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Antimicrobial Agents and Chemotherapy, August 2008, p. 2909-2914, Vol. 52, No. 8
0066-4804/08/$08.00+0     doi:10.1128/AAC.01380-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Mutagenesis in the 34 GyrA Helix and in the Toprim Domain of GyrB Refines the Contribution of Mycobacterium tuberculosis DNA Gyrase to Intrinsic Resistance to Quinolones ^,

Université Pierre et Marie Curie-Paris 6, EA1541, Paris F-75013, France,¹ AP-HP, Groupe Hospitalier Pitié-Salpêtrière, Service Bactériologie, Paris F-75013, France,² Centre National de Référence des Mycobactéries et de la Résistance des Mycobactéries aux Antituberculeux, Paris F-75013, France,³ INSERM, U872, Paris F-75006, France,⁴ AP-HP, Groupe Hospitalier Albert Chenevier-Henri Mondor, Service Bactériologie, Créteil, France,⁵ Université Paris 12, IFR10, Créteil, France⁶

Received 25 October 2007/ Returned for modification 19 December 2007/ Accepted 11 April 2008

The replacement of M74 in GyrA, A83 in GyrA, and R447 in GyrB of Mycobacterium tuberculosis gyrase by their Escherichia coli homologs resulted in active enzymes as quinolone susceptible as the E. coli gyrase. This demonstrates that the primary structure of gyrase determines intrinsic quinolone resistance and was supported by a three-dimensional model of N-terminal GyrA.

Published ahead of print on 21 April 2008.

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