High-level resistance to ceftazidime conferred by a novel enzyme, CTX-M-32, derived from CTX-M-1 through a single Asp240-Gly substitution.

نویسندگان

  • Monica Cartelle
  • Maria del Mar Tomas
  • Francisca Molina
  • Rita Moure
  • Rosa Villanueva
  • German Bou
چکیده

A clinical strain of Escherichia coli isolated from pleural liquid with high levels of resistance to cefotaxime, ceftazidime, and aztreonam harbors a novel CTX-M gene (bla(CTX-M-32)) whose amino acid sequence differs from that of CTX-M-1 by a single Asp240-Gly substitution. Moreover, by site-directed mutagenesis we demonstrated that this replacement is a key event in ceftazidime hydrolysis

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منابع مشابه

Effect of D240G substitution in a novel ESBL CTX-M-27.

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Novel chimeric beta-lactamase CTX-M-64, a hybrid of CTX-M-15-like and CTX-M-14 beta-lactamases, found in a Shigella sonnei strain resistant to various oxyimino-cephalosporins, including ceftazidime.

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High Prevalence of CTXM-15 Type Extended-Spectrum Beta-Lactamase Among Clinical Isolates of Klebsiella Pneumoniae

Background: Production of β–lactamases by enterobacteriacea, especially Klebsiella pneumoniae, is one of the emerging health problems in the world. The purpose of this study was to assess the frequency of blaCTX-M15 gene in K. pneumoniae isolates and determine the molecular diversity of CTXM producing isolates. Methods: In...

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A novel ceftazidime-hydrolysing extended-spectrum beta-lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop.

OBJECTIVES To characterize a novel ceftazidime-hydrolysing CTX-M mutant, designated CTX-M-54, produced by Klebsiella pneumoniae clinical isolate BDK0419 and to investigate its genetic environment. METHODS Antimicrobial susceptibilities were determined by disc diffusion and agar dilution methods, and the double-disc synergy test was carried out. Detection of genes encoding class A beta-lactama...

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عنوان ژورنال:
  • Antimicrobial agents and chemotherapy

دوره 48 6  شماره 

صفحات  -

تاریخ انتشار 2004