Evidence map›Paper›PMID 30301848›Full record

ArticlemBio2018

The Multifaceted Antibacterial Mechanisms of the Pioneering Peptide Antibiotics Tyrocidine and Gramicidin S.

Michaela Wenzel, Marina Rautenbach, J Arnold Vosloo, Tjalling Siersma, Christopher H M Aisenbrey, Ekaterina Zaitseva, Wikus E Laubscher, Wilma van Rensburg, Jan C Behrends, Burkhard Bechinger and 1 more

Open access · goldAbstract read
In one paragraph

Article in mBio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 129 citations in OpenAlex.

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6 more citing papers are in PubMed but not listed here.

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

11 authors at 5 institutions in 4 countries.

Michaela WenzelBacterial Cell Biology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands m.wenzel@uva.nl l.w.hamoen@uva.nl.ORCID 0000-0001-9969-6113
Marina RautenbachBIOPEP Peptide Group, Department of Biochemistry, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.
J Arnold VoslooBIOPEP Peptide Group, Department of Biochemistry, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.
Tjalling SiersmaBacterial Cell Biology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands.
Christopher H M AisenbreyChemistry Institute UMR7177, University of Strasbourg/CNRS, Strasbourg, France.
Ekaterina ZaitsevaDepartment of Physiology, Laboratory for Membrane Physiology and Technology, University of Freiburg, Freiburg, Germany.
Wikus E LaubscherBIOPEP Peptide Group, Department of Biochemistry, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.
Wilma van RensburgBIOPEP Peptide Group, Department of Biochemistry, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.
Jan C BehrendsDepartment of Physiology, Laboratory for Membrane Physiology and Technology, University of Freiburg, Freiburg, Germany.
Burkhard BechingerChemistry Institute UMR7177, University of Strasbourg/CNRS, Strasbourg, France.
Leendert W HamoenBacterial Cell Biology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands m.wenzel@uva.nl l.w.hamoen@uva.nl.ORCID 0000-0001-9251-1403
Stellenbosch University · ZACentre National de la Recherche Scientifique · FRUniversity of Amsterdam · NLUniversity of Freiburg · DEAmsterdam University Medical Centers · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic β-sheet decapeptides from the tyrocidine group and the homologous gramicidin S were the first commercially used antibiotics, yet it remains unclear exactly how they kill bacteria. We investigated their mode of action using a bacterial cytological profiling approach. Tyrocidines form defined ion-conducting pores, induce lipid phase separation, and strongly reduce membrane fluidity, resulting in delocalization of a broad range of peripheral and integral membrane proteins. Interestingly, they also cause DNA damage and interfere with DNA-binding proteins. Despite sharing 50% sequence identity with tyrocidines, gramicidin S causes only mild lipid demixing with minor effects on membrane fluidity and permeability. Gramicidin S delocalizes peripheral membrane proteins involved in cell division and cell envelope synthesis but does not affect integral membrane proteins or DNA. Our results shed a new light on the multifaceted antibacterial mechanisms of these antibiotics and explain why resistance to them is virtually nonexistent.

Indexed as

Anti-Bacterial AgentsBacillus subtilisCell MembraneCell WallDNA-Binding ProteinsDNA DamageGramicidinMicrobial Sensitivity TestsMicroscopy, ElectronTyrocidineAnti-Bacterial AgentsDNA-Binding ProteinsGramicidinTyrocidineantibioticsantimicrobial peptidesbacterial cell biologybacterial cytological profilingcell membranesmode of action

Identifiers

PMID30301848
PMCPMC6178620
OpenAlexW2896169578

What OpenQuestion holds

Textmetadata
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.