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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
Open accessAbstract
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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“The presence of six bacteriocin-like structures encoding genes (PlnA, PlnE, PlnF, PlnJ, PlnK, and PlnN) in the genome of L. plantarum 55A makes the strain similar to L. plantarum C11 [52] in that respect.”
From Genomic Characterization of Lactiplantibacillus plantarum Strains: Potential Probiotics from Ethiopian Traditional Fermented Cottage Cheese (2024) · cites this paper as [52]
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Metadata
- 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)
- 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
- 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
- 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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