Mode of action of lipid II-targeting lantibiotics
Date
2005
Authors
Bauer R.
Dicks L.M.T.
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
The antimicrobial action of bacteriocins from Gram-positive bacteria is based on interaction with the cytoplasmic membrane of sensitive bacteria. Models based on studies with artificial membrane systems propose that nisin forms wedge-like poration complexes in the membrane by electrostatic interaction between the positively charged C terminus of the peptide and anionic membrane phospholipids. Nisin can also permeabilise membranes via a targeted mechanism by using lipid II, the bactoprenol-bound precursor of the bacterial cell wall, as a docking molecule. Another consequence of binding with lipid II is the inhibition of peptidoglycan biosynthesis. Mersacidine and actagardine also form a complex with lipid II, but binding only blocks the incorporation of lipid II into peptidoglycan, resulting in slow cell lysis rather than pore formation. Both peptides share a conserved sequence motif with plantaricin C and pediocin PD-1, which is most probably involved in the binding of these bacteriocins to lipid II. Although pediocin PD-1 and plantaricin C may inhibit peptidoglycan biosynthesis, pore formation is rather due to electrostatic interaction between the positively charged unbridged N-terminus and anionic phospholipids in the cytoplasmic membrane of sensitive cells. In the light of increased antibiotic resistance, this review focuses on the mode of action of lantibiotics that involve lipid II, possible candidates for the development of new-generation novel antibiotic drugs. © 2005 Elsevier B.V. All rights reserved.
Description
Keywords
actagardin, anion, antibiotic agent, antiinfective agent, bacteriocin, epidermin, epilancin, lanthiopeptin, lantibiotic, lipid, mersacidine, nisin, nitrogen, pediocin, peptide, peptidoglycan, phospholipid, plantaricin, subtilin, unclassified drug, vancomycin, antibacterial activity, biosynthesis, cell membrane, channel gating, cytolysis, drug binding, drug resistance, energy, Gram positive bacterium, ligand binding, membrane permeability, molecule, nonhuman, permeability, review, Anti-Bacterial Agents, Bacteriocins, Cell Wall, Lactobacillus, Membranes, Artificial, Nisin, Peptidoglycan, Protein Binding, Bacteria (microorganisms), Posibacteria
Citation
International Journal of Food Microbiology
101
02-Jan
101
02-Jan