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Antimicrobial Agents and Chemotherapy, November 1998, p. 3044-3046, Vol. 42, No. 11
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Quinolone Resistance Mutations in the GrlB Protein of Staphylococcus aureus

Mayumi Tanaka,* Yoshikuni Onodera, Yoko Uchida, and Kenichi Sato

New Product Research Laboratories I, Daiichi Pharmaceutical Co. Ltd., Edogawa-ku, Tokyo 134-8630, Japan

Received 9 June 1998/Returned for modification 4 August 1998/Accepted 1 September 1998

Two altered GrlB proteins (one with an Asp-432right-arrowAsn alteration and one with an Asn-470right-arrowAsp alteration) of Staphylococcus aureus were purified as fusion proteins to maltose-binding protein. The 50% inhibitory concentrations of levofloxacin were 14 and 3.4 µg/ml against topoisomerase IV containing GrlB proteins with alterations at positions 432 and 470, respectively. These results suggest that the alteration of Asp to Asn at position 432 may be responsible for quinolone resistance.

* Corresponding author. Mailing address: New Product Research Laboratories I, Daiichi Pharmaceutical Co. Ltd., 16-13 Kitakasai 1-Chome, Edogawa-ku, Tokyo 134-8630, Japan. Phone: 81-3-3680-0151, ext. 5810. Fax: 81-3-5696-8344. E-mail: tanakpmj{at}daiichipharm.co.jp.

Antimicrobial Agents and Chemotherapy, November 1998, p. 3044-3046, Vol. 42, No. 11
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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