Evidence map›Paper›PMID 37198180›Full record

ArticleNature communications2023

Structural analysis and architectural principles of the bacterial amyloid curli.

Mike Sleutel, Brajabandhu Pradhan, Alexander N Volkov, Han Remaut

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

40 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. De Novo Autogenic Engineered Living Functional Materials.Advanced materials (Deerfield Beach, Fla.) · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Review
  10. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Structural basis ofScience advances · 2025
    Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Mike SleutelStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium. Mike.Sleutel@vub.be.ORCID 0000-0003-3247-2187
Brajabandhu PradhanStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.ORCID 0000-0001-5732-6675
Alexander N VolkovStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Han RemautStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium. Han.Remaut@vub.be.ORCID 0000-0002-9775-4102
Vrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two decades have passed since the initial proposition that amyloids are not only (toxic) byproducts of an unintended aggregation cascade, but that they can also be produced by an organism to serve a defined biological function. That revolutionary idea was borne out of the realization that a large fraction of the extracellular matrix that holds Gram-negative cells into a persistent biofilm is composed of protein fibers (curli; tafi) with cross-β architecture, nucleation-dependent polymerization kinetics and classic amyloid tinctorial properties. The list of proteins shown to form so-called functional amyloid fibers in vivo has greatly expanded over the years, but detailed structural insights have not followed at a similar pace in part due to the associated experimental barriers. Here we combine extensive AlphaFold2 modelling and cryo-electron transmission microscopy to propose an atomic model of curli protofibrils, and their higher modes of organization. We uncover an unexpected structural diversity of curli building blocks and fibril architectures. Our results allow for a rationalization of the extreme physico-chemical robustness of curli, as well as earlier observations of inter-species curli promiscuity, and should facilitate further engineering efforts to expand the repertoire of curli-based functional materials.

Indexed as

Bacterial ProteinsEscherichia coli ProteinsAmyloidAmyloidogenic ProteinsBacteriaBiofilmsAmyloidAmyloidogenic ProteinsBacterial ProteinsEscherichia coli Proteins

Identifiers

PMID37198180
PMCPMC10192328
OpenAlexW4377010749

What OpenQuestion holds

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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.