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Antimicrobial Agents and Chemotherapy, February 2006, p. 445-452, Vol. 50, No. 2
0066-4804/06/$08.00+0     doi:10.1128/AAC.50.2.445-452.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Mutations Conferring Aminoglycoside and Spectinomycin Resistance in Borrelia burgdorferi

Daniel Criswell,1 Virginia L. Tobiason,1 J. Stephen Lodmell,1,2 and D. Scott Samuels1,2*

Division of Biological Sciences,1 Biomolecular Structure and Dynamics Program, The University of Montana, Missoula, Montana 598122

Received 31 August 2005/ Returned for modification 27 September 2005/ Accepted 16 November 2005

We have isolated and characterized in vitro mutants of the Lyme disease agent Borrelia burgdorferi that are resistant to spectinomycin, kanamycin, gentamicin, or streptomycin, antibiotics that target the small subunit of the ribosome. 16S rRNA mutations A1185G and C1186U, homologous to Escherichia coli nucleotides A1191 and C1192, conferred >2,200-fold and 1,300-fold resistance to spectinomycin, respectively. A 16S rRNA A1402G mutation, homologous to E. coli A1408, conferred >90-fold resistance to kanamycin and >240-fold resistance to gentamicin. Two mutations were identified in the gene for ribosomal protein S12, at a site homologous to E. coli residue Lys-87, in mutants selected in streptomycin. Substitutions at codon 88, K88R and K88E, conferred 7-fold resistance and 10-fold resistance, respectively, to streptomycin on B. burgdorferi. The 16S rRNA A1185G and C1186U mutations, associated with spectinomycin resistance, appeared in a population of B. burgdorferi parental strain B31 at a high frequency of 6 x 10–6. These spectinomycin-resistant mutants successfully competed with the wild-type strain during 100 generations of coculture in vitro. The aminoglycoside-resistant mutants appeared at a frequency of 3 x 10–9 to 1 x10–7 in a population and were unable to compete with wild-type strain B31 after 100 generations. This is the first description of mutations in the B. burgdorferi ribosome that confer resistance to antibiotics. These results have implications for the evolution of antibiotic resistance, because the 16S rRNA mutations conferring spectinomycin resistance have no significant fitness cost in vitro, and for the development of new selectable markers.

* Corresponding author. Mailing address: Division of Biological Sciences, The University of Montana, 32 Campus Dr., Missoula, MT 59812-4824. Phone: (406) 243-6145. Fax: (406) 243-4184. E-mail: scott.samuels{at}umontana.edu.

Antimicrobial Agents and Chemotherapy, February 2006, p. 445-452, Vol. 50, No. 2
0066-4804/06/$08.00+0     doi:10.1128/AAC.50.2.445-452.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sarkar, A., Tilly, K., Stewart, P., Bestor, A., Battisti, J. M., Rosa, P. A. (2009). Borrelia burgdorferi Resistance to a Major Skin Antimicrobial Peptide Is Independent of Outer Surface Lipoprotein Content. Antimicrob. Agents Chemother. 53: 4490-4494 [Abstract] [Full Text]  
  • Kehrenberg, C., Schwarz, S. (2007). Mutations in 16S rRNA and Ribosomal Protein S5 Associated with High-Level Spectinomycin Resistance in Pasteurella multocida. Antimicrob. Agents Chemother. 51: 2244-2246 [Abstract] [Full Text]  


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