scholarly journals Characterization of beta-lactamase gene blaPER-2, which encodes an extended-spectrum class A beta-lactamase.

1996 ◽  
Vol 40 (3) ◽  
pp. 616-620 ◽  
Author(s):  
A Bauernfeind ◽  
I Stemplinger ◽  
R Jungwirth ◽  
P Mangold ◽  
S Amann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Beta Lactamase ◽  
Reading Frame ◽  
Beta Lactamases ◽  
Class A ◽  
Extended Spectrum ◽  
The Family ◽  
Extended Spectrum Beta Lactamases ◽  
Lactamase Gene

Plasmidic extended-spectrum beta-lactamases of Ambler class A are mostly inactive against ceftibuten. Salmonella typhimurium JMC isolated in Argentina harbors a bla gene located on a plasmid (pMVP-5) which confers transferable resistance to oxyiminocephalosporins, aztreonam, and ceftibuten. The beta-lactamase PER-2 (formerly ceftibutenase-1; CTI-1) is highly susceptible to inhibition by clavulanate and is located at a pI of 5.4 after isoelectric focusing. The blaPER-2 gene was cloned and sequenced. The nucleotide sequence of a 2.2-kb insert in vector pBluescript includes an open reading frame of 927 bp. Comparison of the deduced amino acid sequence of PER-2 with those of other beta-lactamases indicates that PER-2 is not closely related to TEM or SHV enzymes (25 to 26% homology). PER-2 is most closely related to PER-1 (86.4% homology), an Ambler class A enzyme first detected in Pseudomonas aeruginosa. An enzyme with an amino acid sequence identical to that of PER-1, meanwhile, was found in various members of the family Enterobacteriaceae isolated from patients in Turkey. Our data indicate that PER-2 and PER-1 represent a new group of Ambler class A extended-spectrum beta-lactamases. PER-2 so far has been detected only in pathogens (S. typhimurium, Escherichia coli, Klebsiella pneumoniae, Proteus mirabilis) isolated from patients in South America, while the incidence of PER-1-producing strains so far has been restricted to Turkey, where it occurs both in members of the family Enterobacteriaceae and in P. aeruginosa.

scholarly journals Novel extended-spectrum TEM-type beta-lactamase from an Escherichia coli isolate resistant to ceftazidime and susceptible to cephalothin.

1997 ◽  
Vol 41 (3) ◽  
pp. 715-716 ◽  
Author(s):  
C Chanal-Claris ◽  
D Sirot ◽  
L Bret ◽  
P Chatron ◽  
R Labia ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Coli Isolate ◽  
Resistance Phenotype ◽  
Numbering Scheme ◽  
Extended Spectrum

A novel extended-spectrum TEM-type beta-lactamase was detected in an Escherichia coli isolate which was resistant to ceftazidime and susceptible to cephalothin. The corresponding bla gene was sequenced. The deduced amino acid sequence showed the following three amino acid replacements with respect to the TEM-2 sequence: Glu-->Lys-104, Arg-->Ser-164, and Glu-->Lys-240. Since it confers a ceftazidimase-type resistance phenotype, we propose for this novel enzyme the designation CAZ-9, corresponding to TEM-46 in the sequential numbering scheme of TEM beta-lactamases.

scholarly journals Carboxy groups as essential residues in β-lactamases

1986 ◽  
Vol 240 (1) ◽  
pp. 215-219 ◽  
Author(s):  
C Little ◽  
E L Emanuel ◽  
J Gagnon ◽  
S G Waley
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bacillus Cereus ◽  
Bacillus Licheniformis ◽  
Enterobacter Cloacae ◽  
Amino Acid Sequences ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Class A

Beta-lactamases are divided into classes A, B and C on the basis of their amino acid sequences. Beta-Lactamases were incubated at pH 4.0 with the carboxy-group reagent 1-(3-dimethylaminopropyl)-3-ethylcarbodi-imide plus a coloured nucleophile and the extents of inactivation and nucleophile incorporation were monitored. Two class A enzymes (from Bacillus cereus and Bacillus licheniformis) and two class C enzymes (from Enterobacter cloacae P99 and Pseudomonas aeruginosa) were examined. All four enzymes were inactivated, with total inactivation corresponding to the incorporation of approx. 2-3 mol of nucleophile/mol of enzyme. In the case of beta-lactamase I from Bacillus cereus, some 53% of the incorporated nucleophile was located on glutamic acid-168 in the amino acid sequence.

scholarly journals The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an indigenous class A β-lactamase

