Evidence map›Paper›PMID 19298372›Full record

ArticleMolecular microbiology2009

NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B.

Moriah R Beck, Gregory T Dekoster, David P Cistola, William E Goldman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Genotypic diversity, virulence, and molecular genetic tools inMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Fungal Strategies to Evade the Host Immune Recognition.Journal of fungi (Basel, Switzerland) · 2017
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Recent developments in the interactions between caveolin and pathogens.Advances in experimental medicine and biology · 2012
    Review
  16. Article
  17. Review
  18. Host-microbe interactions: fungi.Current opinion in microbiology · 2010
    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

4 authors at 2 institutions in 2 countries.

Moriah R BeckDepartment of Molecular Microbiology, Washington University in St Louis, St Louis, MO, USA.
Gregory T Dekoster
David P Cistola
William E Goldman
Washington University in St. Louis · USInstitute of Molecular Biology and Biophysics · RU

Funding

Washington University DDRCC Supplemental Equipment RequestP30DK052574 · NIDDK · WASHINGTON UNIVERSITY · PI Nicholas O. Davidson · 2000 to 2026
$30.8M
MOLECULAR MECHANISMS OF HISTOPLASMA PATHOGENESISR01AI025584 · NIAID · WASHINGTON UNIVERSITY · PI GOLDMAN, WILLIAM E · 1988 to 2008
$2.8M
MOLEC RECOGNITION IN INTESTINAL LIPID BINDING PROTEINSR01DK048046 · NIDDK · WASHINGTON UNIVERSITY · PI CISTOLA, DAVID P · 1994 to 2002
$709k
Molecular Mechanisms of Histoplasma PathogenesisR56AI025584 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GOLDMAN, WILLIAM E · 2011 to 2011
$370k
NIAID NIH HHS AI25584NIAID NIH HHS R01 AI025584NIAID NIH HHS R56 AI025584NIDDK NIH HHS DK48046NIDDK NIH HHS DK52574NIDDK NIH HHS P30 DK052574NIDDK NIH HHS R01 DK048046
6 · The paper itself

Abstract

The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four alpha-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells.

Indexed as

Amino Acid SequenceCalcium-Binding ProteinsDimerizationFungal ProteinsHistoplasmaModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationSaposinsVirulence FactorsCalcium-Binding ProteinsFungal ProteinsSaposinsVirulence Factors

Identifiers

PMID19298372
PMCPMC4876643
OpenAlexW1983043901

What OpenQuestion holds

Textmetadata
LicenceTDM
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.