ArticleScientific reports2020
Crystal structure and site-directed mutagenesis of circular bacteriocin plantacyclin B21AG reveals cationic and aromatic residues important for antimicrobial activity.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Amino Acid Substitutions in Bacteriocin Lactolisterin BU Reveal Functional Domains Involved in Biological Activity AgainstMolecules (Basel, Switzerland) · 2025Article
- Production of Pumilarin and a Novel Circular Bacteriocin, Altitudin A, byInternational journal of molecular sciences · 2024Article
- Engineering circular bacteriocins: structural and functional effects of α-helix exchanges and disulfide introductions in circularin A.Frontiers in microbiology · 2024Article
- Using metabolomics to understand stress responses in Lactic Acid Bacteria and their applications in the food industry.Metabolomics : Official journal of the Metabolomic Society · 2023Review
- Functional production of clostridial circularin A inFrontiers in microbiology · 2022Article
- Current Knowledge of the Mode of Action and Immunity Mechanisms of LAB-Bacteriocins.Microorganisms · 2021Review
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
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Abstract
Plantacyclin B21AG is a circular bacteriocin produced by Lactiplantibacillus plantarum B21 which displays antimicrobial activity against various Gram-positive bacteria including foodborne pathogens, Listeria monocytogenes and Clostridium perfringens. It is a 58-amino acid cyclised antimicrobial peptide, with the N and C termini covalently linked together. The circular peptide backbone contributes to remarkable stability, conferring partial proteolytic resistance and structural integrity under a wide temperature and pH range. Here, we report the first crystal structure of a circular bacteriocin from a food grade Lactobacillus. The protein was crystallised using the hanging drop vapour diffusion method and the structure solved to a resolution of 1.8 Å. Sequence alignment against 18 previously characterised circular bacteriocins revealed the presence of conserved charged and aromatic residues. Alanine substitution mutagenesis validated the importance of these residues. Minimum inhibitory concentration analysis of these Ala mutants showed that Phe
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