Evidence map›Paper›PMID 22926563›Full record

ArticleAntimicrobial agents and chemotherapy2012

Proteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane.

Michaela Wenzel, Bastian Kohl, Daniela Münch, Nadja Raatschen, H Bauke Albada, Leendert Hamoen, Nils Metzler-Nolte, Hans-Georg Sahl, Julia E Bandow

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
7.4field-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

43 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
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  20. THCz: Small molecules with antimicrobial activity that block cell wall lipid intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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 3 institutions in 2 countries.

Michaela WenzelBiology of Microorganisms, Ruhr University Bochum, Bochum, Germany.
Bastian Kohl
Daniela Münch
Nadja Raatschen
H Bauke Albada
Leendert Hamoen
Nils Metzler-Nolte
Hans-Georg Sahl
Julia E Bandow
Ruhr University Bochum · DEUniversity of Bonn · DENewcastle University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mersacidin, gallidermin, and nisin are lantibiotics, antimicrobial peptides containing lanthionine. They show potent antibacterial activity. All three interfere with cell wall biosynthesis by binding lipid II, but they display different levels of interaction with the cytoplasmic membrane. On one end of the spectrum, mersacidin interferes with cell wall biosynthesis by binding lipid II without integrating into bacterial membranes. On the other end of the spectrum, nisin readily integrates into membranes, where it forms large pores. It destroys the membrane potential and causes leakage of nutrients and ions. Gallidermin, in an intermediate position, also readily integrates into membranes. However, pore formation occurs only in some bacteria and depends on membrane composition. In this study, we investigated the impact of nisin, gallidermin, and mersacidin on cell wall integrity, membrane pore formation, and membrane depolarization in Bacillus subtilis. The impact of the lantibiotics on the cell envelope was correlated to the proteomic response they elicit in B. subtilis. By drawing on a proteomic response library, including other envelope-targeting antibiotics such as bacitracin, vancomycin, gramicidin S, or valinomycin, YtrE could be identified as the most reliable marker protein for interfering with membrane-bound steps of cell wall biosynthesis. NadE and PspA were identified as markers for antibiotics interacting with the cytoplasmic membrane.

Indexed as

Bacillus subtilisBacterial ProteinsBacteriocinsBiological TransportBiomarkersCell MembraneCell WallElectrophoresis, Gel, Two-DimensionalMembrane PotentialsNisinPeptidesPotassiumProteomeStructure-Activity RelationshipUridine Diphosphate N-Acetylmuramic AcidBacterial ProteinsBacteriocinsBiomarkersgalliderminmersacidinmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolNisinnisin APeptidesPotassiumProteomeUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID22926563
PMCPMC3486579
OpenAlexW2137245829

What OpenQuestion holds

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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.