Evidence map›Paper›PMID 24349428›Full record

ArticlePloS one2013

Characterization of amylolysin, a novel lantibiotic from Bacillus amyloliquefaciens GA1.

Anthony Arguelles Arias, Marc Ongena, Bart Devreese, Mohammed Terrak, Bernard Joris, Patrick Fickers

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.4field-weighted citation impact, top 4% 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

20 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Review
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  4. Frontiers in plant science · 2024
    Review
  5. Review
  6. AntimicrobialAntibiotics (Basel, Switzerland) · 2022
    Review
  7. Article
  8. Mechanism of Antibacterial Activity ofBioMed research international · 2020
    Article
  9. Frontiers in microbiology · 2020
    Review
  10. Molecules (Basel, Switzerland) · 2019
    Review
  11. Review
  12. Article
  13. Secretome of IntestinalFrontiers in microbiology · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

6 authors at 4 institutions in 1 country.

Anthony Arguelles AriasCentre d'Ingénierie des Protéines, Bacterial Physiology and Genetics, Université de Liège, Liège, Belgium.
Marc OngenaCentre Wallon de Biologie Industrielle, Unité de Bioindustrie, Faculté de Sciences Agronomique de Gembloux, Gembloux, Belgium .
Bart DevreeseLaboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit-Gent, Gent, Belgium.
Mohammed TerrakCentre d'Ingénierie des Protéines, Bacterial Physiology and Genetics, Université de Liège, Liège, Belgium.
Bernard JorisCentre d'Ingénierie des Protéines, Bacterial Physiology and Genetics, Université de Liège, Liège, Belgium.
Patrick FickersUnité de Biotechnologies et Bioprocédés, Université Libre de Bruxelles, Brussels, Belgium.
Physiol (Belgium) · BEGembloux Agro-Bio Tech · BEGhent University · BEUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundLantibiotics are heat-stable peptides characterized by the presence of thioether amino acid lanthionine and methyllanthionine. They are capable to inhibit the growth of Gram-positive bacteria, including Listeria monocytogenes, Staphylococcus aureus or Bacillus cereus, the causative agents of food-borne diseases or nosocomial infections. Lantibiotic biosynthetic machinery is encoded by gene cluster composed by a structural gene that codes for a pre-lantibiotic peptide and other genes involved in pre-lantibiotic modifications, regulation, export and immunity. METHODOLOGY/

findingsBacillus amyloliquefaciens GA1 was found to produce an antimicrobial peptide, named amylolysin, active on an array of Gram-positive bacteria, including methicillin resistant S. aureus. Genome characterization led to the identification of a putative lantibiotic gene cluster that comprises a structural gene (amlA) and genes involved in modification (amlM), transport (amlT), regulation (amlKR) and immunity (amlFE). Disruption of amlA led to loss of biological activity, confirming thus that the identified gene cluster is related to amylolysin synthesis. MALDI-TOF and LC-MS analysis on purified amylolysin demonstrated that this latter corresponds to a novel lantibiotic not described to date. The ability of amylolysin to interact in vitro with the lipid II, the carrier of peptidoglycan monomers across the cytoplasmic membrane and the presence of a unique modification gene suggest that the identified peptide belongs to the group B lantibiotic. Amylolysin immunity seems to be driven by only two AmlF and AmlE proteins, which is uncommon within the Bacillus genus. CONCLUSION/SIGNIFICANCE: Apart from mersacidin produced by Bacillus amyloliquefaciens strains Y2 and HIL Y-85,544728, reports on the synthesis of type B-lantibiotic in this species are scarce. This study reports on a genetic and structural characterization of another representative of the type B lantibiotic in B. amyloliquefaciens.

Indexed as

Bacterial ProteinsGenes, BacterialBacillusBacteriocinsGram-Positive BacteriaUridine Diphosphate N-Acetylmuramic Acidamylolysin, Bacillus amyloliquefaciens GA1Bacterial ProteinsBacteriocinsmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID24349428
PMCPMC3857288
OpenAlexW2085966015

What OpenQuestion holds

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LicenceCC BY
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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.