Evidence map›Paper›PMID 24465872›Full record

ArticlePloS one2014

Peptide detection of fungal functional amyloids in infected tissue.

Melissa C Garcia-Sherman, Nataliya Lysak, Alexandra Filonenko, Hazel Richards, Richard E Sobonya, Stephen A Klotz, Peter N Lipke

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Functional Amyloids in Adhesion of Non-Pathogens (Basel, Switzerland) · 2025
    Article
  3. Review
  4. Article
  5. Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. What We Do Not Know about Fungal Cell Adhesion Molecules.Journal of fungi (Basel, Switzerland) · 2018
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

7 authors at 3 institutions in 1 country.

Melissa C Garcia-ShermanDepartment of Biology, City University of New York Brooklyn College, Brooklyn, New York, United States of America.
Nataliya LysakDepartment of Biology, City University of New York Brooklyn College, Brooklyn, New York, United States of America.
Alexandra FilonenkoDepartment of Biology, City University of New York Brooklyn College, Brooklyn, New York, United States of America.
Hazel RichardsDepartment of Biology, City University of New York Brooklyn College, Brooklyn, New York, United States of America.
Richard E SobonyaDepartment of Pathology, University of Arizona, Tuscon, Arizona, United States of America.
Stephen A KlotzDivision of Infectious Diseases, University of Arizona, Tuscon, Arizona, United States of America.
Peter N LipkeDepartment of Biology, City University of New York Brooklyn College, Brooklyn, New York, United States of America.
City University of New York · USBrooklyn College · USUniversity of Arizona · US

Funding

Amyloid-like Interactions in Yeast Cell AdhesionSC1GM083756 · NIGMS · BROOKLYN COLLEGE · PI LIPKE, PETER N · 2008 to 2011
$1.7M
Diversity Supplement to R01 GM 098616 for Ivor JosephR01GM098616 · NIGMS · BROOKLYN COLLEGE · PI LIPKE, PETER N · 2012 to 2015
$1.5M
NIGMS NIH HHS R01 GM098616NIGMS NIH HHS SC1 GM083756
6 · The paper itself

Abstract

Many fungal cell adhesion proteins form functional amyloid patches on the surface of adhering cells. The Candida albicans Agglutinin-like sequence (Als) adhesins are exemplars for this phenomenon, and have amyloid forming sequences that are conserved between family members. The Als5p amyloid sequence mediates amyloid fibril formation and is critical for cell adhesion and biofilm formation, and is also present in the related adhesins Als1p and Als3p. We have developed a fluorescent peptide probe containing the conserved Als amyloid-forming sequence. This peptide bound specifically to yeast expressing Als5p, but not to cells lacking the adhesin. The probe bound to both yeast and hyphal forms of C. albicans. Δals1/Δals3 single and double deletion strains exhibited reduced fluorescence, indicating that probe binding required expression of these proteins. Additionally, the Als peptide specifically stained fungal cells in abscesses in autopsy sections. Counterstaining with calcofluor white showed colocalization with the amyloid peptide. In addition, fungi in autopsy sections derived from the gastrointestinal tract showed colocalization of the amyloid-specific dye thioflavin T and the fluorescent peptide. Collectively, our data demonstrate that we can exploit amyloid sequence specificity for detection of functional amyloids in situ.

Indexed as

Amino Acid SequenceAmyloidAutopsyBenzenesulfonatesBenzothiazolesCandida albicansCandidiasisFluorescent DyesFungal ProteinsGene DeletionHumansHyphaeMolecular Sequence DataOrgan SpecificityPeptidesProtein BindingAmyloidBenzenesulfonatesBenzothiazolesC.I. Fluorescent Brightening Agent 28Fluorescent DyesFungal ProteinsPeptidesThiazolesthioflavin T

Identifiers

PMID24465872
PMCPMC3897640
OpenAlexW2046904716

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.