1989 ◽  
Vol 260 (3) ◽  
pp. 803-812 ◽  
Author(s):  
J I A Campbell ◽  
S Scahill ◽  
T Gibson ◽  
R P Ambler
Keyword(s):  
Sequence Similarity ◽  
Rhodopseudomonas Capsulata ◽  
Beta Lactamase ◽  
Reading Frame ◽  
Beta Lactamases ◽  
Class A ◽  
Coli Plasmid ◽  
Total Dna ◽  
Lactamase Gene ◽  
Protein Sequence Comparison

The nucleotide sequence of a 2.37 kb DNA fragment derived from cloning a total DNA digest of Rhodopseudomonas capsulata sp108 was determined. The DNA codes for a beta-lactamase, a protein showing sequence similarity to the ampR protein of Enterobacter cloacae and an unidentified open reading frame. Hybridization experiments with a probe carrying DNA from within the beta-lactamase gene suggests a chromosomal location for the coding sequences in strain sp108 and in sp109, a penicillin-sensitive revertant of sp108 in which the enzyme is not inducible. A protein-sequence comparison of the deduced amino acid sequence of the Rps. capsulata beta-lactamase indicates that it is a Class A enzyme and that its sequence can be aligned with those of the characterized beta-lactamases from Staphylococcus aureus, Bacillus licheniformis and the Escherichia coli plasmid (R-TEM enzyme), with only a few insertions or deletions. The corresponding DNA sequence is, however, characteristically rhodopseudomonad, suggesting that it is not a recently transposed gene.

scholarly journals TEM-28 from an Escherichia coli clinical isolate is a member of the His-164 family of TEM-1 extended-spectrum beta-lactamases.

1996 ◽  
Vol 40 (1) ◽  
pp. 260-262 ◽  
Author(s):  
P A Bradford ◽  
N V Jacobus ◽  
N Bhachech ◽  
K Bush
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Clinical Isolate ◽  
Amino Acid Substitutions ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Extended Spectrum ◽  
Extended Spectrum Beta Lactamases

TEM-28 (pI 6.1), expressed by an Escherichia coli clinical isolate, is a novel beta-lactamase which hydrolyzed ceftazidime, cefotaxime, and aztreonam with rates of 25, 1.1, and 5.6, respectively, relative to that for benzylpenicillin (100). The nucleotide sequence of blaTEM-28 differed from that of blaTEM-1 by two base changes, resulting in amino acid substitutions of Arg-164 to His and Glu-240 to Lys.

scholarly journals Survey of Klebsiella pneumoniae producing extended-spectrum beta-lactamases: prevalence of TEM-3 and first identification of TEM-26 in France.

1996 ◽  
Vol 40 (4) ◽  
pp. 1027-1029 ◽  
Author(s):  
M J Soilleux ◽  
A M Morand ◽  
G J Arlet ◽  
M R Scavizzi ◽  
R Labia
Keyword(s):  
Klebsiella Pneumoniae ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Extended Spectrum Beta Lactamase ◽  
Extended Spectrum ◽  
Crude Extracts ◽  
Extended Spectrum Beta Lactamases

Crude extracts from 115 extended-spectrum beta-lactamase-producing Klebsiella pneumoniae isolates were analyzed biochemically. The TEM-3 type was encountered 108 times, SHV types were encountered 7 times, and the TEM-26 type was encountered only once. For the last one, the gene was identified; an adenine was detected at position 925, as in blaTEM-26B not in blaTEM-26.

scholarly journals The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275

1985 ◽  
Vol 229 (3) ◽  
pp. 791-797 ◽  
Author(s):  
R Bicknell ◽  
E L Emanuel ◽  
J Gagnon ◽  
S G Waley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
The Other ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Zinc Enzyme ◽  
Pseudomonas Maltophilia ◽  
Measurable Rate ◽  
Beta Lactamase Ii

The production and purification of a tetrameric zinc beta-lactamase from Pseudomonas maltophilia IID 1275 were greatly improved. Three charge variants were isolated by chromatofocusing. The subunits each contain two atomic proportions of zinc and (in two of the variants) one residue of cysteine. The thiol group is not required for activity, nor does it appear to bind to the metal. Replacement of zinc by cobalt, cadmium or nickel takes place at a measurable rate, and gives enzymes that are less active than the zinc enzyme. The properties of this enzyme differ from those of the other known zinc beta-lactamase, beta-lactamase II from Bacillus cereus. The amino acid sequence of the N-terminal 32 residues was determined; there is no similarity to the N-terminal sequences of other beta-lactamases.

