ArticleMicrobiologyOpen2020
The membrane topology of immunity proteins for the two-peptide bacteriocins carnobacteriocin XY, lactococcin G, and lactococcin MN shows structural diversity.
Article in MicrobiologyOpen, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- The DdD protein confers intracellular and extracellular immunity to the leaderless bacteriocin enterocin DD14.PNAS nexus · 2026Article
- Bacteriocin production facilitates nosocomial emergence of vancomycin-resistant Enterococcus faecium.Nature microbiology · 2025Article
- Current status and potential of bacteriocin-producing lactic acid bacteria applied in the food industry.Current research in food science · 2025Review
- Bacteriocin production facilitates nosocomial emergence of vancomycin-resistantmedRxiv : the preprint server for health sciences · 2024Article
- Characterization of Genomic, Physiological, and Probiotic Features ofFoods (Basel, Switzerland) · 2024Article
- Defining Membrane Protein Topology Using pho-lac Reporter Fusions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Current Knowledge of the Mode of Action and Immunity Mechanisms of LAB-Bacteriocins.Microorganisms · 2021Review
- The membrane topology of immunity proteins for the two-peptide bacteriocins carnobacteriocin XY, lactococcin G, and lactococcin MN shows structural diversity.MicrobiologyOpen · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The two-peptide bacteriocins produced by Gram-positive bacteria require two different peptides, present in equimolar amounts, to elicit optimal antimicrobial activity. Producer organisms are protected from their bacteriocin by a dedicated immunity protein. The immunity proteins for two-peptide bacteriocins contain putative transmembrane domains (TMDs) and might therefore be associated with the membrane. The immunity protein CbnZ for the two-peptide bacteriocin carnobacteriocin XY (CbnXY) was identified by heterologously expressing the cbnZ gene in sensitive host strains. Using protein topology prediction methods and the dual pho-lac reporter system, we mapped out the membrane topology of CbnZ, along with those of the immunity proteins LagC and LciM for the two-peptide bacteriocins lactococcin G and lactococcin MN, respectively. Our results reveal wide structural variety between these immunity proteins that can contain as little as one TMD or as many as four TMDs.
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