Evidence map›Paper›PMID 28867522›Full record

ArticleInternational journal of medical microbiology : IJMM2018

Do amyloid structures formed by Staphylococcus aureus phenol-soluble modulins have a biological function?

Yue Zheng, Hwang-Soo Joo, Vinod Nair, Katherine Y Le, Michael Otto

Open access · greenAbstract read
In one paragraph

Article in International journal of medical microbiology : IJMM, 2018. 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
3.9field-weighted citation impact, top 6% 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, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025
    Review
  7. Beyond the double helix: the multifaceted landscape of extracellular DNA inFrontiers in cellular and infection microbiology · 2024
    Review
  8. Article
  9. Review
  10. The great divide: rhamnolipids mediate separation betweenFrontiers in cellular and infection microbiology · 2023
    Article
  11. Article
  12. Colonization and Infection of Indwelling Medical Devices byInternational journal of molecular sciences · 2022
    Review
  13. Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. The structural role of bacterial eDNA in the formation of biofilm streamers.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Phenol-Soluble Modulins FromFrontiers in cellular and infection microbiology · 2022
    Article
  16. Review
  17. Article
  18. Article
  19. Staphylococcal Biofilm Development: Structure, Regulation, and Treatment Strategies.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  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

5 authors at 3 institutions in 2 countries.

Yue ZhengPathogen Molecular Genetics Section, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, U.S. National Institutes of Health, 50 South Drive, Bethesda, MD 20814, USA.
Hwang-Soo JooDepartment of Prepharm-Med, College of Natural Sciences, Duksung Women's University, 33 Samyang-ro 144-gil, Seoul 01369, South Korea.
Vinod NairResearch Technologies Section, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, U.S. National Institutes of Health, 903 South 4th Street, Hamilton, MT 59840, USA.
Katherine Y LePathogen Molecular Genetics Section, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, U.S. National Institutes of Health, 50 South Drive, Bethesda, MD 20814, USA.
Michael OttoPathogen Molecular Genetics Section, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, U.S. National Institutes of Health, 50 South Drive, Bethesda, MD 20814, USA. Electronic address: motto@niaid.nih.gov.
National Institute of Allergy and Infectious Diseases · USDuksung Women's University · KRNational Institutes of Health · US

Funding

Staphylococcal pathogenesisZIAAI000904 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI OTTO, MICHAEL · 2009 to 2025
$22.6M
Staphylococcus Epidermidis Biofilm FormationZ01AI000904 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI OTTO, MICHAEL J · 2002 to 2008
$2.5M
Intramural NIH HHS Z01 AI000904
6 · The paper itself

Abstract

Phenol-soluble modulins (PSMs) are alpha-helical, amphipathic peptides that have multiple functions in staphylococcal physiology and virulence. Recent research has suggested that PSMs form amyloid fibrils and amyloids are involved in PSM-mediated phenotypes such as cytolysis and biofilm stability. While we observed PSM amyloid formation using electron microscopy and dye assays, there were no apparent differences in the production of extracellular fibrous material between a PSM-deficient strain and the isogenic wild-type strain. Furthermore, we detected no correlation between cytolytic or pro-inflammatory activities with the propensity of PSM derivatives to form amyloids. In addition, we propose a model based on our finding of non-specific attachment of PSMs to DNA, which we here report results in resistance to DNase digestion, explaining previous findings on PSM-mediated biofilm stability without the necessity to assume amyloid involvement. Collectively, our results indicate that PSM amyloid formation may not be of major relevance for known key biological functions of PSMs. Intriguingly, however, we found that amyloid-forming capacity of PSMalpha3 allows almost no amino acid exchanges, suggesting importance of amyloid formation in possibly yet unknown functions of PSMs.

Indexed as

AmyloidBacterial ProteinsBacterial ToxinsBiofilmsDNA-Binding ProteinsMicroscopy, Electron, TransmissionModels, BiologicalStaining and LabelingStaphylococcus aureusVirulence FactorsAmyloidBacterial ProteinsBacterial ToxinsDNA-Binding Proteinsstaphylococcal delta toxinVirulence FactorsAmyloidBiofilmPhenol-soluble modulinsStaphylococcus aureusToxin

Identifiers

PMID28867522
PMCPMC5832552
OpenAlexW2751736820

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.