Alternative Bactericidal Mechanism of Action for Lantibiotic Peptides That Target Lipid II

Lantibiotics are polycyclic peptides containing unusual amino acids, which have binding specificity for bacterial cells, targeting the bacterial cell wall component lipid II to form pores and thereby lyse the cells. Yet several members of these lipid II-targeted lantibiotics are too short to be able...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2006-09, Vol.313 (5793), p.1636-1637
Main Authors: Hasper, Hester E, Kramer, Naomi E, Smith, James L, Hillman, J.D, Zachariah, Cherian, Kuipers, Oscar P, Kruijff, Ben de, Breukink, Eefjan
Format: Article
Language:English
Subjects:
Anti-Bacterial Agents - metabolism
Anti-Bacterial Agents - pharmacology
Antibacterial agents
Antibiotics
Antibiotics. Antiinfectious agents. Antiparasitic agents
Bacillus - drug effects
Bacillus - metabolism
Bacillus - ultrastructure
Bacillus megaterium - drug effects
Bacillus megaterium - metabolism
Bacillus megaterium - ultrastructure
Bacillus subtilis - drug effects
Bacillus subtilis - metabolism
Bacillus subtilis - ultrastructure
Bacteria
Bacteriocins
Bacteriocins - chemistry
Bacteriocins - metabolism
Bacteriocins - pharmacology
Biological and medical sciences
Cell division
Cell Division - drug effects
Cell Wall - metabolism
Cell wall components
Cell walls
Diphosphates
Fluorescence
Lipid Bilayers - metabolism
Lipids
Medical sciences
Membranes, Artificial
Molecules
Nisin - chemistry
Nisin - metabolism
Nisin - pharmacology
Peptides
Peptides - chemistry
Peptides - metabolism
Peptides - pharmacology
Peptidoglycan - biosynthesis
Pharmacology. Drug treatments
Septum
Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives
Uridine Diphosphate N-Acetylmuramic Acid - metabolism
Vancomycin - metabolism
Vancomycin - pharmacology
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Description
Summary:Lantibiotics are polycyclic peptides containing unusual amino acids, which have binding specificity for bacterial cells, targeting the bacterial cell wall component lipid II to form pores and thereby lyse the cells. Yet several members of these lipid II-targeted lantibiotics are too short to be able to span the lipid bilayer and cannot form pores, but somehow they maintain their antibacterial efficacy. We describe an alternative mechanism by which members of the lantibiotic family kill Gram-positive bacteria by removing lipid II from the cell division site (or septum) and thus block cell wall synthesis.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1129818