Evidence map›Paper›PMID 29795541›Full record

ArticleNature microbiology2018

Antibiotic-resistant bacteria show widespread collateral sensitivity to antimicrobial peptides.

Viktória Lázár, Ana Martins, Réka Spohn, Lejla Daruka, Gábor Grézal, Gergely Fekete, Mónika Számel, Pramod K Jangir, Bálint Kintses, Bálint Csörgő and 15 more

Abstract read
In one paragraph

Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 184 papers.

0numbers the graph read from it
0cells of the map it votes in
184citing 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

184 citing papers in PubMed.

  1. Adaptive Response ofAntibiotics (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Molecular mechanisms of disinfectant resistance inJAC-antimicrobial resistance · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. A unified model of transient poration induced by antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Micro- and Nano-Bots for Infection Control.Advanced materials (Deerfield Beach, Fla.) · 2025
    Review
  19. Article
  20. Article

124 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

25 authors.

Viktória Lázár *Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Ana Martins *Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.ORCID http://orcid.org/0000-0002-8541-7440
Réka SpohnSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Lejla DarukaSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Gábor GrézalSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Gergely FeketeSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Mónika SzámelSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Pramod K JangirSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Bálint KintsesSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.ORCID http://orcid.org/0000-0003-0844-0310
Bálint CsörgőSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Ákos NyergesSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Ádám GyörkeiSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
András KincsesBiomolecular Electronics Research Group, Bionanoscience Unit, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
András DérBiomolecular Electronics Research Group, Bionanoscience Unit, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Fruzsina R WalterBiological Barriers Research Group, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Mária A DeliBiological Barriers Research Group, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.ORCID http://orcid.org/0000-0001-6084-6524
Edit UrbánInstitute of Clinical Microbiology, Albert Szent-Györgyi Medical and Pharmaceutical Center, Faculty of Medicine, University of Szeged, Szeged, Hungary.
Zsófia HegedűsInstitute of Pharmaceutical Analysis, University of Szeged, Szeged, Hungary.
Gábor OlajosInstitute of Pharmaceutical Analysis, University of Szeged, Szeged, Hungary.
Orsolya MéhiSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
Balázs BálintSeqOmics Biotechnology Ltd, Mórahalom, Hungary.ORCID http://orcid.org/0000-0002-5102-0787
István NagySeqOmics Biotechnology Ltd, Mórahalom, Hungary.ORCID http://orcid.org/0000-0003-2528-9173
Tamás A MartinekInstitute of Pharmaceutical Analysis, University of Szeged, Szeged, Hungary.
Balázs PappSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary. pappb@brc.hu.ORCID http://orcid.org/0000-0003-3093-8852
Csaba PálSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary. cpal@brc.hu.ORCID http://orcid.org/0000-0002-5187-9903

Funding

European Research Council 648364Wellcome Trust 084314Wellcome Trust 098016
6 · The paper itself

Abstract

Antimicrobial peptides are promising alternative antimicrobial agents. However, little is known about whether resistance to small-molecule antibiotics leads to cross-resistance (decreased sensitivity) or collateral sensitivity (increased sensitivity) to antimicrobial peptides. We systematically addressed this question by studying the susceptibilities of a comprehensive set of 60 antibiotic-resistant Escherichia coli strains towards 24 antimicrobial peptides. Strikingly, antibiotic-resistant bacteria show a high frequency of collateral sensitivity to antimicrobial peptides, whereas cross-resistance is relatively rare. We identify clinically relevant multidrug-resistance mutations that increase bacterial sensitivity to antimicrobial peptides. Collateral sensitivity in multidrug-resistant bacteria arises partly through regulatory changes shaping the lipopolysaccharide composition of the bacterial outer membrane. These advances allow the identification of antimicrobial peptide-antibiotic combinations that enhance antibiotic activity against multidrug-resistant bacteria and slow down de novo evolution of resistance. In particular, when co-administered as an adjuvant, the antimicrobial peptide glycine-leucine-amide caused up to 30-fold decrease in the antibiotic resistance level of resistant bacteria. Our work provides guidelines for the development of efficient peptide-based therapies of antibiotic-resistant infections.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesBacterial Outer Membrane ProteinsDrug Resistance, Multiple, BacterialDrug SynergismEscherichia coliEscherichia coli ProteinsMicrobial Sensitivity TestsMutationSmall Molecule LibrariesAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacterial Outer Membrane ProteinsEscherichia coli Proteinspeptide-Gly-Leu-amideSmall Molecule Libraries

Identifiers

PMID29795541
PMCPMC6544545

What OpenQuestion holds

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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.