Applied and Environmental Microbiology · 2009 · 29 citations · 39 references
Life SciencesBiochemistryMicrobiologyLipid BiochemistryMembrane BiochemistryNatural Product BiosynthesisAntimicrobial PeptidesCalcium-binding ProteinsLactic Acid BacteriaLipid ChemistryLipid-protein InteractionsProtein-lipid InteractionsAntimicrobial Peptide ActivityBacterial Cell Wall BiosynthesisBacterial Membrane Lipid CompositionCationic Antimicrobial PeptidesCell Wall Polysaccharide BiosynthesisLipid-lipid InteractionsPeptide Structure-activity RelationshipsTransglycosylation
Mersacidin binds to lipid II and thus blocks the transglycosylation step of the cell wall biosynthesis. Binding of lipid II involves a special motif, the so-called mersacidin-lipid II binding motif, which is conserved in a major subgroup of lantibiotics. We analyzed the role of Ca(2+) ions in the mode of action of mersacidin and some related peptides containing a mersacidin-like lipid II binding motif. We found that the stimulating effect of Ca(2+) ions on the antimicrobial activity known for mersacidin also applies to plantaricin C and lacticin 3147. Ca(2+) ions appear to facilitate the interaction of the lantibiotics with the bacterial membrane and with lipid II rather than being an essential part of a peptide-lipid II complex. In the case of lacticin 481, both the interaction with lipid II and the antimicrobial activity were Ca(2+) independent.
39
Imke Wiedemann, Eefjan Breukink, Cindy van Kraaij et al. · Journal of Biological Chemistry · 2001 · 775 citations · Full text