Evidence map›Paper›PMID 31626631›Full record

ArticlePLoS genetics2019

PilT and PilU are homohexameric ATPases that coordinate to retract type IVa pili.

Jennifer L Chlebek, Hannah Q Hughes, Aleksandra S Ratkiewicz, Rasman Rayyan, Joseph Che-Yen Wang, Brittany E Herrin, Triana N Dalia, Nicolas Biais, Ankur B Dalia

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.8field-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

50 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
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  4. 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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  12. Phenotypic Characterization ofAntibiotics (Basel, Switzerland) · 2025
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  13. Environmental DNA adsorption to chitin can promote horizontal gene transfer by natural transformation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
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  16. Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2025
    Review
  17. Article
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  19. Review
  20. Type IV pili ofEcoSal Plus · 2024
    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

9 authors at 2 institutions in 1 country.

Jennifer L ChlebekDepartment of Biology, Indiana University, Bloomington, Indiana, United States of America.ORCID 0000-0002-1744-0016
Hannah Q HughesDepartment of Biology, Indiana University, Bloomington, Indiana, United States of America.ORCID 0000-0002-8335-2612
Aleksandra S RatkiewiczBiology Department and Graduate Center, City University of New York, Brooklyn, New York, United States of America.
Rasman RayyanBiology Department and Graduate Center, City University of New York, Brooklyn, New York, United States of America.ORCID 0000-0002-6730-6237
Joseph Che-Yen WangElectron Microscopy Center, Indiana University, Bloomington, Indiana, United States of America.ORCID 0000-0001-6580-3531
Brittany E HerrinDepartment of Biology, Indiana University, Bloomington, Indiana, United States of America.ORCID 0000-0003-0479-9510
Triana N DaliaDepartment of Biology, Indiana University, Bloomington, Indiana, United States of America.ORCID 0000-0001-7614-1377
Nicolas BiaisBiology Department and Graduate Center, City University of New York, Brooklyn, New York, United States of America.
Ankur B DaliaDepartment of Biology, Indiana University, Bloomington, Indiana, United States of America.ORCID 0000-0003-2203-1230
Indiana University Bloomington · USThe Graduate Center, CUNY · US

Funding

Mechanisms and regulation of horizontal gene transfer by natural transformation in Vibrio choleraeR35GM128674 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI Ankur Dalia · 2018 to 2026
$3.8M
Mechanobiology of Neisseria MicrocoloniesSC2AI116566 · NIAID · BROOKLYN COLLEGE · PI BIAIS, NICOLAS · 2014 to 2016
$471k
Vibrio cholerae-chitin interactions and their role in cholera transmission and evolutionK22AI118863 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI DALIA, ANKUR · 2016 to 2017
$268k
NIAID NIH HHS K22 AI118863NIAID NIH HHS SC2 AI116566NIGMS NIH HHS R35 GM128674
6 · The paper itself

Abstract

Bacterial type IV pili are critical for diverse biological processes including horizontal gene transfer, surface sensing, biofilm formation, adherence, motility, and virulence. These dynamic appendages extend and retract from the cell surface. In many type IVa pilus systems, extension occurs through the action of an extension ATPase, often called PilB, while optimal retraction requires the action of a retraction ATPase, PilT. Many type IVa systems also encode a homolog of PilT called PilU. However, the function of this protein has remained unclear because pilU mutants exhibit inconsistent phenotypes among type IV pilus systems and because it is relatively understudied compared to PilT. Here, we study the type IVa competence pilus of Vibrio cholerae as a model system to define the role of PilU. We show that the ATPase activity of PilU is critical for pilus retraction in PilT Walker A and/or Walker B mutants. PilU does not, however, contribute to pilus retraction in ΔpilT strains. Thus, these data suggest that PilU is a bona fide retraction ATPase that supports pilus retraction in a PilT-dependent manner. We also found that a ΔpilU mutant exhibited a reduction in the force of retraction suggesting that PilU is important for generating maximal retraction forces. Additional in vitro and in vivo data show that PilT and PilU act as independent homo-hexamers that may form a complex to facilitate pilus retraction. Finally, we demonstrate that the role of PilU as a PilT-dependent retraction ATPase is conserved in Acinetobacter baylyi, suggesting that the role of PilU described here may be broadly applicable to other type IVa pilus systems.

Indexed as

AcinetobacterAdenosine TriphosphatasesFimbriae, BacterialFimbriae ProteinsMutationProtein MultimerizationVibrio choleraeAdenosine TriphosphatasesFimbriae Proteins

Identifiers

PMID31626631
PMCPMC6821130
OpenAlexW2980615774

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.