Increase in IS256 transposition in invasive vancomycin heteroresistant Staphylococcus aureus isolate belonging to ST100 and its derived VISA mutants

Infect Genet Evol. 2016 Sep:43:197-202. doi: 10.1016/j.meegid.2016.05.001. Epub 2016 May 3.

Abstract

In Staphylococcus aureus, transposition of IS256 has been described to play an important role in biofilm formation and antibiotic resistance. This study describes the molecular characterization of two clinical heterogeneous vancomycin-intermediate S. aureus (hVISA) isolates recovered from the same patient (before and after antibiotic treatment) and two VISA derivatives obtained by serial passages in the presence of vancomycin. Our results showed that antibiotic treatment (in vivo and in vitro) could enhance IS256 transposition, being responsible for the eventual loss of agr function. As far as we know this is the first study that reports the increase of IS256 transposition in isogenic strains after antibiotic treatment in a clinical setting.

Keywords: IS256 transposition; S. aureus; hVISA/VISA.

Publication types

  • Case Reports
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Bacterial Typing Techniques
  • Biofilms / drug effects*
  • Biofilms / growth & development
  • DNA Transposable Elements*
  • Gene Expression
  • Genotype
  • Humans
  • Male
  • Microbial Sensitivity Tests
  • Phosphoric Monoester Hydrolases / genetics*
  • Phosphoric Monoester Hydrolases / metabolism
  • Sigma Factor / genetics*
  • Sigma Factor / metabolism
  • Staphylococcal Infections / microbiology
  • Staphylococcus aureus / drug effects*
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / growth & development
  • Vancomycin / pharmacology
  • Vancomycin Resistance / genetics*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • DNA Transposable Elements
  • SigB protein, Bacteria
  • Sigma Factor
  • Vancomycin
  • Phosphoric Monoester Hydrolases