Teicoplanin resistance in Staphylococcus haemolyticus is associated with mutations in histidine kinases VraS and WalK
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
PubMed
29246777
DOI
10.1016/j.diagmicrobio.2017.11.007
PII: S0732-8893(17)30362-0
Knihovny.cz E-zdroje
- Klíčová slova
- Mutation, Resistance, Staphylococcus haemolyticus, Teicoplanin, Vancomycin,
- MeSH
- antibakteriální látky farmakologie MeSH
- bakteriální léková rezistence genetika MeSH
- DNA bakterií genetika MeSH
- fenotyp MeSH
- genom bakteriální genetika MeSH
- histidinkinasa genetika MeSH
- jednonukleotidový polymorfismus genetika MeSH
- lidé MeSH
- rezistence na vankomycin genetika MeSH
- sekvence nukleotidů MeSH
- sekvenční analýza DNA MeSH
- stafylokokové infekce mikrobiologie MeSH
- Staphylococcus haemolyticus účinky léků genetika izolace a purifikace MeSH
- teikoplanin farmakologie MeSH
- vankomycin farmakologie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Geografické názvy
- Polsko MeSH
- Názvy látek
- antibakteriální látky MeSH
- DNA bakterií MeSH
- histidinkinasa MeSH
- teikoplanin MeSH
- vankomycin MeSH
We investigated the genetic basis of glycopeptide resistance in laboratory-derived strains of S. haemolyticus with emphasis on differences between vancomycin and teicoplanin. The genomes of two stable teicoplanin-resistant laboratory mutants selected on vancomycin or teicoplanin were sequenced and compared to parental S. haemolyticus strain W2/124. Only the two non-synonymous mutations, VraS Q289K and WalK V550L were identified. No other mutations or genome rearrangements were detected. Increased cell wall thickness, resistance to lysostaphin-induced lysis and adaptation of cell growth rates specifically to teicoplanin were phenotypes observed in a sequenced strain with the VraS Q289K mutation. Neither of the VraS Q289K and WalK V550L mutations was present in the genomes of 121S. haemolyticus clinical isolates. However, all but two of the teicoplanin resistant strains carried non-synonymous SNPs in vraSRTU and walKR-YycHIJ operons pointing to their importance for the glycopeptide resistance.
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