Evidence map›Paper›PMID 27471053›Full record

ArticleNature communications2016

Antimicrobial peptides trigger a division block in Escherichia coli through stimulation of a signalling system.

Srujana S Yadavalli, Jeffrey N Carey, Rachel S Leibman, Annie I Chen, Andrew M Stern, Manuela Roggiani, Andrew M Lippa, Mark Goulian

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

41 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Hijacking competitor-derived signals: RcsB/C drivesApplied and environmental microbiology · 2026
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  7. Analysis of stress-induced small proteins inbioRxiv : the preprint server for biology · 2025
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  12. Enhancing the Efficacy of Chloramphenicol Therapy forAntibiotics (Basel, Switzerland) · 2024
    Article
  13. Review
  14. Article
  15. The inhibitory mechanism of a small protein reveals its role in antimicrobial peptide sensing.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. TheFrontiers in microbiology · 2022
    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

8 authors at 2 institutions in 1 country.

Srujana S YadavalliDepartment of Biology, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Jeffrey N CareyDepartment of Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.ORCID 0000-0002-5105-0265
Rachel S LeibmanDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Annie I ChenDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Andrew M SternDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Manuela RoggianiDepartment of Biology, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Andrew M LippaDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Mark GoulianDepartment of Biology, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
University of Pennsylvania · USUniversity of the Arts · US

Funding

Regulation of Bacterial Two-Component Signaling by Small Membrane ProteinsR01GM080279 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GOULIAN, MARK D · 2007 to 2020
$3.7M
Training in bacteriologyT32AI060516 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI GOULIAN, MARK D, ZHU, JUN · 2006 to 2015
$2.0M
NIAID NIH HHS T32 AI060516NIGMS NIH HHS R01 GM080279
6 · The paper itself

Abstract

Antimicrobial peptides are an important component of the molecular arsenal employed by hosts against bacteria. Many bacteria in turn possess pathways that provide protection against these compounds. In Escherichia coli and related bacteria, the PhoQ/PhoP signalling system is a key regulator of this antimicrobial peptide defence. Here we show that treating E. coli with sublethal concentrations of antimicrobial peptides causes cells to filament, and that this division block is controlled by the PhoQ/PhoP system. The filamentation results from increased expression of QueE, an enzyme that is part of a tRNA modification pathway but that, as we show here, also affects cell division. We also find that a functional YFP-QueE fusion localizes to the division septum in filamentous cells, suggesting QueE blocks septation through interaction with the divisome. Regulation of septation by PhoQ/PhoP may protect cells from antimicrobial peptide-induced stress or other conditions associated with high-level stimulation of this signalling system.

Indexed as

Antimicrobial Cationic PeptidesBiosynthetic PathwaysCell DivisionChromosome SegregationCytoplasmEscherichia coliEscherichia coli ProteinsGene DeletionGene Expression Regulation, BacterialModels, BiologicalNucleoside QSignal TransductionTranscription, GeneticAntimicrobial Cationic PeptidesEscherichia coli ProteinsNucleoside QPhoQ protein, E coli

Identifiers

PMID27471053
PMCPMC4974570
OpenAlexW2484704120

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.