Gassericin A, produced by Lactobacillus gasseri LA39, is a hydrophobic circular bacteriocin. The DNA region surrounding the gassericin A structural gene, gaaA, was sequenced, and seven open reading frames (ORFs) of 3.5 kbp (gaaBCADITE) were found with possible functions in gassericin A production, secretion, and immunity. The deduced products of the five consecutive ORFs gaaADITE have homology to those of genes involved in butyrivibriocin AR10 production, although the genetic arrangements are different in the two circular bacteriocin genes. GaaI is a small, positively charged hydrophobic peptide of 53 amino acids containing a putative transmembrane segment. Heterologous expression and homologous expression of GaaI in Lactococcus lactis subsp. cremoris MG1363 and L. gasseri JCM1131(T), respectively, were studied. GaaI-expressing strains exhibited at least sevenfold-higher resistance to gassericin A than corresponding control strains, indicating that gaaI encodes an immunity peptide for gassericin A. Comparison of GaaI to peptides with similar characteristics found in the circular bacteriocin gene loci is discussed.
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http://dx.doi.org/10.1128/AEM.02485-08 | DOI Listing |
Microbiol Res
January 2025
International Centre for Advanced Mediterranean Agronomic Studies (CIHEAM of Bari), Via Ceglie 9, Valenzano, Bari 70010, Italy; National Research Council of Italy (CNR), Institute for Sustainable Plant Protection (IPSP), Piazzale Enrico Fermi, 1, Portici, Naples 80055, Italy. Electronic address:
Xylella fastidiosa subsp. pauca (Xfp) currently presents a serious threat to agriculture in Europe and in the Mediterranean, following its discovery in several countries. Addressing this bacterial plant disease with traditional agricultural practices and management strategies has proven inadequate, highlighting the urgent need for effective and environmentally safe antibacterial solutions.
View Article and Find Full Text PDFFront Fungal Biol
December 2024
Department of Biological Sciences, University of Notre Dame, Notre Dame, IN, United States.
The antimicrobial peptide (AMP) circularized bacteriocin enterocin AS-48 produced by sp. exhibits broad-spectrum antibacterial activity via dimer insertion into the plasma membrane to form membrane pore structures, compromising membrane integrity and leading to bactericidal activity. A specific alpha-helical region of enterocin AS-48 has been shown to be responsible for the membrane-penetrating activity of the peptide.
View Article and Find Full Text PDFAppl Environ Microbiol
December 2024
School of Microbiology, University College Cork, Cork, County Cork, Ireland.
Unlabelled: APC 4099, isolated from bees' gut, has been identified as a promising candidate for food biopreservation. Antimicrobial activity screening revealed a broad-spectrum inhibition potential, ranging from gram-positive pathogenic bacteria to fungi responsible for food spoilage. Genomic analysis identified biosynthetic gene clusters coding for several antimicrobial peptides and secondary metabolites.
View Article and Find Full Text PDFJ Biosci Bioeng
February 2025
Bioscience Research Laboratory, Sumitomo Chemical Co., Ltd., 1-98 Kasugadenaka 3-chome, Konohana-ku, Osaka 554-8558, Japan.
We have identified and characterized a circular bacteriocin, termed garvicin SC (GarSC), produced by Lactococcus garvieae ABG0038 isolated from pine cones. Genome analysis of L. garvieae ABG0038 revealed that GarSC was a variant of the circular bacteriocin, garvicin ML (GarML), caused by an amino acid substitution, and predicted that GarSC was produced through a biosynthetic mechanism very similar to that of GarML.
View Article and Find Full Text PDFAntibiotics (Basel)
August 2024
Department of Biomedical Sciences and Biomedical Engineering, Faculty of Medicine, Prince of Songkla University, Hat Yai, Songkhla 90110, Thailand.
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