Disruption of the Escherichia coli outer membrane permeability barrier by immobilized polymyxin B.
- 1 January 1977
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 30 (12) , 1087-1092
- https://doi.org/10.7164/antibiotics.30.1087
Abstract
One of the apparent roles of the outer membrane system in gram-negative bacteria is to function as a selective permeability barrier. A number of antibiotics active against gram-positive bacteria are relatively ineffective against gram-negative bacteria presumably because of the implied barrier function of the outer membrane. This interpretation was strengthened by studies demonstrating synergism between outer membrane perturbing agents such as EDTA or polymyxin B and specific antibiotics. In the case of polymyxin B, it is not totally clear that synergism with other antimicrobials is due to disruption of the outer membrane permeability barrier or to interactions with the inner membrane. In order to resolve this question, polymyxin B was covalently attached to agarose in order to limit interactions with the outer surface of E. coli. These studies demonstrate that immobilized polymyxin B acts synergistically with bacitracin, rifampicin or lysozyme. Synergistic effects exhibited by polymyxin B may be due to its interaction with the outer membrane system.This publication has 2 references indexed in Scilit:
- Polymyxin and Related Peptide AntibioticsAnnual Review of Biochemistry, 1977
- [13] Bacterial MembranesPublished by Elsevier ,1971