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Nanomechanics of Drug-target Interactions and Antibacterial Resistance Detection
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High-Level Fosfomycin Resistance in Vancomycin-Resistant Enterococcus faecium.

Yan Guo, Adam D Tomich, Christi L McElheny

    Emerging Infectious Diseases
    |October 20, 2017
    PubMed
    Summary

    Four vancomycin-resistant Enterococcus faecium isolates showed extremely high fosfomycin resistance. A specific mutation in UDP-N-acetylglucosamine enolpyruvyl transferase was identified as the cause of this resistance.

    Keywords:
    Enterococcus faeciumMurAUDP-N-acetylglucosamine enolpyruvyl transferaseantimicrobial resistancebacteriafosfomycinfosfomycin resistancevancomycinvancomycin resistancevancomycin-resistant enterococci

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    Area of Science:

    • Microbiology
    • Drug Resistance
    • Biochemistry

    Background:

    • Vancomycin-resistant Enterococcus faecium (VRE) is a significant healthcare-associated pathogen.
    • Fosfomycin is an antibiotic used to treat certain bacterial infections, including those caused by VRE.
    • Emergence of fosfomycin resistance in VRE is a growing concern.

    Purpose of the Study:

    • To investigate the prevalence and mechanisms of high-level fosfomycin resistance in vancomycin-resistant Enterococcus faecium isolates.
    • To identify genetic alterations associated with fosfomycin resistance in these isolates.

    Main Methods:

    • Rectal screening of patients to obtain VRE isolates.
    • Determination of fosfomycin Minimum Inhibitory Concentrations (MICs).
    • Biochemical assays to assess drug activity and enzyme function.
    • Genetic sequencing to identify mutations in UDP-N-acetylglucosamine enolpyruvyl transferase.

    Main Results:

    • Out of 890 VRE isolates, 4 exhibited exceptionally high fosfomycin MICs (>1,024 μg/mL).
    • These resistant isolates possessed a Cys119Asp substitution in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase.
    • This specific mutation conferred a >4-fold increase in fosfomycin MIC.
    • The Cys119Asp substitution rendered fosfomycin inactive in biochemical assays.

    Conclusions:

    • A specific mutation (Cys119Asp) in UDP-N-acetylglucosamine enolpyruvyl transferase is responsible for high-level fosfomycin resistance in VRE.
    • This finding highlights a potential mechanism for fosfomycin treatment failure in VRE infections.
    • Further surveillance and research are needed to monitor and understand fosfomycin resistance in VRE.