ArticleScientific reports2015
Distinct colicin M-like bacteriocin-immunity pairs in Burkholderia.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Bacterial weaponry and the ecological factors of competitive success.Essays in biochemistry · 2026Review
- The evolution of short- and long-range weapons for bacterial competition.Nature ecology & evolution · 2023Article
- Compilation of the Antimicrobial Compounds Produced byMolecules (Basel, Switzerland) · 2023Review
- Heterologous overexpression and preliminary antimicrobial activity test of salmocin M, a novel colicin M-like bacteriocin against Salmonella sp.Archives of microbiology · 2022Article
- The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021Review
- Article
- Pseudomonas bacteriocin syringacin M released upon desiccation suppresses the growth of sensitive bacteria in plant necrotic lesions.Microbial biotechnology · 2020Article
- A Colicin M-Type Bacteriocin from Pseudomonas aeruginosa Targeting the HxuC Heme Receptor Requires a Novel Immunity Partner.Applied and environmental microbiology · 2018Article
- Article
- Diversity and distribution of nuclease bacteriocins in bacterial genomes revealed using Hidden Markov Models.PLoS computational biology · 2017Article
- A Natural ChimericmBio · 2017Article
- Novel Immunity Proteins Associated with Colicin M-like Bacteriocins Exhibit Promiscuous Protection inFrontiers in microbiology · 2017Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli bacteriocin colicin M (ColM) acts via degradation of the cell wall precursor lipid II in target cells. ColM producers avoid self-inhibition by a periplasmic immunity protein anchored in the inner membrane. In this study, we identified colM-like bacteriocin genes in genomes of several β-proteobacterial strains belonging to the Burkholderia cepacia complex (Bcc) and the Burkholderia pseudomallei group. Two selected Burkholderia ambifaria proteins, designated burkhocins M1 and M2, were produced recombinantly and showed antagonistic activity against Bcc strains. In their considerably sequence-diverged catalytic domain, a conserved aspartate residue equally proved pivotal for cytotoxicity. Immunity to M-type burkhocins is conferred upon susceptible strains by heterologous expression of a cognate gene located either upstream or downstream of the toxin gene. These genes lack homology with currently known ColM immunity genes and encode inner membrane-associated proteins of two distinct types, differing in predicted transmembrane topology and moiety exposed to the periplasm. The addition of burkhocins to the bacteriocin complement of Burkholderia reveals a wider phylogenetic distribution of ColM-like bacteriotoxins, beyond the γ-proteobacterial genera Escherichia, Pectobacterium and Pseudomonas, and illuminates the diversified nature of immunity-providing proteins.
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