scholarly journals Molecular characterization of extended-spectrum beta-lactamases in Enterobacteriaceae from patients of two hospitals in Saxony, Germany

2007 ◽  
Vol 56 (2) ◽  
pp. 241-249 ◽  
Author(s):  
Joachim Schmitt ◽  
Enno Jacobs ◽  
Herbert Schmidt
Keyword(s):  
Plasmid Dna ◽  
Klebsiella Oxytoca ◽  
Rflp Analysis ◽  
Beta Lactamase ◽  
M Gene ◽  
Beta Lactamases ◽  
Extended Spectrum Beta Lactamase ◽  
Extended Spectrum ◽  
Genes Encoding ◽  
Extended Spectrum Beta Lactamases

Between January and September 2003, 39 isolates of the family Enterobacteriaceae with phenotypically positive Vitek 1 extended-spectrum beta-lactamase (ESBL) test results were collected, originating from patients of two hospitals in Saxony, Germany. Plasmid DNA was isolated and screened by PCR for the presence of genes encoding beta-lactamases of SHV, TEM and CTX-M types. To differentiate ESBL and non-ESBL among SHV and TEM genes, detailed analysis of PCR products was performed. Twenty-four strains carried SHV-2, SHV-5 or SHV-12 genes. In a further 11 strains a CTX-M gene was detected. The CTX-M genes could be affiliated to the CTX-M-1 and CTX-M-9 cluster by RFLP analysis. In the case of four Klebsiella oxytoca isolates, hyperproduction of the chromosomal beta-lactamase K1 was inferred, because genes of the above-mentioned types were not detected. The strains contained plasmid DNA between 45 and 160 kb in size. Common plasmid restriction patterns among SHV-5 producers provided evidence of horizontal spread. Twenty strains had a MIC for cefotaxime of ⩽4 mg l−1, 18 strains had the same MIC for ceftazidime, and nine strains had this MIC of >4 mg l−1 for both antibiotics. The ESBL phenotypes often coincided with ciprofloxacin or gentamicin resistance.

scholarly journals Relationship between isolation of extended spectrum beta-lactamase-producing Klebsiella pneumoniae and course of hospital-acquired pneumonia

Medicina ◽  
2007 ◽  
Vol 43 (10) ◽  
pp. 778
Author(s):  
Astra Vitkauskienė ◽  
Agnė Giedraitienė ◽  
Vytis Dudzevičius ◽  
Raimundas Sakalauskas
Keyword(s):  
Klebsiella Pneumoniae ◽  
Late Onset ◽  
Lavage Fluid ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Extended Spectrum Beta Lactamase ◽  
Extended Spectrum ◽  
Extended Spectrum Beta Lactamases ◽  
Hospital Acquired Pneumonia ◽  
Hospital Acquired

Aim of the study. To evaluate relationship between isolation of extended spectrum beta-lactamaseproducing Klebsiella pneumoniae strains and course of hospital-acquired pneumonia. Materials and methods. K. pneumoniae strains isolated from bronchial secretions or bronchoalveolar lavage fluid samples of patients hospitalized at an intensive care unit of Kaunas University of Medicine Hospital were analyzed. By means of synergistic two-antibiotics disc method, K. pneumoniae strains producing extended spectrum beta-lactamases were selected for further analysis using E-test (AB Biodisk, Solna, Sweden). Hospitalacquired pneumonia was diagnosed based on standard criteria for the diagnosis of pneumonia if signs of pneumonia occurred after 48 hours following admission. Late-onset hospital-acquired pneumonia was considered if these signs of pneumonia occurred on fifth day of hospitalization or later. Results. Total of 45 strains of K. pneumoniae were isolated during the study period; 18 isolated strains produced ESBL. Thirty-two patients investigated have developed hospital-acquired pneumonia, 20 of which were cases of late-onset hospital-acquired pneumonia. Thirteen cases of K. pneumoniae isolation were classified as airway colonization. Extended spectrum beta-lactamase-producing K. pneumoniae strains were more frequently isolated from patients with hospital-acquired pneumonia (88.9%, n=16 and 11.1%, n=2, P<0.05) in comparison with non-producing strains. Extended spectrum beta-lactamase-producing strains were more prevalent in late-onset pneumonia group (93.8%, n=15) than in early-onset group (6.2%, n=1, P<0.001). Conclusions. Extended spectrum beta-lactamase-producing K. pneumoniae strains were more frequently isolated from patients with hospital-acquired pneumonia as compared to colonized patients. Extended spectrum beta-lactamase-producing K. pneumoniae strains were more frequently isolated from patients with late-onset hospital-acquired pneumonia.

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