Evidence map›Paper›PMID 41993355›Full record

ArticlebioRxiv : the preprint server for biology2026

Structural determinants of endopilus assembly, stability and functional specificity in bacterial type II secretion.

Maylis Lejeune, Stefaniia Ivashchenko, Régine Dazzoni, Benjamin Bardiaux, Ravi R Sonani, Matthijn Vos, Theis Jacobsen, Edward H Egelman, Michael Nilges, Olivera Francetic and 2 more

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Maylis LejeuneInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Bacterial Transmembrane Systems Unit, F-75015 Paris, France.
Stefaniia IvashchenkoInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Structural Bioinformatics Unit, F-75015 Paris, France.ORCID 0000-0002-2302-115X
Régine DazzoniInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Bacterial Transmembrane Systems Unit, F-75015 Paris, France.ORCID 0000-0003-4666-5617
Benjamin BardiauxInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Bacterial Transmembrane Systems Unit, F-75015 Paris, France.ORCID 0000-0003-4014-9195
Ravi R SonaniDepartment of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA, USA.
Matthijn VosInstitut Pasteur, Université Paris Cité, Nanoimaging Core Facility, F-75015 Paris, France.ORCID 0000-0002-6046-9949
Theis JacobsenInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Structural Bioinformatics Unit, F-75015 Paris, France.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA, USA.ORCID 0000-0003-4844-5212
Michael NilgesInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Structural Bioinformatics Unit, F-75015 Paris, France.ORCID 0000-0002-1451-8092
Olivera FranceticInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Biochemistry of Macromolecular Interactions Unit, F-75015 Paris, France.ORCID 0000-0002-4145-5314
Vladimir E ShevchikUniversité Lyon 1, INSA Lyon, CNRS UMR 5240 Microbiologie Adaptation et Pathogénie, Villeurbanne, France.
Nadia Izadi-PruneyreInstitut Pasteur, Université Paris Cité, CNRS UMR3528, Bacterial Transmembrane Systems Unit, F-75015 Paris, France.ORCID 0000-0002-6864-2961

Funding

Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic ResolutionR35GM122510 · NIGMS · UNIVERSITY OF VIRGINIA · PI EDWARD H. EGELMAN · 2017 to 2026
$7.3M
NIGMS NIH HHS R35 GM122510
6 · The paper itself

Abstract

Gram-negative bacteria employ the type II secretion system (T2SS) to transport folded protein effectors across the outer membrane. This multiprotein nanomachine assembles the endopilus, a periplasmic helical polymer composed of one major and four minor pilin subunits. Endopili are structurally related to type IV pili but exhibit distinct features including a conserved calcium-binding site stabilizing their major pilin subunits. Endopilus polymerisation is coupled to substrate translocation through a dedicated outer membrane channel. To investigate the structural basis of endopilus assembly, stability and functional specificity, we performed a comparative analysis of the Out T2SS from the plant pathogen

Indexed as

calciumcryo-EMNMRpilus structuretype II secretion system

Identifiers

PMID41993355
PMCPMC13081927

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.