Evidence map›Paper›PMID 36400765›Full record

ArticleNature communications2022

Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms.

Jan Böhning, Mnar Ghrayeb, Conrado Pedebos, Daniel K Abbas, Syma Khalid, Liraz Chai, Tanmay A M Bharat

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed.

  1. Bioinformatic Analysis ofInternational journal of molecular sciences · 2026
    Article
  2. Review
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  4. Article
  5. Article
  6. Article
  7. Precision Labeling of Native Antibodies with Lock Coupling.Journal of the American Chemical Society · 2026
    Article
  8. Review
  9. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Structural basis ofScience advances · 2025
    Article
  15. Article
  16. Tat-dependent bundling pilus of a halophilic archaeon assembles by a strand donation mechanism and facilitates biofilm formation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Structure of the virulence-associatedProceedings of the National Academy of Sciences of the United States of America · 2025
    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

7 authors.

Jan BöhningSir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.ORCID 0000-0002-6242-1041
Mnar GhrayebInstitute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem, 91904, Israel.
Conrado PedebosDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Daniel K AbbasSir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
Syma KhalidDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.ORCID 0000-0002-3694-5044
Liraz ChaiInstitute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem, 91904, Israel. liraz.chai@mail.huji.ac.il.ORCID 0000-0001-9644-4455
Tanmay A M BharatSir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK. tbharat@mrc-lmb.cam.ac.uk.ORCID 0000-0002-0168-0277

Funding

Medical Research Council MC_UP_1201/31Wellcome Trust 202231/Z/16/Z
6 · The paper itself

Abstract

Many bacteria in nature exist in multicellular communities termed biofilms, where cells are embedded in an extracellular matrix that provides rigidity to the biofilm and protects cells from chemical and mechanical stresses. In the Gram-positive model bacterium Bacillus subtilis, TasA is the major protein component of the biofilm matrix, where it has been reported to form functional amyloid fibres contributing to biofilm structure and stability. Here, we present electron cryomicroscopy structures of TasA fibres, which show that, rather than forming amyloid fibrils, TasA monomers assemble into fibres through donor-strand exchange, with each subunit donating a β-strand to complete the fold of the next subunit along the fibre. Combining electron cryotomography, atomic force microscopy, and mutational studies, we show how TasA fibres congregate in three dimensions to form abundant fibre bundles that are essential for B. subtilis biofilm formation. Our study explains the previously observed biochemical properties of TasA and shows how a bacterial extracellular globular protein can assemble from monomers into β-sheet-rich fibres, and how such fibres assemble into bundles in biofilms.

Indexed as

Bacillus subtilisSpidersAmyloidAnimalsBacterial ProteinsBiofilmsAmyloidBacterial Proteins

Identifiers

PMID36400765
PMCPMC9674648

What OpenQuestion holds

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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.