2006
DOI: 10.1128/aem.72.4.2809-2814.2006
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Lipid II-Based Antimicrobial Activity of the Lantibiotic Plantaricin C

Abstract: We analyzed the mode of action of the lantibiotic plantaricin C (PlnC), produced by Lactobacillus plantarum LL441. Compared to the well-characterized type A lantibiotic nisin and type B lantibiotic mersacidin, which are both able to interact with the cell wall precursor lipid II, PlnC displays structural features of both prototypes. In this regard, we found that lipid II plays a key role in the antimicrobial activity of PlnC besides that of pore formation. The pore forming activity of PlnC in whole cells was p… Show more

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Cited by 75 publications
(59 citation statements)
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“…The resulting lantibiotic-lipid II complex inhibits peptidoglycan synthesis. Nisin binds the pyrophosphate linker of lipid II (16), as does plantaricin C and lacticin 3147 (Ltn␣) (13,14). Mersacidin and members of the mersacidin group of lantibiotics target the N-acetylglucosamine (GlcNAc) moiety and most probably the sugar and phosphate residues of lipid II (17).…”
Section: Mode Of Actionmentioning
confidence: 99%
See 1 more Smart Citation
“…The resulting lantibiotic-lipid II complex inhibits peptidoglycan synthesis. Nisin binds the pyrophosphate linker of lipid II (16), as does plantaricin C and lacticin 3147 (Ltn␣) (13,14). Mersacidin and members of the mersacidin group of lantibiotics target the N-acetylglucosamine (GlcNAc) moiety and most probably the sugar and phosphate residues of lipid II (17).…”
Section: Mode Of Actionmentioning
confidence: 99%
“…Once at the membrane, lantibiotics, such as nisin, mersacidin, epidermin, plantaricin C, and lacticin 3147 (Ltn␣; one of two components of a dual-peptide bacteriocin), bind to and form a complex with a docking molecule, lipid II (11)(12)(13)(14)(15). Lipid II is a precursor of cell wall peptidoglycan and is found at the outer leaflet of the bacterial membrane.…”
Section: Mode Of Actionmentioning
confidence: 99%
“…Its activity is based on the permeabilization of the cytoplasmic membrane, leading to its depolarization (47,70). Other potent bacteriocins include plantaricin and pediocin, which are widely distributed among L. plantarum and pediococci, respectively (41,172). The broad activity spectrum of bacteriocins has been exploited for the inhibition of the outgrowth of spoilage microbes and pathogens (4,91).…”
Section: Classifying Interactions On the Basis Of Mutually Beneficialmentioning
confidence: 99%
“…To consider the role of lipid II as molecular target and its impact on binding intensity, 0.1 mol% lipid II was added to the matrix lipids. In accordance to other peptide/model membrane studies [27][28][29][30][31][32][33] and to avoid non-specific binding of the cationic antimicrobial peptides to the membrane surface, DOPC was initially selected as membrane lipid. As depicted in Fig 2A, [34,35], the gallidermin structure ( Fig.…”
Section: Kinetics Of Peptide Binding To Model Membranesmentioning
confidence: 99%