» Articles » PMID: 334063

Function of the Outer Membrane of Escherichia Coli As a Permeability Barrier to Beta-lactam Antibiotics

Overview
Specialty Pharmacology
Date 1977 Sep 1
PMID 334063
Citations 148
Authors
Affiliations
Soon will be listed here.
Abstract

On the basis of a simple theoretical model, the ease of penetration of beta-lactam antibiotics through the outer membrane of Escherichia coli was measured. The cell envelope was found to act as a diffusion barrier to both penicillins and cephalosporins. The validity of the model and the cooperative action of cell-bound beta-lactamase and outer membrane were further verified by comparing calculated and experimentally determined velocities of beta-lactam hydrolysis by intact cells and sonically treated cell suspensions. The results showed good correspondence at five different antibiotic concentrations. Similar conclusions could be drawn from a comparison of beta-lactam concentrations on both sides of the outer membrane, calculated from enzyme kinetic measurements and minimal inhibitory concentrations for both a beta-lactamase-producing E. coli and its enzyme-negative variant. in the case of benzylpenicillin and cephalothin, however, no correspondence was found. The joint action of several parameters determining the efficacy of penicillins and cephalosporins against beta-lactamase-producing E. coli is discussed.

Citing Articles

Carbon-TiO Hybrid Quantum Dots for Photocatalytic Inactivation of Gram-Positive and Gram-Negative Bacteria.

Dong X, Liu Y, Adcock A, Sheriff K, Liang W, Yang L Int J Mol Sci. 2024; 25(4).

PMID: 38396872 PMC: 10889188. DOI: 10.3390/ijms25042196.


Guiding the Way: Traditional Medicinal Chemistry Inspiration for Rational Gram-Negative Drug Design.

Stoorza A, Duerfeldt A J Med Chem. 2023; 67(1):65-80.

PMID: 38134355 PMC: 11342810. DOI: 10.1021/acs.jmedchem.3c01831.


Mycobacterium tuberculosis β-lactamase variant reduces sensitivity to ampicillin/avibactam in a zebrafish-Mycobacterium marinum model of tuberculosis.

van Alen I, Aguirre Garcia M, Maaskant J, Kuijl C, Bitter W, Meijer A Sci Rep. 2023; 13(1):15406.

PMID: 37717068 PMC: 10505137. DOI: 10.1038/s41598-023-42152-8.


Penicillin-Binding Protein 5/6 Acting as a Decoy Target in Pseudomonas aeruginosa Identified by Whole-Cell Receptor Binding and Quantitative Systems Pharmacology.

Lopez-Arguello S, Montaner M, Sayed A, Oliver A, Bulitta J, Moya B Antimicrob Agents Chemother. 2023; 67(6):e0160322.

PMID: 37199612 PMC: 10269149. DOI: 10.1128/aac.01603-22.


Effect of pH-Regulation on the Capture of Lipopolysaccharides from EH100 by Four-Antennary Oligoglycines in Aqueous Medium.

Gyurova A, Berberov K, Chinarev A, Nikolov L, Karashanova D, Mileva E Materials (Basel). 2021; 14(24).

PMID: 34947254 PMC: 8709477. DOI: 10.3390/ma14247659.


References
1.
Smith J, Hamilton-Miller J . Differences between pencillinases from gram-positive and gram-negative bacteria. Nature. 1963; 197:976-8. DOI: 10.1038/197976a0. View

2.
Novick R . Micro-iodometric assay for penicillinase. Biochem J. 1962; 83:236-40. PMC: 1243538. DOI: 10.1042/bj0830236. View

3.
Smith J, Hamilton-Miller J, Knox R . Bacterial resistance to penicillins and cephalosporins. J Pharm Pharmacol. 1969; 21(6):337-58. DOI: 10.1111/j.2042-7158.1969.tb08267.x. View

4.
Neu H, Chou J . Release of surface enzymes in Enterobacteriaceae by osmotic shock. J Bacteriol. 1967; 94(6):1934-45. PMC: 276925. DOI: 10.1128/jb.94.6.1934-1945.1967. View

5.
Boman H, Nordstrom K, Normark S . Penicillin resistance in Escherichia coli K12: synergism between penicillinases and a barrier in the outer part of the envelope. Ann N Y Acad Sci. 1974; 235(0):569-86. DOI: 10.1111/j.1749-6632.1974.tb43291.x. View