Structure, Function and Regulation of Outer Membrane Proteins Involved in Drug Transport in Enterobactericeae: the OmpF/C – TolC Case
Open Access
- 22 March 2013
- journal article
- Published by Bentham Science Publishers Ltd. in The Open Microbiology Journal
- Vol. 7 (1), 22-33
- https://doi.org/10.2174/1874285801307010022
Abstract
Antibiotic translocation across membranes of Gram-negative bacteria is a key step for the activity on their specific intracellular targets. Resistant bacteria control their membrane permeability as a first line of defense to protect themselves against external toxic compounds such as antibiotics and biocides. On one hand, resistance to small hydrophilic antibiotics such as ß-lactams and fluoroquinolones frequently results from the « closing » of their way in: the general outer membrane porins. On the other hand, an effective way out for a wide range of antibiotics is provided by TolC-like proteins, which are outer membrane components of multidrug efflux pumps. Accordingly, altered membrane permeability, including porin modifications and/or efflux pumps’ overexpression, is always associated to multidrug resistance (MDR) in a number of clinical isolates.Several recent studies have highlighted our current understanding of porins/TolC structures and functions inEnterobacteriaceae. Here, we review the transport of antibiotics through the OmpF/C general porins and the TolC-like channels with regards to recent data on their structure, function, assembly, regulation and contribution to bacterial resistance.Because MDR strains have evolved global strategies to identify and fight our antibiotic arsenal, it is important to constantly update our global knowledge on antibiotic transport.Keywords
This publication has 135 references indexed in Scilit:
- Targeting bacterial membrane function: an underexploited mechanism for treating persistent infectionsNature Reviews Microbiology, 2010
- Bacterial charity work leads to population-wide resistanceNature, 2010
- Assembly and transport mechanism of tripartite drug efflux systemsBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2009
- The assembled structure of a complete tripartite bacterial multidrug efflux pumpProceedings of the National Academy of Sciences of the United States of America, 2009
- Outer membrane permeability and antibiotic resistanceBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2008
- Assembly and Channel Opening in a Bacterial Drug Efflux MachineMolecular Cell, 2008
- Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coliProceedings of the National Academy of Sciences of the United States of America, 2007
- A periplasmic coiled-coil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumpsProceedings of the National Academy of Sciences of the United States of America, 2007
- Deletion of TolC orthologs in Francisella tularensis identifies roles in multidrug resistance and virulenceProceedings of the National Academy of Sciences of the United States of America, 2006
- Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coliProceedings of the National Academy of Sciences of the United States of America, 2006