The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide

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The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide.

Beta-lactamase induction in Enterobacter cloacae, which is linked to peptidoglycan recycling, was investigated by high-performance liquid chromatographic analysis of cell wall fragments in genetically defined cells of Escherichia coli. After treatment of cells with beta-lactams, we detected an increase in a D-tripeptide (disaccharide-tripeptide, N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-...

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Chromosomal beta-lactamase expression and antibiotic resistance in Enterobacter cloacae.

The activities of beta-lactam antibiotics were compared against Enterobacter cloacae clinical isolates and mutants which had inducible, stably-derepressed, and basal expression of a pI 8.4 subtype of the Ia chromosomal beta-lactamase. These activities were correlated with the results of studies of the beta-lactamase-lability and beta-lactamase-inducer-power of the antibiotics. Cefoxitin and amp...

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SHV-type extended-spectrum beta-lactamase production is associated with Reduced cefepime susceptibility in Enterobacter cloacae.

Cefepime is a potentially useful antibiotic for treatment of infections with Enterobacter cloacae. However, in our institution the MIC(90) for E. cloacae bloodstream isolates is 16 microg/ml. PCR amplification of bla genes revealed that one-third (15/45) of E. cloacae bloodstream isolates produced SHV-type extended-spectrum beta-lactamases (ESBLs) in addition to hyperproduction of AmpC-type bet...

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Outbreak of infection caused by Enterobacter cloacae producing the novel VEB-3 beta-lactamase in China.

Over a 4-month period from November 2002 to February 2003, 27 ceftazidime-resistant or cefotaxime-resistant nonrepetitive Enterobacter cloacae isolates were collected from 27 patients hospitalized at HuaShan Hospital, Shanghai, People's Republic of China. The Etest did not detect extended-spectrum beta-lactamases (ESBLs) in those 27 isolates; however, screening by the NCCLS ESBL disk test and c...

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Structure-function studies of Ser-289 in the class C beta-lactamase from Enterobacter cloacae P99.

Site-directed mutagenesis of Ser-289 of the class C beta-lactamase from Enterobacter cloacae P99 was performed to investigate the role of this residue in beta-lactam hydrolysis. This amino acid lies near the active site of the enzyme, where it can interact with the C-3 substituent of cephalosporins. Kinetic analysis of six mutant beta-lactamases with five cephalosporins showed that Ser-289 can ...

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ژورنال

عنوان ژورنال: Antimicrobial Agents and Chemotherapy

سال: 1997

ISSN: 0066-4804,1098-6596

DOI: 10.1128/aac.41.10.2113