High-level amikacin resistance in Pseudomonas aeruginosa associated with a 3'-phosphotransferase with high affinity for amikacin.

  1. Torres, C. 3
  2. Perlin, M.H. 1
  3. Baquero, F. 5
  4. Lerner, D.L. 2
  5. Lerner, S.A. 4
  1. 1 University of Louisville
    info

    University of Louisville

    Louisville, Estados Unidos

    ROR https://ror.org/01ckdn478

  2. 2 Washington University in St. Louis
    info

    Washington University in St. Louis

    San Luis, Estados Unidos

    ROR https://ror.org/01yc7t268

  3. 3 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  4. 4 Wayne State University
    info

    Wayne State University

    Detroit, Estados Unidos

    ROR https://ror.org/01070mq45

  5. 5 Hospital Ramón y Cajal
    info

    Hospital Ramón y Cajal

    Madrid, España

    ROR https://ror.org/050eq1942

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Revista:
International Journal of Antimicrobial Agents

ISSN: 0924-8579

Año de publicación: 2000

Volumen: 15

Número: 4

Páginas: 257-263

Tipo: Artículo

DOI: 10.1016/S0924-8579(00)00174-6 PMID: 10929874 SCOPUS: 2-s2.0-0033861098 WoS: WOS:000088309700002 GOOGLE SCHOLAR

Otras publicaciones en: International Journal of Antimicrobial Agents

Repositorio institucional: lock_openAcceso abierto Editor

Resumen

This work describes the characterization of the phosphotransferase enzymatic activity responsible for amikacin resistance in two clinical Pseudomona aeruginosa strains, isolated from a hospital that used amikacin as first-line aminoglycoside. Amikacin-resistant P. aeruginosa PA40 and PA43 (MIC: 128 mg/l) were shown to have APH activity with a substrate profile similar to that of APH(3')-VI. The enzyme from P. aeruginosa PA40 was purified to >70% homogeneity. The K(m) of amikacin for this enzyme was 1.4 μM, the V(max)/K(m) ratio for amikacin was higher than for the other aminoglycosides tested and PCR and DNA sequencing ruled out the presence of aph(3')-IIps. Amikacin resistance in this strain was, therefore, associated with APH(3')-VI and the high affinity of this enzyme for amikacin could explain the high-level resistance that we observed.