scholarly journals Chromosomal beta-lactamase genes of Klebsiella oxytoca are divided into two main groups, blaOXY-1 and blaOXY-2.

1996 ◽  
Vol 40 (2) ◽  
pp. 454-459 ◽  
Author(s):  
B Fournier ◽  
P H Roy ◽  
P H Lagrange ◽  
A Philippon
Keyword(s):  
Sequence Similarity ◽  
Klebsiella Oxytoca ◽  
Dna Probe ◽  
Beta Lactamase ◽  
Amino Acid Similarity ◽  
Beta Lactamases ◽  
Isoelectric Points ◽  
Extended Spectrum Beta Lactamases ◽  
Citrobacter Diversus ◽  
Lactamase Gene

The chromosomally encoded beta-lactamase gene (blaOXY-2) of the wild-type Klebsiella oxytoca SL911 was cloned and sequenced. Its nucleotide sequence similarity with the previously sequenced K. oxytoca beta-lactamase gene (blaOXY-1) (Y. Arakawa, M. Ohta, N. Kido, M. Mori, H. Ito, T. Komatsu, Y. Fujii, and N. Kato, Antimicrob. Agents Chemother. 33:63-70, 1989) is 87.3%, and its amino acid similarity is 89.7%. This group of K. oxytoca beta-lactamases is related to chromosomal beta-lactamases of Citrobacter diversus, Proteus vulgaris, and Yersinia enterocolitica and to the plasmid-mediated extended-spectrum beta-lactamases MEN-1 and Toho-1. By colony hybridization with 86 strains susceptible and resistant to aztreonam, isolated in six countries, K. oxytoca beta-lactamase genes hybridized with either a specific blaOXY-1 DNA probe (668 bp) or a blaOXY-2 DNA probe (723 bp). Thus, beta-lactamase genes could be divided into two groups: blaOXY-1 (47% of the strains) and blaOXY-2 (53% of the strains). A study of isoelectric points confirmed the great variability reported in the literature. However, the two beta-lactamase groups were each represented by four different pIs: for OXY-2, 5.2, 5.7, 6.4, and 6.8, with the 5.2 form representing 59% of all OXY-2 enzymes, and for OXY-1, 7.1, 7.5, 8.2, and 8.8, with the 7.5 form representing 88% of all OXY-1 enzymes.

scholarly journals Variability of chromosomally encoded beta-lactamases from Klebsiella oxytoca.

1997 ◽  
Vol 41 (8) ◽  
pp. 1641-1648 ◽  
Author(s):  
B Fournier ◽  
P H Roy
Keyword(s):  
Klebsiella Oxytoca ◽  
Beta Lactamase ◽  
Beta Lactam ◽  
Beta Lactams ◽  
Beta Lactamases ◽  
Main Form ◽  
Extended Spectrum Beta Lactamases ◽  
Lactamase Gene ◽  
Hydrolysis Of ◽  
Substrate Hydrolysis

The beta-lactamase genes of Klebsiella oxytoca were previously divided into two main groups: bla(OXY-1) and bla(OXY-2). The two beta-lactamase groups were each represented by beta-lactamases with four different pIs. In each group, one form of beta-lactamase is more frequent than the others combined. The beta-lactamase gene of each representative beta-lactamase with a different pI that was not yet sequenced (pIs 5.7, 6.8 [OXY-2], 7.1, 8.2, and 8.8 [OXY-1]) was cloned and sequenced. The susceptibility patterns as well as relative rates and kinetic parameters for beta-lactam hydrolysis revealed that OXY-2 enzymes hydrolyzed several of the beta-lactams that were examined (carbenicillin, cephalothin, cefamandole, ceftriaxone, and aztreonam) at a greater rate than the OXY-1 enzymes did. Comparison of K. oxytoca beta-lactamases with plasmid-mediated extended-spectrum beta-lactamases MEN-1 and TOHO-1 implied that the threonine at position 168 present in OXY-2 beta-lactamase instead of the alanine in OXY-1 could be responsible for its modified substrate hydrolysis. In each group, the beta-lactamase with a variant pI differs from the main form of beta-lactamase by one to five amino acid substitutions. The substrate profile and the 50% inhibitory concentrations revealed that all substitutions differing from the main form of beta-lactamase were neutral except one difference in the OXY-1 group. This substitution of an Ala to a Gly at position 237 increases the hydrolysis of some beta-lactams, particularly aztreonam; decreases the hydrolysis of benzylpenicillin, cephaloridine, and cefamandole, and decreases the susceptibility to clavulanic acid (fivefold increase in the 50% inhibitory concentration).

