Evidence map›Paper›PMID 23062338›Full record

ArticleBiophysical journal2012

Peptide-lipid interactions of the stress-response peptide TisB that induces bacterial persistence.

Thomas Steinbrecher, Sebastian Prock, Johannes Reichert, Parvesh Wadhwani, Benjamin Zimpfer, Jochen Bürck, Marina Berditsch, Marcus Elstner, Anne S Ulrich

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mechanism of action ofFrontiers in microbiology · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Phosphate-dependent aggregation of [KL]Scientific reports · 2020
    Article
  15. Article
  16. Characterization of an OrtT-like toxin of Salmonella enterica serovar Houten.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2019
    Article
  17. mBio · 2019
    Article
  18. Article
  19. Article
  20. Article
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 1 institution in 1 country.

Thomas SteinbrecherInstitute of Physical Chemistry, Karlsruhe Institute of Technology, Karlsruhe, Germany.
Sebastian Prock
Johannes Reichert
Parvesh Wadhwani
Benjamin Zimpfer
Jochen Bürck
Marina Berditsch
Marcus Elstner
Anne S Ulrich
Karlsruhe Institute of Technology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial stress-response peptide TisB in Escherichia coli has been suggested to dissipate the transmembrane potential, such that the depletion of ATP levels induces the formation of dormant persister cells which can eventually form biofilms. We studied the structure and membrane interactions of TisB to find out whether it forms pores or other proton-selective channels. Circular dichroism revealed an amphiphilic α-helical structure when reconstituted in lipid vesicles, and oriented circular dichroism showed that the helix assumes a transmembrane alignment. The addition of TisB to dye-loaded vesicles caused leakage only at very high peptide concentration, notably with a Hill coefficient of 2, which suggests that dimers must be involved. Coarse-grained molecular dynamics simulations showed that membrane binding of monomeric TisB is rapid and spontaneous, and transmembrane insertion is energetically feasible. When TisB oligomers are assembled as transmembrane pores, these channels collapse during the simulations, but transmembrane dimers are found to be stable. Given the pattern of charges on the amphiphilic TisB helix, we postulate that antiparallel dimers could be assembled via a ladder of salt bridges. This electrostatic charge-zipper could enable protons to pass along a wire of trapped water molecules across the hydrophobic membrane.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceBacterial ToxinsCell MembraneEscherichia coliEscherichia coli ProteinsLipid BilayersMolecular Sequence DataPeptide FragmentsPorosityProtein BindingProtein MultimerizationProtein Structure, QuaternaryStress, PhysiologicalThermodynamicsUnilamellar LiposomesBacterial ToxinsEscherichia coli ProteinsLipid BilayersPeptide FragmentsTisB toxin, E coliUnilamellar Liposomes

Identifiers

PMID23062338
PMCPMC3471478
OpenAlexW2053518734

What OpenQuestion holds

Textmetadata
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.