To decipher conserved features involved in production of these bacteriocins, genome mining was used to identify 11 candidates for new multipeptide bacteriocins; four were obtained synthetically and confirmed to be bioactive peptides inhibiting important pathogens including Listeria monocytogenes and enterococci.
Abstract
Garvicin KS (GarKS) is a three-peptide, leaderless, broad-spectrum bacteriocin that is active against a wide range of Gram-positive bacteria, including several foodborne pathogens and antibiotic-resistant strains. This bacteriocin is considered a candidate for application in food preservation and medical treatments; however, key knowledge about the producer strain, regulation of production, and the mechanism of action is still lacking for leaderless, multipeptide bacteriocins, including GarKS. A hybrid sequencing strategy was used to obtain a high-quality closed genome assembly of the native GarKS producer Lactococcus garvieae KS1546, which showed that the bacteriocin was encoded on a 50 kb plasmid (pKS50). Comparative analysis with updated sequence databases indicates that the producer strain should be reclassified as Lactococcus petauri. The roles of the biosynthetic genes, putatively encoding a transcriptional regulator (gakR) and immunity protein (gakI), were examined using heterologous expression. Removal of gakR resulted in a 6-fold decrease in GarKS production, and expression of gakI caused a 250-fold decrease in susceptibility to GarKS, with varying degrees of cross-immunity to other multipeptide bacteriocins. Isolation and whole-genome sequencing of spontaneous GarKS mutants in L. lactis showed that resistance levels are low, but that ythA, a PspC-domain-containing protein involved in a phage stress response pathway is involved in the GarKS susceptible phenotype. To decipher conserved features involved in production of these bacteriocins, we finally used genome mining to identify 11 candidates for new multipeptide bacteriocins; four of them were obtained synthetically and confirmed to be bioactive peptides inhibiting important pathogens including Listeria monocytogenes and enterococci.
A BLAST analysis of the assembled genome sequence indicated that vB_AbaP_IME546 is a novel bacteriophage and confirms that the IME546 phage exhibits depolymerase activity during the lysis of Ab2897.
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The putative biosynthetic pathway of the paenialvins is described and structural variations are explained, bringing useful data on Paenibacillus secondary metabolism for future antibiotic development.
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Detailed analysis of the genome and structural proteome of phage Miki is presented, including in silico predictions and modeling of receptor-binding proteins, including central and proximal fibers resembling the adsorption apparatus of Escherichia phage T5.
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Pseudoiodinine is an antimicrobial compound produced by Pseudomonas mosselii that exhibits strong inhibitory activity against bacterial and fungal pathogens of rice, highlighting its potential as a green biopesticide. However, the regulatory mechanisms underlying pseudoiodinine production remain poorly understood. In t...
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A new machine-learning framework aims to improve the success rate of computational protein design while moving away from results that reproduce sequences found in nature.