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Antimicrobial Agents and Chemotherapy, August 1998, p. 1966-1972, Vol. 42, No. 8
Microbiologie Moléculaire et
Génie des Protéines, Sciences de la Vie et de la
Santé, Faculté de Médecine et Pavillon
Charles-Eugène Marchand, Université Laval, Ste-Foy,
Québec, Canada G1K 7P4
Received 23 May 1997/Returned for modification 21 September
1997/Accepted 30 May 1998
We determined the nucleotide sequences of
blaCARB-4 encoding CARB-4 and deduced a
polypeptide of 288 amino acids. The gene was characterized as a variant
of group 2c carbenicillin-hydrolyzing
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Structure of CARB-4 and AER-1 CarbenicillinHydrolyzing
-Lactamases
-lactamases such as
PSE-4, PSE-1, and CARB-3. The level of DNA homology between the
bla genes for these
-lactamases varied from 98.7 to 99.9%, while that between these genes and
blaCARB-4 encoding CARB-4 was 86.3%. The
blaCARB-4 gene was acquired from some other source because it has a G+C content of 39.1%, compared to a G+C content of 67% for typical Pseudomonas aeruginosa genes.
DNA sequencing revealed that blaAER-1 shared
60.8% DNA identity with blaPSE-3 encoding
PSE-3. The deduced AER-1
-lactamase peptide was compared to class A, B, C, and D enzymes and had 57.6% identity with PSE-3, including an STHK tetrad at the active site. For CARB-4 and AER-1, conserved canonical amino acid boxes typical of class A
-lactamases were identified in a multiple alignment.
Analysis of the DNA sequences flanking
blaCARB-4 and blaAER-1
confirmed the importance of gene cassettes acquired via integrons in
bla gene distribution.
*
Corresponding author. Mailing address: Microbiologie
Moléculaire et Génie des Protéines, Sciences de la
Vie et de la Santé, Faculté de Médecine et Pavillon
Charles-Eugène Marchand, Université Laval, Ste-Foy,
Québec, Canada G1K 7P4. Phone: (418) 656-3070. Fax: (418)
656-7176. E-mail: rclevesq{at}rsvs.ulaval.ca.
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