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has been cited by the following article:

• TITLE: Activity of Fosfomycin in Extended-Spectrum Beta-Lactamases Producing Klebsiella pneumonae from Hospital Acquired Urinary Tract Infections

  AUTHORS: Ghada El-Saeed Mashaly

  KEYWORDS: Klebsiella pneumonae, Extended-Spectrum Beta-Lactamases, Fosfomycin, Urinary Tract Infection, Plasmid Mediated Resistance

  JOURNAL NAME: Open Journal of Medical Microbiology, Vol.6 No.3, August 3, 2016

  ABSTRACT: Treatment of hospital acquired urinary tract infections (UTIs) caused by extended-spectrum beta-Lactamases producing Klebsiella pneumonae is a major problem. This organism expresses a high level of resistance to many groups of antibiotics. Fosfomycin is an agent which is recommended for treatment of UTIs caused by ESBLs producers. The aim of this study is to determine the sensitivity pattern of ESBLs producing urinary K. pneumonae to antimicrobial agents including fosfomycin in patients of MUHs and determine the prevalence of fosfomycin resistance mediated by plasmid mediated fosfomycin modifying enzymes fosA, fosB and fosA3. Methods: Klebsiella pneumonae urinary isolates were collected from patients with hospital acquired UTIs in Mansoura University Hospitals (MUHs). The susceptibility pattern was determined by Kirby Baur method. Isolates resistant to extended spectrum cephalosporins were tested for ESBLs production by double disc diffusion method. Fosfomycin resistance was determined by broth dilution method. Isolates resistant to fosfomycin were tested for fosA, fosB and fosA3 by PCR. Results: A total of 128 ESBLs producing K. pneumonae isolates were collected. The highest sensitivity was to imipenem (94.5%). The lowest was to trimethoprime-sulphamethoxazole (21.8%). Co-resistance of ESBLs isolates with fosfomycin was 23.2%. Eighteen fosfomycin resistant isolates (18/30) were positive to fosA. Conclusion: ESBLs producing urinary Klebsiella pneumonae express moderate sensitivity to fosfomycin. Resistance is mainly mediated by plasmid mediated fosfomycin modifying enzymes fosA.