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Characterization of the enzyme aac(3)-id in a clinical isolate of Salmonella enterica serovar Haifa causing traveler's diarrhea

  • Roberto Cabrera
    ,
  • ,
  • Javier Sánchez-Céspedes
    ,
  • Pilar Goñi
    ,
  • Rafael Gómez-Lus
    ,
  • M. Teresa Jiménez De Anta
*Corresponding author for this work
  • Hospital Clinic Barcelona
    ,
  • ,
  • Hospital Clínic – Universitat de Barcelona
    ,
  • University of Zaragoza
Research Output:
Contribution to journal
Article
Peer-review

Publication Information

Output type

Research Output:
Contribution to journal
Article
Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 453-456 (4 pages)

Journal (Volume, Issue Number)

Enfermedades Infecciosas y Microbiologia Clinica (Volume 27, Issue 8)

Publication milestones

  • Published - 10/2009

Publication status

Published - 10/2009

ISSN

0213-005X

Publication IDs

  • Scopus: 70349440862
  • PubMed: 19403206

Abstract

Introduction: The objective of this investigation was to identify the mechanism of decreased susceptibility to gentamicin in a Salmonella clinical isolate, leading to the detection of a aminoglycoside acetyltransferase gene found in a class 1 integron. Methods: A multidrug-resistant Salmonella strain was recovered from feces of a traveler to Egypt. The antimicrobial susceptibility test to 12 antimicrobial agents was performed with the Kirby-Bauer method. The presence of class 1 integron was determined by PCR. The ampli.ed product was recovered and sequenced in order to establish the genes carried. In addition, susceptibility to gentamicin C1a, gentamicin C1, sisomicin, neomycin, dibekacin, kanamycin, tobramycin, amikacin, netilmicin, apramycin, dactimicin, spectinomycin, streptomycin, lividomycin and butirosin, was established. The Champion™ pET101 Directional TOPO® Expression Kit was used to clone and express the aac(3)-I gene. Results: The isolate was identi.ed as Salmonella enterica serovar Haifa, showing resistance to nalidixic acid, tetracycline and decreased susceptibility to gentamicin. One integron with a size circa 1,500 bp, encoding an aac(3)-Id plus aadA7 genes was observed. The analysis of the susceptibility to different aminoglycosides in the E. coli TOP10F' transformed with the vector carrying aac(3)-Id gene showed resistance to gentamicin C1a, gentamicin C1, and dactimicin, in accordance with the presence of this enzyme but, was susceptible to sisomicin. The homology of the amino acid and nucleotide sequences with the AAC(3)-Id enzyme was of 100%. Conclusion: The presence of the AAC(3)-Id enzyme was described for the first time in a S. Haifa.

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