Aminoglycoside-modifying enzymes in high-level streptomycin and gentamicin resistant Enterococcus spp strains in Spain.
- Del Campo, R. 2
- Tenorio, C. 1
- Rubio, C. 2
- Castillo, J. 2
- Torres, C. 1
- Gómez-Lus, R. 2
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1
Universidad de La Rioja
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2
Universidad de Zaragoza
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ISSN: 0924-8579
Ano de publicación: 2000
Volume: 15
Número: 3
Páxinas: 221-226
Tipo: Artigo
Outras publicacións en: International Journal of Antimicrobial Agents
Indicadores
Citas recibidas
JCR (Journal Impact Factor)
- Ano 2000
- Factor de impacto da revista: 1.141
- Factor de impacto sen autocitas: 1.047
- Article influence score: 0.0
- Cuartil maior: Q3
- Área: MICROBIOLOGY Cuartil: Q3 Posición na área: 50/83 (Edición: SCIE)
- Área: PHARMACOLOGY & PHARMACY Cuartil: Q3 Posición na área: 105/181 (Edición: SCIE)
- Área: INFECTIOUS DISEASES Cuartil: Q4 Posición na área: 28/36 (Edición: SCIE)
SCImago Journal Rank
- Ano 2000
- Impacto SJR da revista: 0.446
- Cuartil maior: Q1
- Área: Medicine (miscellaneous) Cuartil: Q1 Posición na área: 681/3043
- Área: Microbiology (medical) Cuartil: Q2 Posición na área: 30/100
- Área: Infectious Diseases Cuartil: Q2 Posición na área: 68/153
- Área: Pharmacology (medical) Cuartil: Q2 Posición na área: 54/173
Resumo
Aminoglycoside resistance was evaluated in 690 enterococcus strains isolated from different clinical sources originating from patients at the University Clinic Hospital of Zaragoza (Spain). The enterococci obtained from clinically significant samples (blood, urine, or exudates) showed more high- level resistance to gentamicin and streptomycin (65 and 42%, respectively) than those isolated from faecal samples (49 and 23%, respectively). Aminoglycoside-modifying enzymes (AME) from 119 of these high-level gentamicin and streptomycin resistant enterococcus strains were studied. The most frequent AMEs found were APH(3') and AAC(6')-APH(2''). More than one enzyme was detected in 71% of the strains (four different enzymes in 5% of the strains). Three Enterococcus faecalis strains had ANT(4')(4'') enzymatic activity. Different enzymatic expressions of the bifunctional enzyme AAC(6')- APH(2'') were demonstrated in strains in which the complete aac(6')-aph(2'') gene was detected by PCR and hybridization: (i) AAC(6') + APH(2'') activity; (ii) AAC(6') only; (iii) APH(2'') only; and (iv) no activity of AAC(6') or APH(2''). (C) 2000 Elsevier Science B.V. and International Society of Chemotherapy.