Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A

• Published in: Applied and Environmental Microbiology Vol. 64; no. 6; pp. 2269 - 2272
• Main Authors: Anderssen, E.L. (University of Oslo, Oslo, Norway.), Diep, D.B, Nes, I.F, Eijsink, V.G, Nissen-Meyer, J
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.06.1998
• Subjects: Amino Acid Sequence; ANTIBACTERIAL PROPERTIES; ANTIMICROBIAL PROPERTIES; Bacteria; BACTERIAS ACIDOLACTICAS; BACTERIE LACTIQUE; Bacteriocins - genetics; Bacteriocins - isolation & purification; Bacteriocins - pharmacology; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Drug Interactions; Food Microbiology; Fundamental and applied biological sciences. Psychology; Genes, Bacterial; LACTIC ACID BACTERIA; Lactobacillus - drug effects; Lactobacillus - genetics; Lactobacillus - metabolism; LACTOBACILLUS PLANTARUM; Microbiology; Miscellaneous; Mission oriented research; Molecular Sequence Data; Peptides; plantaricin A; plantaricin EF; plantaricin JK; PROPIEDADES ANTIMICROBIANAS; PROPRIETE ANTIMICROBIENNE; Lactic acid bacteria; Lactobacillus plantarum; Purification; Peptides; Bacteriocin; Bacteria; Lactobacillaceae; Antagonist; Strain specificity; Antibacterial agent; Biological activity
• ISSN: 0099-2240; 1098-5336
• DOI: 10.1128/aem.64.6.2269-2272.1998

Six bacteriocinlike peptides (plantaricin A [PlnA], PlnE, PlnF, PlnJ, PlnK, and PlnN) produced by Lactobacillus plantarum C11 were detected by amino acid sequencing and mass spectrometry. Since purification to homogeneity was problematic, all six peptides were obtained by solid-phase peptide synthesis and were tested for bacteriocin activity. It was found that L. plantarum C11 produces two two-peptide bacteriocins (PlnEF and PlnJK); a strain-specific antagonistic activity was detected at nanomolar concentrations when PlnE and PlnF were combined and when PlnJ and PlnK were combined. Complementary peptides were at least 10(3) times more active when they were combined than when they were present individually, and optimal activity was obtained when the complementary peptides were present in approximately equal amounts. The interaction between complementary peptides was specific, since neither PlnE nor PlnF could complement PlnJ or PlnK, and none of these peptides could complement the peptides constituting the two-peptide bacteriocin lactococcin G. Interestingly, PlnA, which acts as an extracellular signal (pheromone) that triggers bacteriocin production, also possessed a strain-specific antagonistic activity. No bacteriocin activity could be detected for PlnN