Evidence map›Paper›PMID 38063437›Full record

ArticlemBio2024

Membrane platform protein PulF of the

Ingrid Guilvout, Firdaus Samsudin, Roland G Huber, Peter J Bond, Benjamin Bardiaux, Olivera Francetic

Open access · goldAbstract read
In one paragraph

Article in mBio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

10 citing papers in PubMed, 10 citations in OpenAlex.

  1. Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  3. Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025
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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

6 authors at 2 institutions in 2 countries.

Ingrid Guilvout *Institut Pasteur, Université Paris Cité, CNRS UMR 3528, Biochemistry of Macromolecular Interactions Unit, Paris, France.ORCID 0009-0004-1812-4682
Firdaus Samsudin *Bioinformatics Institute (A-STAR), Singapore, Singapore.ORCID 0000-0003-2766-4459
Roland G HuberBioinformatics Institute (A-STAR), Singapore, Singapore.ORCID 0000-0001-5093-5988
Peter J BondBioinformatics Institute (A-STAR), Singapore, Singapore.ORCID 0000-0003-2900-098X
Benjamin BardiauxInstitut Pasteur, Université Paris Cité, CNRS UMR 3528, Structural Bioinformatics Unit, Paris, France.ORCID 0000-0003-4014-9195
Olivera FranceticInstitut Pasteur, Université Paris Cité, CNRS UMR 3528, Biochemistry of Macromolecular Interactions Unit, Paris, France.ORCID 0000-0002-4145-5314
Agency for Science, Technology and Research · SGCentre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche (ANR) ANR-14-CE09-0004Agence Nationale de la Recherche (ANR) ANR-16-CONV-0005Agence Nationale de la Recherche (ANR) ANR-19-CE11-0020Agence Nationale de la Recherche (ANR) ANR-22-CE95-0001-01
6 · The paper itself

Abstract

importanceType IV pili and type II secretion systems are members of the widespread type IV filament (T4F) superfamily of nanomachines that assemble dynamic and versatile surface fibers in archaea and bacteria. The assembly and retraction of T4 filaments with diverse surface properties and functions require the plasma membrane platform proteins of the GspF/PilC superfamily. Generally considered dimeric, platform proteins are thought to function as passive transmitters of the mechanical energy generated by the ATPase motor, to somehow promote insertion of pilin subunits into the nascent pilus fibers. Here, we generate and experimentally validate structural predictions that support the trimeric state of a platform protein PulF from a type II secretion system. The PulF trimers form selective proton or sodium channels which might energize pilus assembly using the membrane potential. The conservation of the channel sequence and structural features implies a common mechanism for all T4F assembly systems. We propose a model of the oligomeric PulF-PulE ATPase complex that provides an essential framework to investigate and understand the pilus assembly mechanism.

Indexed as

Type II Secretion SystemsAdenosine TriphosphatasesFimbriae, BacterialFimbriae ProteinsIon ChannelsKlebsiellaAdenosine TriphosphatasesFimbriae ProteinsIon ChannelsType II Secretion SystemsAlphaFold2cardiolipinion channelion motive forceresidue coevolutiontype II secretion systemtype IV filamentstype IV pili

Identifiers

PMID38063437
PMCPMC10790770
OpenAlexW4389488396

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.