ArticleApplied and environmental microbiology2015
Solution structure of acidocin B, a circular bacteriocin produced by Lactobacillus acidophilus M46.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- A Novel Bacteriocin from Insectivorous Bat (Hipposideros speoris) Intestine Mimicking Mammalian FAM216B: Probiotic, Antioxidant, and Antimicrobial Properties of Enterococcus hirae BNT6.Probiotics and antimicrobial proteins · 2026Article
- Current status and potential of bacteriocin-producing lactic acid bacteria applied in the food industry.Current research in food science · 2025Review
- Characterization of a novel circular bacteriocin fromHeliyon · 2024Article
- Engineering circular bacteriocins: structural and functional effects of α-helix exchanges and disulfide introductions in circularin A.Frontiers in microbiology · 2024Article
- Perspectives in Searching Antimicrobial Peptides (AMPs) Produced by the Microbiota.Microbial ecology · 2023Review
- 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
- Leader- and Terminal Residue Requirements for Circularin A Biosynthesis Probed by Systematic Mutational Analyses.ACS synthetic biology · 2023Article
- Transient comparison of techniques to counter multi-drug resistant bacteria: prime modules in curation of bacterial infections.Frontiers in antibiotics · 2023Review
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Transporter Protein-Guided Genome Mining for Head-to-Tail Cyclized Bacteriocins.Molecules (Basel, Switzerland) · 2021Article
- Crystal structure and site-directed mutagenesis of circular bacteriocin plantacyclin B21AG reveals cationic and aromatic residues important for antimicrobial activity.Scientific reports · 2020Article
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- Bioinformatic prospecting and phylogenetic analysis reveals 94 undescribed circular bacteriocins and key motifs.BMC microbiology · 2020Article
- The role of disulfide bonds in a Solanum tuberosum saposin-like protein investigated using molecular dynamics.PloS one · 2020Article
- Singularities of Pyogenic Streptococcal Biofilms - From Formation to Health Implication.Frontiers in microbiology · 2020Review
- Bioinspired Designs, Molecular Premise and Tools for Evaluating the Ecological Importance of Antimicrobial Peptides.Pharmaceuticals (Basel, Switzerland) · 2018Review
- Metabolomics of Early Stage Plant Cell-Microbe Interaction Using Stable Isotope Labeling.Frontiers in plant science · 2018Article
- Circular and Leaderless Bacteriocins: Biosynthesis, Mode of Action, Applications, and Prospects.Frontiers in microbiology · 2018Review
- Plantaricyclin A, a Novel Circular Bacteriocin Produced by Lactobacillus plantarum NI326: Purification, Characterization, and Heterologous Production.Applied and environmental microbiology · 2018Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acidocin B, a bacteriocin produced by Lactobacillus acidophilus M46, was originally reported to be a linear peptide composed of 59 amino acid residues. However, its high sequence similarity to gassericin A, a circular bacteriocin from Lactobacillus gasseri LA39, suggested that acidocin B might be circular as well. Acidocin B was purified from culture supernatant by a series of hydrophobic interaction chromatographic steps. Its circular nature was ascertained by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry and tandem mass spectrometry (MS/MS) sequencing. The peptide sequence was found to consist of 58 amino acids with a molecular mass of 5,621.5 Da. The sequence of the acidocin B biosynthetic gene cluster was also determined and showed high nucleotide sequence similarity to that of gassericin A. The nuclear magnetic resonance (NMR) solution structure of acidocin B in sodium dodecyl sulfate micelles was elucidated, revealing that it is composed of four α-helices of similar length that are folded to form a compact, globular bundle with a central pore. This is a three-dimensional structure for a member of subgroup II circular bacteriocins, which are classified based on their isoelectric points of ∼7 or lower. Comparison of acidocin B with carnocyclin A, a subgroup I circular bacteriocin with four α-helices and a pI of 10, revealed differences in the overall folding. The observed variations could be attributed to inherent diversity in their physical properties, which also required the use of different solvent systems for three-dimensional structural elucidation.
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