| Literature DB >> 19429551 |
T Böttiger1, T Schneider, B Martínez, H-G Sahl, I Wiedemann.
Abstract
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.Entities:
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Year: 2009 PMID: 19429551 PMCID: PMC2704811 DOI: 10.1128/AEM.00262-09
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792