Cited by 280Probiotics and Fermented FoodsAntimicrobial Peptides and ActivitiesBacterial Genetics and Biotechnology

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Antagonistic Activity of Lactobacillus plantarum C11: Two New Two-Peptide Bacteriocins, Plantaricins EF and JK, and the Induction Factor Plantaricin A

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Anderssen, Erlend L., Diep, Dzung Bao, Nes, Ingolf F., Eijsink, Vincent G. H., Nissen-Meyer, Jon·1998·Applied and Environmental Microbiology

DOI 10.1128/aem.64.6.2269-2272.1998PMC PMC106311

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Abstract

Six bacteriocinlike peptides (plantaricin A [PlnA], PlnE, PlnF, PlnJ, PlnK, and PlnN) produced by Lactobacillus plantarum C11 were detected by amino acid sequencing and mass spectrometry. Since purification to homogeneity was problematic, all six peptides were obtained by solid-phase peptide synthesis and were tested for bacteriocin activity. It was found that L. plantarum C11 produces two two-peptide bacteriocins (PlnEF and PlnJK); a strain-specific antagonistic activity was detected at nanomolar concentrations when PlnE and PlnF were combined and when PlnJ and PlnK were combined. Complementary peptides were at least 10(3) times more active when they were combined than when they were present individually, and optimal activity was obtained when the complementary peptides were present in approximately equal amounts. The interaction between complementary peptides was specific, since neither PlnE nor PlnF could complement PlnJ or PlnK, and none of these peptides could complement the peptides constituting the two-peptide bacteriocin lactococcin G. Interestingly, PlnA, which acts as an extracellular signal (pheromone) that triggers bacteriocin production, also possessed a strain-specific antagonistic activity. No bacteriocin activity could be detected for PlnN.

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Authors: Anderssen, E. L., Diep, D. B., Nes, I. F., Eijsink, V. G. H., & Nissen-Meyer, J.
Affiliations: University of Oslo (NO)
Norwegian University of Life Sciences (NO)
ORCID: Diep, Dzung Bao
Eijsink, Vincent G. H.
Venue: Applied and Environmental Microbiology
Publisher: American Society for Microbiology
Published: 1998-06
Volume: 64
Issue: 6
Pages: 2269-2272
ISSN: 0099-2240 (ISSN-L)
1098-5336
DOI: 10.1128/aem.64.6.2269-2272.1998
PMC: PMC106311
OpenAlex: W2163836917
Cited by: 280
References: 33
Citations by year: 2026: 12 · 2025: 9 · 2024: 13 · 2023: 3 · 2022: 5 · 2021: 8 · 2020: 12 · 2019: 17 · 2018: 4 · 2017: 13 · 2016: 16 · 2015: 9 · 2014: 10 · 2013: 10 · 2012: 15
FWCI: 25.85
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Applied and Environmental Microbiology (publishedVersion)
PubMed Central (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed (publishedVersion)
Funders: Norges Forskningsråd
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: bacteriocins, two-peptide bacteriocin, plantaricin, bacteriocin-like peptides, pheromones, complementary peptides, lactic acid bacteria
MeSH terms: Amino Acid Sequence, Bacteriocins, Drug Interactions, Genes, Bacterial, Lactobacillus, Molecular Sequence Data

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Antagonistic Activity of Lactobacillus plantarum C11: Two New Two-Peptide Bacteriocins, Plantaricins EF and JK, and the Induction Factor Plantaricin A

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