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Microbiology and Molecular Biology Reviews, December 2000, p. 672-693, Vol. 64, No. 4
1092-2172/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Molecular Properties of Bacterial Multidrug Transporters

Monique Putman, Hendrik W. van Veen, and Wil N. Konings^*

Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, NL-9751 NN Haren, The Netherlands

One of the mechanisms that bacteria utilize to evade the toxic effects of antibiotics is the active extrusion of structurally unrelated drugs from the cell. Both intrinsic and acquired multidrug transporters play an important role in antibiotic resistance of several pathogens, including Neisseria gonorrhoeae, Mycobacterium tuberculosis, Staphylococcus aureus, Streptococcus pneumoniae, Pseudomonas aeruginosa, and Vibrio cholerae. Detailed knowledge of the molecular basis of drug recognition and transport by multidrug transport systems is required for the development of new antibiotics that are not extruded or of inhibitors which block the multidrug transporter and allow traditional antibiotics to be effective. This review gives an extensive overview of the currently known multidrug transporters in bacteria. Based on energetics and structural characteristics, the bacterial multidrug transporters can be classified into five distinct families. Functional reconstitution in liposomes of purified multidrug transport proteins from four families revealed that these proteins are capable of mediating the export of structurally unrelated drugs independent of accessory proteins or cytoplasmic components. On the basis of (i) mutations that affect the activity or the substrate specificity of multidrug transporters and (ii) the three-dimensional structure of the drug-binding domain of the regulatory protein BmrR, the substrate-binding site for cationic drugs is predicted to consist of a hydrophobic pocket with a buried negatively charged residue that interacts electrostatically with the positively charged substrate. The aromatic and hydrophobic amino acid residues which form the drug-binding pocket impose restrictions on the shape and size of the substrates. Kinetic analysis of drug transport by multidrug transporters provided evidence that these proteins may contain multiple substrate-binding sites.

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^* Corresponding author. Mailing address: Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, NL-9751 NN Haren, The Netherlands. Phone: 31 50 3632150. Fax: 31 50 3632154.

Present address: Department of Pharmacology, University of Cambridge, Cambridge CB2 1QJ, United Kingdom.

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Microbiology and Molecular Biology Reviews, December 2000, p. 672-693, Vol. 64, No. 4
1092-2172/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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