Evidence map›Paper›PMID 29625984›Full record

ArticleApplied and environmental microbiology2018

Increasing the Antimicrobial Activity of Nisin-Based Lantibiotics against Gram-Negative Pathogens.

Qian Li, Manuel Montalban-Lopez, Oscar P Kuipers

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
17.9field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
  2. Structure and Activity of Class II Lanthipeptides From a Thermophilic Bacterium.Chembiochem : a European journal of chemical biology · 2026
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  11. Hijacking the Electron Train: Menaquinone-Binding Antimicrobial Peptides.Chembiochem : a European journal of chemical biology · 2025
    Review
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  16. Article
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12 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

3 authors at 2 institutions in 2 countries.

Qian LiDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands.
Manuel Montalban-LopezDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands.
Oscar P KuipersDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands o.p.kuipers@rug.nl.
University of Groningen · NLUniversidad de Granada · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lantibiotics are ribosomally synthesized and posttranslationally modified antimicrobial compounds containing lanthionine and methyl-lanthionine residues. Nisin, one of the most extensively studied and used lantibiotics, has been shown to display very potent activity against Gram-positive bacteria, and stable resistance is rarely observed. By binding to lipid II and forming pores in the membrane, nisin can cause the efflux of cellular constituents and inhibit cell wall biosynthesis. However, the activity of nisin against Gram-negative bacteria is much lower than that against Gram-positive bacteria, mainly because lipid II is located at the inner membrane, and the rather impermeable outer membrane in Gram-negative bacteria prevents nisin from reaching lipid II. Thus, if the outer membrane-traversing efficiency of nisin could be increased, the activity against Gram-negative bacteria could, in principle, be enhanced. In this work, several relatively short peptides with activity against Gram-negative bacteria were selected from literature data to be fused as tails to the C terminus of either full or truncated nisin species. Among these, we found that one of three tails (tail 2 [T2; DKYLPRPRPV], T6 [NGVQPKY], and T8 [KIAKVALKAL]) attached to a part of nisin displayed improved activity against Gram-negative microorganisms. Next, we rationally designed and reengineered the most promising fusion peptides. Several mutants whose activity significantly outperformed that of nisin against Gram-negative pathogens were obtained. The activity of the tail 16 mutant 2 (T16m2) construct against several important Gram-negative pathogens (i.e.,

Indexed as

Anti-Bacterial AgentsBacteriocinsEscherichia coliGram-Negative BacteriaMicrobial Sensitivity TestsMutationNisinPseudomonas aeruginosaRecombinant Fusion ProteinsAnti-Bacterial AgentsBacteriocinsNisinRecombinant Fusion Proteinsantimicrobial activityantimicrobial peptideGram-negative pathogenslantibioticnisinouter membrane

Identifiers

PMID29625984
PMCPMC5981070
OpenAlexW2795587983

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.