scholarly journals Desferrioxamine:gallium-pluronic micelles increase outer membrane permeability and potentiate antibiotic activity againstPseudomonas aeruginosa

2018 ◽  
Vol 54 (99) ◽  
pp. 13929-13932 ◽  
Author(s):  
Max Purro ◽  
Jing Qiao ◽  
Zhi Liu ◽  
Morgan Ashcraft ◽  
May P. Xiong
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antibiotic Resistance ◽  
Membrane Permeability ◽  
Outer Membrane ◽  
Broad Spectrum ◽  
Antibiotic Activity ◽  
Permeability Barrier ◽  
Outer Membrane Permeability

The outer membrane ofPseudomonas aeruginosafunctions primarily as a permeability barrier and imparts a broad spectrum of intrinsic antibiotic resistance.

scholarly journals Antibiotic adjuvants to rescue Pseudomonas aeruginosa from tetracycline antibiotics resistance

2020 ◽  
Vol 18 ◽  
Author(s):  
Azza Troudi ◽  
Hana Douafer ◽  
Jean-Michel Bolla ◽  
Naouel Klibi ◽  
Jean Michel Brunel
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antibiotic Resistance ◽  
Membrane Permeability ◽  
Mechanism Of Action ◽  
Antibiotic Activity ◽  
Antibiotics Resistance ◽  
Bacterial Strains ◽  
Tetracycline Antibiotics ◽  
Design And Synthesis ◽  
Outer Membrane Permeability

Introduction: An attractive antibiotic-adjuvant strategy consisting in the design and synthesis of polyaminoisoprenyl molecules able to restore antibiotic activity of tetracycline antibiotics against resistant Pseudomonas aeruginosa bacterial strains has been developed. Methods: These chemo-sensitizers are readily prepared from geraniol and farnesol in an efficient two steps synthesis with good to moderate yields varying from 38 to 64% and leading to a significant decrease of antibiotic resistance. Results: Thus, the influence of the nature of the tetracycline antibiotic used as well as the structure of the polyaminoisoprenyl derivatives involved on the outcome of the antibiotic-adjuvant combination against P. aeruginosa resistance to tetracyclines were investigated. Conclusion: Additionally, our data suggested that their mechanism of action is closely associated with the increase of the outer-membrane permeability.

scholarly journals Reevaluation, using intact cells, of the exclusion limit and role of porin OprF in Pseudomonas aeruginosa outer membrane permeability.

1992 ◽  
Vol 174 (16) ◽  
pp. 5196-5203 ◽  
Author(s):  
F Bellido ◽  
N L Martin ◽  
R J Siehnel ◽  
R E Hancock
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Membrane Permeability ◽  
Outer Membrane ◽  
Exclusion Limit ◽  
Intact Cells ◽  
Outer Membrane Permeability

Outer Membrane Permeability of Pseudomonas aeruginosa

1986 ◽  
pp. 145-193 ◽  
Author(s):  
HIROSHI NIKAIDO ◽  
R.E.W. HANCOCK
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Membrane Permeability ◽  
Outer Membrane ◽  
Outer Membrane Permeability

scholarly journals Understanding antibiotic resistance via outer membrane permeability

2018 ◽  
Vol Volume 11 ◽  
pp. 523-530 ◽  
Author(s):  
Ishan Ghai ◽  
Shashank Ghai
Keyword(s):  
Antibiotic Resistance ◽  
Membrane Permeability ◽  
Outer Membrane ◽  
Outer Membrane Permeability

scholarly journals Outer Membrane Permeability Barrier in Escherichia coli Mutants That Are Defective in the Late Acyltransferases of Lipid A Biosynthesis

1999 ◽  
Vol 43 (6) ◽  
pp. 1459-1462 ◽  
Author(s):  
Martti Vaara ◽  
Marjatta Nurminen
Keyword(s):  
Escherichia Coli ◽  
Membrane Permeability ◽  
Outer Membrane ◽  
Lipid A ◽  
Enteric Bacteria ◽  
Normal Function ◽  
Permeability Barrier ◽  
Core Oligosaccharide ◽  
Hydrophobic Solutes ◽  
Outer Membrane Permeability

ABSTRACT The tight packing of six fatty acids in the lipid A constituent of lipopolysaccharide (LPS) has been proposed to contribute to the unusually low permeability of the outer membrane of gram-negative enteric bacteria to hydrophobic antibiotics. Here it is shown that theEscherichia coli msbB mutant, which elaborates defective, penta-acylated lipid A, is practically as resistant to a representative set of hydrophobic solutes (rifampin, fusidic acid, erythromycin, clindamycin, and azithromycin) as the parent-type control strain. The susceptibility index, i.e., the approximate ratio between the MIC for the msbB mutant and that for the parent-type control, was maximally 2.7-fold. In comparison, the rfa mutant defective in the deep core oligosaccharide part of LPS displayed indices ranging from 20 to 64. The lpxA and lpxD lipid A mutants had indices higher than 512. Furthermore, the msbBmutant was resistant to glycopeptides (vancomycin, teicoplanin), whereas the rfa, lpxA, and lpxDmutants were susceptible. The msbB htrB double mutant, which elaborates even-more-defective, partially tetra-acylated lipid A, was still less susceptible than the rfa mutant. These findings indicate that hexa-acylated lipid A is not a prerequisite for the normal function of the outer membrane permeability barrier.

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