Evidence map›Paper›PMID 40442073›Full record

ArticleNature communications2025

Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination.

Paul Bachmann, Pavel Afanasyev, Daniel Boehringer, Rudi Glockshuber

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Antibiotics (Basel, Switzerland) · 2026
    Article
  2. A cold-responsiveApplied and environmental microbiology · 2026
    Article
  3. Mannose Derivatives as Anti-Infective Agents.International journal of molecular sciences · 2025
    Review
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.

Paul BachmannInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, Zürich, 8093, Switzerland.ORCID http://orcid.org/0009-0005-5516-826X
Pavel AfanasyevCryo-EM Knowledge Hub (CEMK), ETH Zürich, Otto-Stern-Weg 3, Zürich, 8093, Switzerland.ORCID http://orcid.org/0000-0002-6353-6895
Daniel BoehringerCryo-EM Knowledge Hub (CEMK), ETH Zürich, Otto-Stern-Weg 3, Zürich, 8093, Switzerland.ORCID http://orcid.org/0000-0002-6666-8447
Rudi GlockshuberInstitute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, Zürich, 8093, Switzerland. rudi@mol.biol.ethz.ch.ORCID http://orcid.org/0000-0003-3320-3843

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 310030_201234
6 · The paper itself

Abstract

Uropathogenic Escherichia coli strains use filamentous type 1 pili to adhere to and invade uroepithelial cells. The pilus consists of a flexible tip fibrillum, formed by the adhesin FimH and the subunits FimG and FimF. The pilus rod is a helical assembly of up to 3000 copies of the main subunit FimA, terminated by a single copy of the subunit FimI that anchors the rod to the assembly platform FimD in the outer membrane. Although type 1 pilus assembly can be completely reconstituted in vitro, the precise mechanism of assembly termination on FimD is still unknown. Here, we present cryo-electron microscopy structures of the fully assembled pilus with all its components prior to and after incorporation of FimI, capped with the assembly chaperone FimC. The structures reveal that FimD positions the proximal end of the pilus rod at an angle of ca. 50 degrees relative to the plane of the outer membrane. Specific interactions between FimI and FimC, absent in the equivalent FimA-FimC interface of the non-terminated pilus, stabilize the assembly-terminated state. In addition, we present structures of the transition region between the tip fibrillum and the helical rod, showing how FimF aligns the tip fibrillum along the rod axis.

Indexed as

Escherichia coliEscherichia coli ProteinsFimbriae, BacterialFimbriae ProteinsUropathogenic Escherichia coliAdhesins, Escherichia coliCryoelectron MicroscopyModels, MolecularAdhesins, Escherichia coliEscherichia coli ProteinsFimbriae ProteinsfimC protein, E colifimD protein, E colifimH protein, E coli

Identifiers

PMID40442073
PMCPMC12122975

What OpenQuestion holds

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LicenceCC BY
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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.