Journal of Antimicrobial Chemotherapy, Vol 40, 543-549, Copyright © 1997 by The British Society for Antimicrobial Chemotherapy
T Deguchi, M Yasuda, M Nakano, S Ozeki, E Kanematsu, Y Nishino, S Ishihara and Y Kawada
We have determined partial sequences of the gyrA and parC genes of
Enterobacter cloacae type strain including the regions analogous to the
quinolone resistance-determining region of the Escherichia coli gyrA gene.
The deduced 65- and 49-amino acid sequences of the determined regions of
the E. cloacae gyrA and parC genes were identical to the corresponding
regions of the E. coli GyrA and ParC proteins, respectively. We examined 40
clinical strains of E. cloacae isolated from patients with urinary tract
infection for susceptibilities to nalidixic acid and ciprofloxacin. Based
on the nalidixic acid and ciprofloxacin MICs, these isolates were divided
into 19 quinolone- susceptible strains (MICs of nalidixic acid, 3.13-25
mg/L; MICs of ciprofloxacin, < or = 0.025 mg/L) and 21
quinolone-resistant strains (MICs of nalidixic acid, 400 to > 800 mg/L;
MICs of ciprofloxacin, 0.39- 100 mg/L). We analysed five
quinolone-susceptible and 21 quinolone- resistant strains for alterations
in GyrA and ParC. The five quinolone- susceptible strains had amino acid
sequences in GyrA and ParC identical to those of type strain. Of the 21
quinolone-resistant isolates, three (MICs of nalidixic acid, 400 to >
800 mg/L; MICs of ciprofloxacin, 0.39- 3.13 mg/L) had a single amino acid
change at the position equivalent to Ser-83 in the E. coli GyrA protein and
no alterations in ParC; one (MIC of nalidixic acid, > 800 mg/L; MIC of
ciprofloxacin, 3.13 mg/L) had a single amino acid change at Ser-83 in GyrA
and a single amino acid change at the position equivalent to Glu-84 in the
E. coli ParC protein; two (MIC of nalidixic acid, > 800 mg/L; MIC of
ciprofloxacin, 25 mg/L) had double amino acid changes at Ser-83 and Asp-87
in GyrA and no alterations in ParC; and 15 (MICs of nalidixic acid, >
800 mg/L; MICs of ciprofloxacin, 25-100 mg/L) had double amino acid changes
at Ser-83 and Asp-87 in GyrA and a single amino acid change at Ser-80 or
Glu-84 in ParC. This study suggests, that in clinical isolates of E.
cloacae, DNA gyrase is a primary target of quinolones, that only a single
amino acid change at Ser-83 in GyrA is sufficient to generate high-level
resistance to nalidixic acid and to decrease susceptibility to
ciprofloxacin, and that the accumulation of amino acid changes in GyrA and
the simultaneous presence of the ParC alterations play a central role in
developing high-level resistance to ciprofloxacin.
ORIGINAL ARTICLES
Detection of mutations in the gyrA and parC genes in quinolone- resistant clinical isolates of Enterobacter cloacae
Department of Urology, Gifu University School of Medicine, Japan.
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