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Applied and Environmental Microbiology, July 2009, p. 4427-4434, Vol. 75, No. 13
0099-2240/09/$08.00+0 doi:10.1128/AEM.00262-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Institute of Medical Microbiology, Immunology and Parasitology-Pharmaceutical Microbiology Section, University of Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany,1 Instituto de Productos Lácteos de Asturias, IPLA-CSIC, 33300 Villaviciosa, Asturias, Spain2
Received 3 February 2009/ Accepted 1 May 2009
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.
Published ahead of print on 8 May 2009.
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