Evidence map›Paper›PMID 31469892›Full record

ArticlePLoS pathogens2019

Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.

Sergei Perov, Ofir Lidor, Nir Salinas, Nimrod Golan, Einav Tayeb-Fligelman, Maya Deshmukh, Dieter Willbold, Meytal Landau

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

63 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Microbiota-Gut-Brain Axis in Neurodegenerative Diseases: The Role of Bacterial Amyloids.Cellular and molecular gastroenterology and hepatology · 2026
    Review
  9. Brain, behavior, & immunity - health · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Multidrug Resistance and Virulence Traits ofAntibiotics (Basel, Switzerland) · 2025
    Article
  17. Review
  18. Antibiofilm Activities of Halogenated Pyrimidines Against EnterohemorrhagicInternational journal of molecular sciences · 2025
    Article
  19. Article
  20. Functional constraints ofbioRxiv : the preprint server for biology · 2025
    Article

3 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 2 countries.

Sergei PerovDepartment of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Ofir LidorDepartment of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0001-6392-4647
Nir SalinasDepartment of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0002-3511-2243
Nimrod GolanDepartment of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0001-5064-0776
Einav Tayeb-FligelmanDepartment of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Maya DeshmukhDepartment of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0002-3704-3229
Dieter WillboldInstitute of Complex Systems (ICS-6, Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-0065-7366
Meytal LandauDepartment of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0002-1743-3430
Technion – Israel Institute of Technology · ILForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and contribute to biofilm formation, thereby promoting bacterial resistance to environmental stressors. Here, we present crystal structures of amyloid-forming segments from the major curli subunit, CsgA, revealing steric zipper fibrils of tightly mated β-sheets, demonstrating a structural link between curli and human pathological amyloids. D-enantiomeric peptides, originally developed to interfere with Alzheimer's disease-associated amyloid-β, inhibited CsgA fibrillation and reduced biofilm formation in Salmonella typhimurium. Moreover, as previously shown, CsgA fibrils cross-seeded fibrillation of amyloid-β, providing support for the proposed structural resemblance and potential for cross-species amyloid interactions. The presented findings provide structural insights into amyloidogenic regions important for curli formation, suggest a novel strategy for disrupting amyloid-structured biofilms, and hypothesize on the formation of self-propagating prion-like species originating from a microbial source that could influence neurodegenerative diseases.

Indexed as

AmyloidBiofilmsCrystallography, X-RayEscherichia coli ProteinsHumansMicroscopy, Electron, TransmissionPeptide FragmentsProtein BindingSalmonella typhimuriumAmyloidcsgA protein, E coliEscherichia coli ProteinsPeptide Fragments

Identifiers

PMID31469892
PMCPMC6748439
OpenAlexW2971262787

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.