[Discovery of new structure of class 1 integron in MDR Pseudomonas aeruginosa and its association with drug-resistance]

Wei Sheng Wu Xue Bao. 2013 Sep 4;53(9):927-32.
[Article in Chinese]

Abstract

Objective: To investigate the characteristics of class I integrons among clinical multidrug-resistant Pseudomonas aeruginosa isolates, and to analyze the association between class I integrons and multidrug resistance.

Methods: Pseudomonas aeruginosa strains were isolated from clinical samples, and the multidrug-resistant ones were picked out from these isolates. PCR assays were used to detect the variable regions of class I integrons, and the resulting products were then digested with restriction enzyme Sau 3A I and sequenced. SPSS19.0 software was used for statistical analysis.

Results: Class I integrons were detected in 27.3% of the clinical multidrug-resistant Pseudomonas aeruginosa isolates. Amplification of variable regions of class I integrons revealed three different gene cassette arrays (1500, 2300 and 4000 bp), two of them were also found in other bacteria. These gene cassette arrays encoded aminoglycoside-modifying enzymes (aadA, aadB, aac(6') II and aadA13), beta-lactamases (blaCARB8 and oxa10) and chloromycetin efflux pump (cmlA8). Analysis results suggested closely relationship between class I integrons and aminoglycoside resistance.

Conclusion: We revealed three different gene cassette arrays in the clinical isolates of the multidrug-resistant Pseudomonas aeruginosa, and gene cassette array aadB-aac(6') II -blaCARB8 was the most prevalent. The three gene cassette arrays all contained the aminoglycoside-resistant genes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Drug Resistance, Multiple, Bacterial*
  • Integrons*
  • Microbial Sensitivity Tests
  • Pseudomonas aeruginosa / drug effects*
  • Pseudomonas aeruginosa / genetics*
  • Pseudomonas aeruginosa / metabolism
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • beta-Lactamases