Genetic and biochemical characterization of GES-5, an extended-spectrum class A β-lactamase from Klebsiella pneumoniae

2007 ◽  
Vol 58 (4) ◽  
pp. 465-468 ◽  
Author(s):  
Il Kwon Bae ◽  
You-Nae Lee ◽  
Seok Hoon Jeong ◽  
Seong Geun Hong ◽  
Jung Hun Lee ◽  
...  
2008 ◽  
Vol 52 (5) ◽  
pp. 1897-1898 ◽  
Author(s):  
Nuno Mendonça ◽  
Richard Bonnet ◽  
Manuela Caniça ◽  
Vera Manageiro

2011 ◽  
Vol 55 (12) ◽  
pp. 5930-5932 ◽  
Author(s):  
Kyungwon Lee ◽  
Jong Hwa Yum ◽  
Dongeun Yong ◽  
Seok Hoon Jeong ◽  
Gian Maria Rossolini ◽  
...  

ABSTRACTThe TEM-107 extended-spectrum β-lactamase detected in aKlebsiella pneumoniaeclinical isolate had a Gly238Ser substitution compared to the TEM-43 β-lactamase. The MIC of ceftazidime was higher (64 μg/ml) than that of cefotaxime (2 μg/ml) for the isolate. Clavulanic acid reduced the MIC of ceftazidime 64-fold.


2009 ◽  
Vol 53 (7) ◽  
pp. 3010-3016 ◽  
Author(s):  
Anaïs Potron ◽  
Laurent Poirel ◽  
Jacques Croizé ◽  
Vanessa Chanteperdrix ◽  
Patrice Nordmann

ABSTRACT Acinetobacter baumannii isolate KAR was uncommonly more resistant to cefepime and cefpirome than to ceftazidime and cefotaxime. Cloning and expression of the β-lactamase gene content of this isolate into Escherichia coli TOP10 identified ß-lactamase RTG-4 (or CARB-10), which corresponds to the first reported extended-spectrum CARB-type enzyme. RTG-4 is a plasmid-encoded Ambler class A β-lactamase whose sequence differs by 4 amino acid substitutions from the narrow-spectrum β-lactamase RTG-3. RTG-4 hydrolyzes cefepime and cefpirome and weakly hydrolyzes ceftazidime due to the single Ser-to-Thr substitution at Ambler position 69. RTG-4 is less susceptible to inhibition by tazobactam and sulbactam than RTG-3. Expression of β-lactamase RTG-4 in a wild-type A. baumannii reference strain showed that it conferred resistance to cefepime and cefpirome. The genetic environment of the bla RTG-4 gene was made of a peculiar transposon located on a ca. 50-kb plasmid. ISAba9, located upstream of bla RTG-4, may be responsible for its acquisition by recognizing a secondary right inverted repeat sequence, thus acting by a one-ended transposition process.


2011 ◽  
Vol 60 (9) ◽  
pp. 1344-1352 ◽  
Author(s):  
Abouddihaj Barguigua ◽  
Fatima El Otmani ◽  
Mustapha Talmi ◽  
Fatna Bourjilat ◽  
Fatima Haouzane ◽  
...  

2016 ◽  
Vol 60 (5) ◽  
pp. 3183-3186 ◽  
Author(s):  
Sushmita D. Lahiri ◽  
Richard A. Alm

ABSTRACTCeftazidime-avibactam has activity againstPseudomonas aeruginosaandEnterobacteriaceaeexpressing numerous class A and class C β-lactamases, although the ability to inhibit many minor enzyme variants has not been established. Novel VEB class A β-lactamases were identified during characterization of surveillance isolates. The cloned novel VEB β-lactamases possessed an extended-spectrum β-lactamase phenotype and were inhibited by avibactam in a concentration-dependent manner. The residues that comprised the avibactam binding pocket were either identical or functionally conserved. These data demonstrate that avibactam can inhibit VEB β-lactamases.


2004 ◽  
Vol 48 (9) ◽  
pp. 3579-3582 ◽  
Author(s):  
Bibiana Caporale ◽  
Nicola Franceschini ◽  
Mariagrazia Perilli ◽  
Bernardetta Segatore ◽  
Gian Maria Rossolini ◽  
...  

ABSTRACT Three mutants of the extended-spectrum β-lactamase TEM-60, the P51L, K104E, and S164R mutants, were constructed by site-directed mutagenesis. The kinetic parameters of the mutated enzymes and interactions of inhibitors were significantly different from those of TEM-60, revealing that the L51P mutation plays an important role in enzyme activity and stability in the TEM-60 background.


2012 ◽  
Vol 13 (1) ◽  
pp. 901-917 ◽  
Author(s):  
Mun Teng Wong ◽  
Sy Bing Choi ◽  
Chee Sian Kuan ◽  
Siang Ling Chua ◽  
Chiat Han Chang ◽  
...  

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