Plazomicin Activity against 346 Extended-Spectrum-β-Lactamase/AmpC-Producing Escherichia coli Urinary Isolates in Relation to Aminoglycoside-Modifying Enzymes | Zendy

Maria del Carmen López-Diaz | Zendy; Esther Culebras | Zendy; Iciar Rodríguez-Avial | Zendy; Esther Ríos | Zendy; José Manuel Viñuela-Prieto | Zendy; Juan J. Picazo | Zendy; Carmen Rodríguez-Avial | Zendy

Open Access

Plazomicin Activity against 346 Extended-Spectrum-β-Lactamase/AmpC-Producing Escherichia coli Urinary Isolates in Relation to Aminoglycoside-Modifying Enzymes

Author(s) -

Maria del Carmen López-Diaz,

Esther Culebras,

Iciar Rodríguez-Avial,

Esther Ríos,

José Manuel Viñuela-Prieto,

Juan J. Picazo,

Carmen Rodríguez-Avial

Publication year - 2016

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.02454-16

Subject(s) - escherichia coli , aminoglycoside , microbiology and biotechnology , enterobacteriaceae , urinary system , enzyme , antibiotics , biology , chemistry , gene , biochemistry , endocrinology

The activity of plazomicin and clinically relevant aminoglycosides was tested against 346 extended-spectrum-β-lactamase/AmpC-producingEscherichia coli urinary isolates, and the results were correlated with the presence of aminoglycoside-modifying enzymes (AMEs). Data showed that plazomicin was very active against all ESBL/AmpC-producingE. coli urinary isolates. Its activity was not related to the AME genes studied.

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