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- W1965884802 abstract "We have recently shown that certain polycationic agents make the outer membrane (OM) of smooth, even encapsulated enteric bacteria as permeable to hydrophobic antibiotics (e.g., novobiocin, fusidic acid, erythromycin and others) as is the OM of 'deep' lipopolysaccharide mutants. These agents include protamine and lysine polymers with 50 or more lysine residues which are growth inhibitory or bactericidal at higher concentrations as well as a polymyxin B derivative (polymyxin B nonapeptide, PMBN) and a lysine polymer with approximately 20 lysine residues (lysin%0) which have little or no antibacterial activity of their own [1-3]. Furthermore, PMBN is able to sensitize the serum-resistant bacteria to the bactericidal action of normal and hyperimmune sera [1]. The exact molecular mechanisms involved in the increase of OM permeability or sensitivity to serum are not yet known. None of the agents produce holes in theOM large enough to allow the leakage of periplasmic proteins. All these agents are known to interact with the acidic lipopolysaccharide (LPS) present on the outer surface of the OM [3,4] and to cause structural alterations on the OM [3]. Protamine and lysine20 but not PMBN release a significant portion of the LPS from the OM [3]. One possible mechanism for the increase of the permeability of the OM caused by the polycations would be an activation of the phospholipase present in the OM of gram-negative bacteria [5,6], with a resultant hydrolysis of the phospholipids in the OM. Such an activation is known to take place during outer membrane perturbations caused by EDTA [7,8], polymyxin [9,10], cationic leukocyte protein BPI [9,11 ], immune bacteriolysis [ 12,13] or multiple phage attachment [14,15]. However, Escherichia coli mutants deficient in this phospholipase are still fully sensitive to polymyxin [16,17], BPI [11] or immune bacteriolysis [13] indicating that under these conditions the role of phospholipase is secondary. On the other hand, a phospholipase-deficient mutant was resistant to the increase of the permeability of the OM caused by EDTA, indicating that phospholipase is an important mediator in the action of EDTA on the OM [7]. In this communication we show that the OM phospholipase is not essential for the bactericidal action of protamine or polylysines, or the permeability-increasing action of PMBN and lysine2o." @default.
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- W1965884802 date "1983-07-01" @default.
- W1965884802 modified "2023-09-27" @default.
- W1965884802 title "Outer membrane phospholipase is not the mediator in the bactericidal or outer membrane permeability-increasing action of polycations" @default.
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- W1965884802 doi "https://doi.org/10.1111/j.1574-6968.1983.tb00552.x" @default.
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