Evidence map›Paper›PMID 31894376›Full record

ArticleCurrent microbiology2020

Characterization of New Fengycin Cyclic Lipopeptide Variants Produced by Bacillus amyloliquefaciens (ET) Originating from a Salt Lake of Eastern Algeria.

Asma Ait Kaki, Nicolas Smargiasso, Marc Ongena, Mounira Kara Ali, Nassim Moula, Edwin De Pauw, Noreddine Kacem Chaouche

Abstract read
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Article in Current microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Broad antibiosis activity ofFrontiers in microbiology · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Lipopeptides from Bacillus: unveiling biotechnological prospects-sources, properties, and diverse applications.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Review
  9. Article
  10. Characterization ofantifungal properties of lipopeptide-producingFrontiers in bioengineering and biotechnology · 2023
    Article
  11. Article
  12. Bacillus sp.: A Remarkable Source of Bioactive Lipopeptides.Advances in biochemical engineering/biotechnology · 2022
    Article
  13. Metabolic Profiling of RhizobacteriaFrontiers in microbiology · 2021
    Article
  14. 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

7 authors at 4 institutions in 2 countries.

Asma Ait KakiFaculty of Sciences, Department of Biology, University of M'Hamed Bougara, 35000, Boumerdès, Algeria. askaki.biotechno@gmail.com.
Nicolas SmargiassoMass Spectrometry Laboratory, Molecular Systems Research Unit, University of Liege, B6C, B 400, Liege, Belgium.
Marc OngenaBioindustries Unit, Gembloux Agrobiotech, University of Liege, Passage of the Deportees 2, 5030, Gembloux, Belgium.
Mounira Kara AliLaboratory of Mycology, Biology and Biotechnology, Faculty of Natural and Life Sciences, Department of Applied Biology, University of Mentouri 1, 25000, Constantine, Algeria.
Nassim MoulaDepartment of Animal Productions, Faculty of Veterinary Medicine, University of Liege, Colonster Boulevard 20, 4000, Liege, Belgium.
Edwin De PauwMass Spectrometry Laboratory, Molecular Systems Research Unit, University of Liege, B6C, B 400, Liege, Belgium.
Noreddine Kacem ChaoucheLaboratory of Mycology, Biology and Biotechnology, Faculty of Natural and Life Sciences, Department of Applied Biology, University of Mentouri 1, 25000, Constantine, Algeria.
University of Liège · BEConstantine 1 University · DZGembloux Agro-Bio Tech · BEUniversity of Boumerdes · DZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fengycin antibiotic displays a strong antifungal activity and inhibits the growth of a wide range of plant pathogens especially filamentous fungi. The main objective of the present study is to characterize fengycin variants produced by B. amyloliquefaciens strain (ET). LC-MS analysis of fengycin extracts has shown several molecular ion peaks corresponding to conventional fengycin homologues (MH + : m/z 1463.9; 1491.9; 1506) and some new ones (MH + : m/z 1433; 1447; 1461; and 1477). Further characterization of these precursor ions was carried out by LC-MS.MS analysis. Reporter fragment ions were observed (named A and B), they correspond to the cleavage of Orn2-Tyr3 (A), Glu1-Orn2 (B), and used for identifying fengycin variants. The reporter fragment couple ions [A/B] at [m/z 966.5/1080.5] and [m/z 994.4 /1108.5] represent fengycin A and B, respectively. The diagnostic ions at ([m/z 980/1094]) may correspond to fengycin C3, D, S or B2. Interestingly, unknown diagnostic product ions at [m/z 951/1065] and [m/z 979/1093] were detected for the first time in this study which prove that they correspond to new fengycin variants, named fengycin X and fengycin Y, respectively. The fengycin X results from a substitution of the glutamine amino acid (Q), at position 8 of the fengycin A peptide part, by an isoleucine (I) or a leucine (L) residue. This mutation should be the same in fengycin Y but compared to fengycin B.

Indexed as

AlgeriaAmino Acid SubstitutionBacillus amyloliquefaciensGlutamineIsoleucineLakesLeucineLipopeptidesMutationSaline WatersTandem Mass SpectrometryfengycinGlutamineIsoleucineLeucineLipopeptides

Identifiers

PMID31894376
OpenAlexW2997971672

What OpenQuestion holds

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Registered trials

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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.