ArticleFrontiers in microbiology2015
Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 18 citations in OpenAlex.
- Genetic Characterisation of Closely RelatedInternational journal of molecular sciences · 2025Article
- Isolation and Proteomic Analysis of Extracellular Vesicles fromJournal of microbiology and biotechnology · 2024Article
- Generation of Lactose- and Protease-Positive ProbioticApplied and environmental microbiology · 2021Article
- Natural bacterial isolates as an inexhaustible source of new bacteriocins.Applied microbiology and biotechnology · 2021Review
- Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion inFrontiers in microbiology · 2019Article
- Functional Characterization of the Lactolisterin BU Gene Cluster ofFrontiers in microbiology · 2018Article
- LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor.Applied and environmental microbiology · 2016Article
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Authors and funding
8 authors at 1 institution in 1 country.
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Abstract
Proteinases and bacteriocins are of great importance to the dairy industry, but their interactions have not been studied so far. Lactococcus lactis subsp. lactis BGMN1-5 is a natural isolate from homemade semi-hard cheese which produces two bacteriocins (Lactococcin B and LsbB), as well as proteinase PrtP. A medium-dependent increase in the bacteriocin LcnB activity of L. lactis BGMN1-501, a derivate of L. lactis subsp. lactis BGMN1-5, was shown to be accompanied by a decrease in its promoter activity. A similar effect of media components on gene expression was reported for proteinase PrtP, whose gene is co-localized on the same plasmid as the lcnB gene. Thus, the PrtP-LcnB interplay was investigated. Single gene knockout mutants were constructed with disrupted prtP or lcnB genes. PrtP(-) mutants showed higher bacteriocin activity that had lost its growth medium dependence, which was in contrast to the original strain. When LcnB from this mutant was combined with proteinase from the LcnB(-) mutant in vitro, its activity was rendered to the original level, suggesting that proteinase reduces bacteriocin activity. We propose a new model of medium dependent expression of these genes with regard to the effects of their interaction in vivo.
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