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 Proteolytic interconversion and N-terminal sequences of the Citrobacter diversus major β-lactamases

1991 ◽  
Vol 275 (3) ◽  
pp. 629-633 ◽  
Author(s):  
N Franceschini ◽  
G Amicosante ◽  
M Perilli ◽  
M Maccarrone ◽  
A Oratore ◽  
...  
Keyword(s):  
Klebsiella Oxytoca ◽  
Limited Proteolysis ◽  
Major Product ◽  
Beta Lactamase ◽  
Amino Acid Residues ◽  
Beta Lactamases ◽  
Citrobacter Diversus ◽  
High Degree ◽  
Papain Digestion ◽  
Degree Of Similarity

The N-terminal sequences of the two major beta-lactamases produced by Citrobacter diversus differed only by the absence of the first residue in form II and the loss of five amino acid residues at the C-terminal end. Limited proteolysis of the homogeneous form I protein yielded a variety of enzymatically active products. In the major product obtained after the action of papain, the first three N-terminal residues of form I had been cleaved, whereas at the C-terminal end the treated enzyme lacked five residues. However, this cannot explain the different behaviours of form I, form II and papain digestion product upon chromatofocusing. Form I, which was sequenced up to position 56, exhibited a very high degree of similarity with a Klebsiella oxytoca beta-lactamase. The determined sequence, which contained the active serine residue, demonstrated that the chromosome-encoded beta-lactamase of Citrobacter diversus belong to class A.

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 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 Acquisition of Beta-Lactamase by Neisseria meningitidis through Possible Horizontal Gene Transfer

2018 ◽  
Vol 62 (9) ◽  
Author(s):  
Eva Hong ◽  
Ala-Eddine Deghmane ◽  
Muhamed-Kheir Taha
Keyword(s):  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Genome Sequencing ◽  
Meningococcal Disease ◽  
Bacterial Species ◽  
Whole Genome ◽  
Beta Lactamase ◽  
Content Type ◽  
Beta Lactamases ◽  
Lactamase Gene

ABSTRACT We report the detection in France of a beta-lactamase-producing invasive meningococcal isolate. Whole-genome sequencing of the isolate revealed a ROB-1-type beta-lactamase gene that is frequently encountered in Haemophilus influenzae, suggesting horizontal transfer between isolates of these bacterial species. Beta-lactamases are exceptional in meningococci, with no reports for more than 2 decades. This report is worrying, as the expansion of such isolates may jeopardize the effective treatment against invasive meningococcal disease.

scholarly journals Molecular aspects of high-level resistance to sulbactam-cefoperazone in Klebsiella oxytoca clinical isolates.

1996 ◽  
Vol 40 (9) ◽  
pp. 1988-1994 ◽  
Author(s):  
K Kimura ◽  
Y Arakawa ◽  
S Ohsuka ◽  
H Ito ◽  
K Suzuki ◽  
...  
Keyword(s):  
Klebsiella Oxytoca ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Point Of View ◽  
Clinical Isolates ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Molecular Aspects ◽  
High Level ◽  
Level Resistance

