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Role of lipid‐bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
Results demonstrate that, in vitro and in vivo, lipid II serves as a docking molecule for nisin and epidermin, but not for Pep5 and epilancin K7, and thereby facilitates the formation of pores in the cytoplasmic membrane.
The Lantibiotic Mersacidin Inhibits Peptidoglycan Synthesis by Targeting Lipid II
- H. Brötz, G. Bierbaum, K. Leopold, P. Reynolds, H. Sahl
- Biology, MedicineAntimicrobial Agents and Chemotherapy
- 1 January 1998
The interaction of mersacidin with lipid II apparently occurs via a binding site which is not targeted by any antibiotic currently in use, and in contrast to the glycopeptide antibiotics, complex formation does not involve the C-terminald-alanyl–d-alanine moiety of the lipid intermediate.
Proteomic Approach to Understanding Antibiotic Action
- J. Bandow, H. Brötz, L. Leichert, H. Labischinski, M. Hecker
- Medicine, BiologyAntimicrobial Agents and Chemotherapy
- 1 March 2003
Proteomic technology is used to elucidate the complex cellular responses of Bacillus subtilis to antimicrobial compounds belonging to classical and emerging antibiotic classes and suggests that novel compounds with unknown mechanisms of action may be classified.
Cloning, sequencing and production of the lantibiotic mersacidin.
The comparison of the mersacidin prepeptide with those of hitherto known lantibiotics demonstrates that mers acidin is more closely related to type B lant ibiotic cinnamycin than to type A lantIBiotics.
New insights into the mechanism of action of lantibiotics--diverse biological effects by binding to the same molecular target.
Identification of novel essential Escherichia coli genes conserved among pathogenic bacteria.
- C. Freiberg, B. Wieland, F. Spaltmann, K. Ehlert, H. Brötz, H. Labischinski
- Biology, MedicineJournal of molecular microbiology and…
- 1 July 2001
The deletion of a subset of 27 open reading frames from Escherichia coli which encode previously uncharacterized, probably soluble gene products homologous to proteins from a broad spectrum of bacterial pathogens demonstrates the potential of such proteins to be used in screening of large chemical libraries for inhibitors which could be further developed to novel broad-spectrum antibiotics.
The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation.
- H. Brötz, G. Bierbaum, P. Reynolds, H. Sahl
- Biology, MedicineEuropean journal of biochemistry
- 1 May 1997
The target reaction is described and a mersacidin-induced accumulation of UDP-N-acetylmuramoyl-pentapeptide is described, indicating that inhibition of peptidoglycan synthesis occurs after the formation of cytoplasmic precursors and that no cross-resistance exists between the two antibiotics.
Mode of action of the lantibiotic mersacidin: inhibition of peptidoglycan biosynthesis via a novel mechanism?
- H. Brötz, G. Bierbaum, A. Markus, E. Molitor, H. Sahl
- Biology, MedicineAntimicrobial agents and chemotherapy
- 1 March 1995
Comparison with tunicamycin-treated cells indicated that peptidoglycan rather than teichoic acid metabolism is primarily affected, which suggests that mersacidin acts on a novel target, which opens new perspectives for the treatment of methicillin-resistant S. aureus.
The role of peptide deformylase in protein biosynthesis: A proteomic study
Dual channel imaging revealed that actinonin treatment caused the majority of newly synthesised proteins to accumulate in spots different from the ones usually observed, indicating a more acidic isoelectric point.
Bacillus subtilis Tolerance of Moderate Concentrations of Rifampin Involves the σB-Dependent General and Multiple Stress Response
It is concluded that the general stress response of B. subtilis is induced by rifampin depending on RsbP activity and that loss of SigB function causes increased sensitivity to the antibiotic.