lacticin 481
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2017 ◽  
Vol 139 ◽  
pp. 138-142 ◽  
Author(s):  
Tomás García-Cayuela ◽  
Teresa Requena ◽  
M. Carmen Martínez-Cuesta ◽  
Carmen Peláez

2016 ◽  
Vol 63 ◽  
pp. 18-28 ◽  
Author(s):  
Susana C. Ribeiro ◽  
Paula M. O'Connor ◽  
R. Paul Ross ◽  
Catherine Stanton ◽  
Célia C.G. Silva

2016 ◽  
Vol 138 (20) ◽  
pp. 6436-6444 ◽  
Author(s):  
Christopher J. Thibodeaux ◽  
Joshua Wagoner ◽  
Yi Yu ◽  
Wilfred A. van der Donk
Keyword(s):  

2012 ◽  
Vol 7 (11) ◽  
pp. 1791-1795 ◽  
Author(s):  
Patrick J. Knerr ◽  
Trent J. Oman ◽  
Chantal V. Garcia De Gonzalo ◽  
Tania J. Lupoli ◽  
Suzanne Walker ◽  
...  

2009 ◽  
Vol 92 (10) ◽  
pp. 4805-4811 ◽  
Author(s):  
D. Bravo ◽  
E. Rodríguez ◽  
M. Medina

2009 ◽  
Vol 75 (13) ◽  
pp. 4427-4434 ◽  
Author(s):  
T. Böttiger ◽  
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 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.


2009 ◽  
Vol 4 (5) ◽  
pp. 379-385 ◽  
Author(s):  
Young Ok You ◽  
Matthew R. Levengood ◽  
L. A. Furgerson Ihnken ◽  
Aaron K. Knowlton ◽  
Wilfred A. van der Donk

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