Nine Klebsiella oxytoca strains which demonstrated resistance to the combination of sulbactam and cefoperazone were isolated from geographically separate hospitals in Japan in 1995. Among them, K. oxytoca SB23 showed high-level resistance to sulbactam-cefoperazone (MIC > 128 micrograms/ml) and aztreonam (MIC, 128 micrograms/ml). The sulbactam-cefoperazone resistance was not transferred from strain SB23 to Escherichia coli CSH2 by conjugation, beta-Lactamase RbiA, produced by strain SB23, was purified, and the molecular mass was estimated to be 29 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Kinetic parameters for RbiA revealed that cefoperazone and aztreonam were hydrolyzed efficiently by this enzyme. Moreover, ceftazidime and imipenem were also hydrolyzed weakly by RbiA, although strain SB23 did not show any resistance to these agents. Clavulanate, sulbactam, and tazobactam failed to block the hydrolysis of cefoperazone by RbiA. The structural gene of RbiA (blaRBI) was cloned and sequenced, and the deduced amino acid sequence of RbiA demonstrated high-level similarities to those of the beta-lactamases found in K. oxytoca D488, E23004, and plasmid-mediated MEN-1, which have been classified into Bush functional group 2be. Although RbiA demonstrates high-level molecular similarity to the enzymes in group 2be, from an enzymological point of view, this enzyme might be differentiated from the enzymes in that group. Hybridization analysis revealed that beta-lactamase genes highly similar to blaRBI were generally encoded on the chromosome of the sulbactam-cefoperazone-resistant clinical isolates of K. oxytoca tested in the study, despite their different derivations. This observation suggests that sulbactam-cefoperazone-resistant A. oxytoca strains which produce RbiA-type beta-lactamases have been proliferating in many hospitals in Japan.

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 Extended-spectrum beta-lactamases producing Escherichia coli and Klebsiella pneumoniaei: A Multi-centric Study Across Karnataka

2014 ◽  
Vol 6 (01) ◽  
pp. 007-013 ◽  
Author(s):  
Sridhar PN Rao ◽  
Prasad Subba Rama ◽  
Vishwanath Gurushanthappa ◽  
Radhakrishna Manipura ◽  
Krishna Srinivasan
Keyword(s):  
Escherichia Coli ◽  
Clinical Isolates ◽  
Beta Lactamase ◽  
Beta Lactam ◽  
Esbl Production ◽  
Beta Lactamases ◽  
E Coli ◽  
Karnataka State ◽  
Extended Spectrum Beta Lactamases ◽  
Esbl Producers

ABSTRACT Background: There are sporadic reports on detection of extended-spectrum beta-lactamases (ESBL) producers from Karnataka; hence, this is a first multicentric study across Karnataka state to determine the prevalence of ESBL production among clinical isolates of Escherichia coli and Klebsiella pneumoniaei. Aims and objectives: To determine the prevalence of ESBL producing clinical isolates of E. coli and K. pneumoniae from five geographically distributed centers across Karnataka, to study the susceptibility of ESBL producing isolates to other beta-lactam and beta-lactam-beta-lactamase inhibitors and to demonstrate transferability of plasmids coding for ESBL phenotype. Materials and Methods: Two hundred isolates of E. coli and K. pneumoniae each were collected from each of the five centers (Bellary, Dharwad, Davangere, Kolar and Mangalore). They were screened for resistance to screening agents (ceftazidime, cefotaxime, ceftriaxone, aztreonam) and positive isolates were confirmed for ESBL production by test described by Clinical and Laboratory Standards Institute . Co-production of ESBL and AmpC beta-lactamase was identified by using amino-phenylboronic acid disk method. Susceptibility of ESBL producers to beta-lactam antibiotics and beta-lactamase inhibitors was performed. Transferability of plasmids was performed by conjugation experiment. Results: Overall prevalence of ESBL production among E. coli and K. pneumoniae across five centers of the state was 57.5%. ESBL production was found to be 61.4% among E. coli and 46.2% among K. pneumoniae. ESBL production was significantly more among E. coli than K. pneumoniae. Significant variations in distribution of ESBL across the state was observed among E. coli isolates, but not among K. pneumoniae isolates. All ESBL producers demonstrated minimum inhibitory concentration levels ≥2 μg/ml towards cefotaxime, ceftazidime and ceftriaxone. Conclusion: Overall prevalence of ESBL production among clinical isolates of E. coli and K. pneumoniae across Karnataka state was high. The prevalence of ESBL production was significantly higher with E. coli than K. pneumoniae isolates. Higher rates of resistance to ceftriaxone and cefotaxime than to ceftazidime suggests the possibility of presence of CTX-M type ESBLs. Of all the beta-lactam/beta-lactamase inhibitor combinations tested, cefepime-tazobactam demonstrated highest in-vitro activity against ESBL producers. There was no statistical difference in the transferability of plasmids among E. coli and K. pneumoniae.

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