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Antimicrobial Agents and Chemotherapy, December 2009, p. 5275-5278, Vol. 53, No. 12
0066-4804/09/$08.00+0     doi:10.1128/AAC.01032-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mutations in Ribosomal Protein L3 Are Associated with Oxazolidinone Resistance in Staphylococci of Clinical Origin{triangledown}

Jeffrey B. Locke, Mark Hilgers, and Karen Joy Shaw*

Trius Therapeutics, Inc., 6310 Nancy Ridge Drive, Suite 105, San Diego, California 92121

Received 22 July 2009/ Returned for modification 20 September 2009/ Accepted 28 September 2009

Following recent reports of ribosomal protein L3 mutations in laboratory-derived linezolid-resistant (LZDr) Staphylococcus aureus, we investigated whether similar mutations were present in LZDr staphylococci of clinical origin. Sequence analysis of a variety of LZDr isolates revealed two L3 mutations, {Delta}Ser145 (S. aureus NRS127) and Ala157Arg (Staphylococcus epidermidis 1653059), both occurring proximal to the oxazolidinone binding site in the peptidyl transferase center. The oxazolidinone torezolid maintained a ≥8-fold potency advantage over linezolid for both strains.

* Corresponding author. Mailing address: Trius Therapeutics, Inc., 6310 Nancy Ridge Drive, Suite 105, San Diego, CA 92121. Phone: (858) 452-0370, ext. 225. Fax: (858) 452-0412. E-mail: kshaw{at}triusrx.com

{triangledown} Published ahead of print on 5 October 2009.

Antimicrobial Agents and Chemotherapy, December 2009, p. 5275-5278, Vol. 53, No. 12
0066-4804/09/$08.00+0     doi:10.1128/AAC.01032-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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