Evidence map›Paper›PMID 38589417›Full record

ArticleNature communications2024

The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili.

Dawid S Zyla, Thomas Wiegand, Paul Bachmann, Rafal Zdanowicz, Christoph Giese, Beat H Meier, Gabriel Waksman, Manuela K Hospenthal, Rudi Glockshuber

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. A cold-responsiveApplied and environmental microbiology · 2026
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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

9 authors at 3 institutions in 4 countries.

Dawid S ZylaInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-8471-469X
Thomas WiegandLaboratory of Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 1-5/10, 8093, Zürich, Switzerland.
Paul BachmannInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093, Zürich, Switzerland.ORCID http://orcid.org/0009-0005-5516-826X
Rafal ZdanowiczInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093, Zürich, Switzerland.ORCID http://orcid.org/0009-0005-5694-2704
Christoph GieseInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-9875-9629
Beat H MeierLaboratory of Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 1-5/10, 8093, Zürich, Switzerland.
Gabriel WaksmanInstitute of Structural and Molecular Biology, University College London and Birkbeck, London, WC1E 7HX, UK.
Manuela K HospenthalInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093, Zürich, Switzerland. manuela.hospenthal@mol.biol.ethz.ch.ORCID http://orcid.org/0000-0003-1175-6826
Rudi GlockshuberInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0003-3320-3843
ETH Zurich · CHInstitute of Structural and Molecular Biology · GBLa Jolla Institute for Immunology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of copies of the main structural subunit FimA and is assembled in vivo by the assembly platform FimD. Although type 1 pilus rods can self-assemble from FimA in vitro, this reaction is slower and produces structures with lower kinetic stability against denaturants compared to in vivo-assembled rods. Our study reveals that FimD-catalysed in vitro-assembled type 1 pilus rods attain a similar stability as pilus rods assembled in vivo. Employing structural, biophysical and biochemical analyses, we show that in vitro assembly reactions lacking FimD produce pilus rods with structural defects, reducing their stability against dissociation. Overall, our results indicate that FimD is not only required for the catalysis of pilus assembly, but also to control the assembly of the most stable quaternary structure.

Indexed as

Escherichia coli ProteinsFimbriae ProteinsEscherichia coliFimbriae, BacterialEscherichia coli ProteinsFimbriae Proteins

Identifiers

PMID38589417
PMCPMC11001860
OpenAlexW4394568386

What OpenQuestion holds

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LicenceCC BY
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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.