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Antimicrobial Agents and Chemotherapy, November 2002, p. 3339-3342, Vol. 46, No. 11
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.11.3339-3342.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Interaction of Avilamycin with Ribosomes and Resistance Caused by Mutations in 23S rRNA

Christine B. Kofoed{dagger} and Birte Vester*

Institute of Molecular Biology, University of Copenhagen, DK-1307 Copenhagen K, Denmark

Received 13 May 2002/ Returned for modification 24 June 2002/ Accepted 26 July 2002

The antibiotic growth promoter avilamycin inhibits protein synthesis by binding to bacterial ribosomes. Here the binding site is further characterized on Escherichia coli ribosomes. The drug interacts with domain V of 23S rRNA, giving a chemical footprint at nucleotides A2482 and A2534. Selection of avilamycin-resistant Halobacterium halobium cells revealed mutations in helix 89 of 23S rRNA. Furthermore, mutations in helices 89 and 91, which have previously been shown to confer resistance to evernimicin, give cross-resistance to avilamycin. These data place the binding site of avilamycin on 23S rRNA close to the elbow of A-site tRNA. It is inferred that avilamycin interacts with the ribosomes at the ribosomal A-site interfering with initiation factor IF2 and tRNA binding in a manner similar to evernimicin.

* Corresponding author. Present address: Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark. Phone: 45 6550 2377. Fax: 45 6593 2467. E-mail: b.vester{at}bmb.sdu.dk.

{dagger} Present address: Department of Clinical Biochemistry, Glostrup Hospital, DK-2600 Glostrup, Denmark.

Antimicrobial Agents and Chemotherapy, November 2002, p. 3339-3342, Vol. 46, No. 11
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.11.3339-3342.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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