Evidence map›Paper›PMID 26587649›Full record

ArticlePLoS pathogens2015

Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis.

Natalia Pakharukova, James A Garnett, Minna Tuittila, Sari Paavilainen, Mamou Diallo, Yingqi Xu, Steve J Matthews, Anton V Zavialov

Abstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Deciphering the virulence factors, regulation, and immune response toFrontiers in cellular and infection microbiology · 2023
    Review
  13. Review
  14. A combinedCell cycle (Georgetown, Tex.) · 2022
    Article
  15. Article
  16. Subunit vaccines forFrontiers in immunology · 2022
    Review
  17. Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021
    Article
  18. Article
  19. 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

8 authors.

Natalia PakharukovaDepartment of Chemistry, University of Turku, Turku, JBL, Arcanum, Turku, Finland.
James A GarnettCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom.
Minna TuittilaDepartment of Chemistry, University of Turku, Turku, JBL, Arcanum, Turku, Finland.
Sari PaavilainenDepartment of Chemistry, University of Turku, Turku, JBL, Arcanum, Turku, Finland.
Mamou DialloCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom.
Yingqi XuCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom.
Steve J MatthewsCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom.
Anton V ZavialovDepartment of Chemistry, University of Turku, Turku, JBL, Arcanum, Turku, Finland.

Funding

Medical Research Council G1001664Medical Research Council MR/J006874/1Wellcome Trust 085464Wellcome Trust 100280
6 · The paper itself

Abstract

Gram-negative pathogens express fibrous adhesive organelles that mediate targeting to sites of infection. The major class of these organelles is assembled via the classical, alternative and archaic chaperone-usher pathways. Although non-classical systems share a wider phylogenetic distribution and are associated with a range of diseases, little is known about their assembly mechanisms. Here we report atomic-resolution insight into the structure and biogenesis of Acinetobacter baumannii Csu and Escherichia coli ECP biofilm-mediating pili. We show that the two non-classical systems are structurally related, but their assembly mechanism is strikingly different from the classical assembly pathway. Non-classical chaperones, unlike their classical counterparts, maintain subunits in a substantially disordered conformational state, akin to a molten globule. This is achieved by a unique binding mechanism involving the register-shifted donor strand complementation and a different subunit carboxylate anchor. The subunit lacks the classical pre-folded initiation site for donor strand exchange, suggesting that recognition of its exposed hydrophobic core starts the assembly process and provides fresh inspiration for the design of inhibitors targeting chaperone-usher systems.

Indexed as

Acinetobacter baumanniiAmino Acid SequenceCrystallography, X-RayEscherichia coliEscherichia coli ProteinsFimbriae, BacterialFimbriae ProteinsMolecular ChaperonesPhylogenyProtein SubunitsEscherichia coli ProteinsFimbriae ProteinsMolecular ChaperonesProtein Subunits

Identifiers

PMID26587649
PMCPMC4654587

What OpenQuestion holds

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Registered trials

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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.