron from inorganic or organic ferric salts, from H. capsulatum hydroxamate siderophores, or from host Fe(III)-binding proteins, such as transferrin.

Indexed as

FMN ReductaseCulture MediaEndopeptidase KFerric CompoundsHistoplasmaHumansIronNADH, NADPH OxidoreductasesOxidation-ReductionCulture MediaEndopeptidase Kferric citrate iron reductaseFerric CompoundsFMN ReductaseIronNADH, NADPH Oxidoreductases

Identifiers

PMID10569756
PMCPMC97048
OpenAlexW2095673877

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.