Influence of Ca2+ Ions on the Activity of Lantibiotics Containing a Mersacidin-Like Lipid II Binding Motif

被引:24
作者
Boettiger, T. [1 ]
Schneider, T. [1 ]
Martinez, B. [2 ]
Sahl, H. -G. [1 ]
Wiedemann, I. [1 ]
机构
[1] Univ Bonn, Inst Med Microbiol Immunol & Parasitol, Pharmaceut Microbiol Sect, D-53115 Bonn, Germany
[2] IPLA CSIC, Villaviciosa 33300, Asturias, Spain
关键词
CELL-WALL BIOSYNTHESIS; PEPTIDOGLYCAN BIOSYNTHESIS; ANTIMICROBIAL ACTIVITY; ANTIBIOTIC DAPTOMYCIN; INVITRO ACTIVITY; PLANTARICIN-C; NUKACIN ISK-1; NISIN; MODE; LACTICIN-481;
D O I
10.1128/AEM.00262-09
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
引用
收藏
页码:4427 / 4434
页数:8
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