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JAC Advance Access published online on July 29, 2005
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dki253
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© The Author 2005. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For Permissions, please e-mail: journals.permissions@oupjournals.org
Received March 18, 2005
Revised May 24, 2005
Accepted June 23, 2005

Original article

Molecular basis of macrolide resistance in Campylobacter: role of efflux pumps and target mutations

Laurent Mamelli 1, Valérie Prouzet-Mauléon 2, Jean-Marie Pagès 1, Francis Mégraud 2, and Jean-Michel Bolla 1*

1 Université de la Méditerranée, Enveloppe Bactérienne, Perméabilité et Antibiotiques, EA2197, IFR48, Faculté de Médecine, 27 Bd Jean Moulin 13385, Marseille Cedex 05, France
2 Université Victor Segalen Bordeaux 2, Laboratoire de Bactériologie, Centre National de Référence des Campylobacters, Bordeaux, France

* To whom correspondence should be addressed.
Jean-Michel Bolla, E-mail: Jean-Michel.Bolla{at}medecine.univ-mrs.fr


  Abstract

Background: Erythromycin is the drug of choice to treat human campylobacteriosis. Campylobacter isolates exhibit two different phenotypes with regard to erythromycin resistance: high-level resistant strains (HLR) and low-level resistant strains (LLR).

Objectives: To study the mechanisms of resistance of Campylobacter to erythromycin, its 6-O-methyl derivative clarithromycin and the ketolide telithromycin.

Results: We observed a cross-resistance against these three molecules but in contrast, no cross-resistance to quinolones. Analyses of LLR showed no mutation on the 23S rDNA and the presence of a drug transport system, which can be inhibited by phenylalanine arginine {beta}-naphthylamide (PA{beta}N), an efflux-pump inhibitor. In contrast, no PA{beta}N-sensitive drug transport was identified in HLR but we found mutations in the rDNA, which were responsible for decreased binding of telithromycin to purified ribosomes. We further showed that the CmeB efflux pump already described in Campylobacter is not involved in the PA{beta}N-sensitive transport of telithromycin.

Conclusions: Mutations in the ribosome confer high-level macrolide/ketolide resistance. Low-level resistance was mediated by an efflux mechanism which is sensitive to PA{beta}N. This efflux pump was selective to macrolides/ketolide and was different from the previously described Campylobacter efflux pump.

Keywords: macrolides; ketolides; efflux pumps; efflux pump inhibitors; ribosome binding.
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