期刊
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
卷 75, 期 13, 页码 4427-4434出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.00262-09
关键词
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资金
- German Research Foundation [Sa 292/91-1, 9-4]
- Medical Faculty of Bonn
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 Ca2+ 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 Ca2+ ions on the antimicrobial activity known for mersacidin also applies to plantaricin C and lacticin 3147. Ca2+ 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 Ca2+ independent.
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