Evidence map›Paper›PMID 26083926›Full record

ArticleBiophysical journal2015

Nanoscale Pulling of Type IV Pili Reveals Their Flexibility and Adhesion to Surfaces over Extended Lengths of the Pili.

Shun Lu, Maximiliano Giuliani, Hanjeong Harvey, Lori L Burrows, Robert A Wickham, John R Dutcher

Abstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024
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  7. Proceedings of the National Academy of Sciences of the United States of America · 2022
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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.

Shun LuDepartment of Physics, University of Guelph, Guelph, Ontario, Canada.
Maximiliano GiulianiDepartment of Physics, University of Guelph, Guelph, Ontario, Canada.
Hanjeong HarveyDepartment of Biochemistry and Biomedical Science, McMaster University, Hamilton, Ontario, Canada.
Lori L BurrowsDepartment of Biochemistry and Biomedical Science, McMaster University, Hamilton, Ontario, Canada.
Robert A WickhamDepartment of Physics, University of Guelph, Guelph, Ontario, Canada.
John R DutcherDepartment of Physics, University of Guelph, Guelph, Ontario, Canada. Electronic address: dutcher@uoguelph.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type IV pili (T4P) are very thin protein filaments that extend from and retract into bacterial cells, allowing them to interact with and colonize a broad array of chemically diverse surfaces. The physical aspects that allow T4P to mediate adherence to many different surfaces remain unclear. Atomic force microscopy (AFM) nanoscale pulling experiments were used to measure the mechanical properties of T4P of a mutant strain of Pseudomonas aeruginosa PAO1 unable to retract its T4P. After adhering bacteria to the end of an AFM cantilever and approaching surfaces of mica, gold, or polystyrene, we observed adhesion of the T4P to all of the surfaces. Pulling of single and multiple T4P on retraction of the cantilever from the surfaces could be described using the worm-like chain (WLC) model. Distinct peaks in the measured distributions of the best-fit values of the persistence length Lp on two different surfaces provide strong evidence for close-packed bundling of very flexible T4P. In addition, we observed force plateaus indicating that adhesion of the T4P to both hydrophilic and hydrophobic surfaces occurs along extended lengths of the T4P. These data shed new light, to our knowledge, on T4P flexibility and support a low-affinity, high-avidity adhesion mechanism that mediates bacteria-surface interactions.

Indexed as

Bacterial AdhesionAmino Acid SequenceBiomechanical PhenomenaFimbriae, BacterialFimbriae ProteinsMolecular Sequence DataMutationPseudomonas aeruginosaFimbriae Proteins

Identifiers

PMID26083926
PMCPMC4472224

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.