Antimicrobial Agents and Chemotherapy, December 2001, p. 3355-3361, Vol. 45, No. 12
0066-4804/01/$04.00+0 DOI: 10.1128/AAC.45.12.3355-3361.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
-Lactamase That
Hydrolyzes Ceftazidime through a Single Amino Acid Substitution in
the Omega Loop
Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, 94275 Le Kremlin-Bicêtre Cedex,1 and Service de Microbiologie, Hôpital Robert Debré, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Xavier-Bichat, 75018 Paris,2 France
Received 18 December 2000/Returned for modification 11 April 2001/Accepted 21 August 2001
Escherichia coli ILT-1, Klebsiella
pneumoniae ILT-2, and K. pneumoniae
ILT-3 were isolated in May 1999 in Paris, France, from a rectal swab of
a hospitalized 5-month-old girl. These isolates had a clavulanic
acid-inhibited substrate profile that included expanded-spectrum
cephalosporins. The MICs of cefotaxime were higher for E. coli ILT-1 and K. pneumoniae ILT-2 than for K. pneumoniae ILT-3, while the opposite was found for the MICs of
ceftazidime. Genetic and biochemical analyses revealed that E. coli ILT-1 and K. pneumoniae ILT-2 produced the
CTX-M-18
-lactamase, while K. pneumoniae ILT-3 produced
the CTX-M-19
-lactamase. The amino acid sequence of the
CTX-M-18
-lactamase differed from that of the CTX-M-9
-lactamase
by an Ala-to-Val change at position 231, while CTX-M-19 possessed
an additional Pro-to-Ser change at position 167 in the omega loop of
Ambler class A enzymes. The latter amino acid substitution may explain
the CTX-M-19-mediated hydrolysis of ceftazidime, which has not been
reported for other CTX-M-type enzymes. The
blaCTX-M-18 and
blaCTX-M-19 genes were located on transferable plasmids that varied in size (ca. 60 and 50 kb,
respectively) but that showed similar restriction patterns.
This article has been cited by other articles:
| Clin. Vaccine Immunol. | Clin. Microbiol. Rev. |
|---|---|
| J. Clin. Microbiol. | ALL ASM JOURNALS |