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J Antimicrob Chemother. 2004 Jan;53(1):102-4. Epub 2003 Dec 4.

The isoleucyl-tRNA synthetase mutation V588F conferring mupirocin resistance in glycopeptide-intermediate Staphylococcus aureus is not associated with a significant fitness burden.

Author information

1
Antimicrobial Research Centre and Division of Microbiology, School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.

Abstract

OBJECTIVES AND METHODS:

Failure to eradicate nasal carriage of a glycopeptide-intermediate Staphylococcus aureus (strain GISA-2) with mupirocin was recently attributed to a mutation that confers low-level mupirocin resistance. To identify this mutation the ileS genes of GISA-2 and its mupirocin-susceptible progenitor GISA-1 were sequenced. For comparison, the ileS genes of 10 laboratory-derived mupirocin-resistant mutants of the GISA strain Mu50 were also examined. The fitness of GISA-2 and mupirocin-susceptible GISA-1, as well as Mu50 and its mupirocin-resistant derivatives, were compared by evaluation of growth rates and performance in mixed-culture competition assays.

RESULTS:

The point mutation V588F in the isoleucyl-tRNA synthetase was identified from the ileS sequences of GISA-2 and mupirocin-resistant mutants of Mu50. The V588F mutation was not associated with a significant fitness burden.

CONCLUSIONS:

The low fitness cost of the V588F substitution in isoleucyl-tRNA synthetase is consistent with the frequent appearance and maintenance of this mutation in mupirocin-resistant clinical isolates, including GISA-2.

PMID:
14657089
DOI:
10.1093/jac/dkh020
[Indexed for MEDLINE]

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