scholarly journals Multidrug-Resistant Pseudomonas aeruginosa Strain That Caused an Outbreak in a Neurosurgery Ward and Its aac(6′)-Iae Gene Cassette Encoding a Novel Aminoglycoside Acetyltransferase

2005 ◽  
Vol 49 (9) ◽  
pp. 3734-3742 ◽  
Author(s):  
Jun-ichiro Sekiguchi ◽  
Tsukasa Asagi ◽  
Tohru Miyoshi-Akiyama ◽  
Tomoko Fujino ◽  
Intetsu Kobayashi ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Resistance Gene ◽  
Gene Cassette ◽  
Multidrug Resistant ◽  
Aminoglycoside Resistance ◽  
Amino Acid Sequence Level ◽  
Class 1 Integron ◽  
Class 1 ◽  
Tract Infections

ABSTRACT We characterized multidrug-resistant Pseudomonas aeruginosa strains isolated from patients involved in an outbreak of catheter-associated urinary tract infections that occurred in a neurosurgery ward of a hospital in Sendai, Japan. Pulsed-field gel electrophoresis of SpeI-, XbaI-, or HpaI-digested genomic DNAs from the isolates revealed that clonal expansion of a P. aeruginosa strain designated IMCJ2.S1 had occurred in the ward. This strain possessed broad-spectrum resistance to aminoglycosides, β-lactams, fluoroquinolones, tetracyclines, sulfonamides, and chlorhexidine. Strain IMCJ2.S1 showed a level of resistance to some kinds of disinfectants similar to that of a control strain of P. aeruginosa, ATCC 27853. IMCJ2.S1 contained a novel class 1 integron, In113, in the chromosome but not on a plasmid. In113 contains an array of three gene cassettes of bla IMP-1, a novel aminoglycoside resistance gene, and the aadA1 gene. The aminoglycoside resistance gene, designated aac(6′)-Iae, encoded a 183-amino-acid protein that shared 57.1% identity with AAC(6′)-Iq. Recombinant AAC(6′)-Iae protein showed aminoglycoside 6′-N-acetyltransferase activity by thin-layer chromatography. Escherichia coli expressing exogenous aac(6′)-Iae showed resistance to amikacin, dibekacin, isepamicin, kanamycin, netilmicin, sisomicin, and tobramycin but not to arbekacin, gentamicins, or streptomycin. Alterations of gyrA and parC at the amino acid sequence level were detected in IMCJ2.S1, suggesting that such mutations confer the resistance to fluoroquinolones observed for this strain. These results indicate that P. aeruginosa IMCJ2.S1 has developed multidrug resistance by acquiring resistance determinants, including a novel member of the aac(6′)-I family and mutations in drug resistance genes.

scholarly journals Characterization of Class 1 Integrons from Pseudomonas aeruginosa That Contain the blaVIM-2Carbapenem-Hydrolyzing β-Lactamase Gene and of Two Novel Aminoglycoside Resistance Gene Cassettes

2001 ◽  
Vol 45 (2) ◽  
pp. 546-552 ◽  
Author(s):  
Laurent Poirel ◽  
Thierry Lambert ◽  
Salih Türkoglü ◽  
Esthel Ronco ◽  
Jean-Louis Gaillard ◽  
...  
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Resistance Gene ◽  
Gene Cassette ◽  
Amino Acid Sequences ◽  
Aminoglycoside Resistance ◽  
Class 1 Integron ◽  
Gene Cassettes ◽  
Class 1

ABSTRACT Two clonally unrelated Pseudomonas aeruginosa clinical strains, RON-1 and RON-2, were isolated in 1997 and 1998 from patients hospitalized in a suburb of Paris, France. Both isolates expressed the class B carbapenem-hydrolyzing β-lactamase VIM-2 previously identified in Marseilles in the French Riviera. In both isolates, thebla VIM-2 cassette was part of a class 1 integron that also encoded aminoglycoside-modifying enzymes. In one case, two novel aminoglycoside resistance gene cassettes,aacA29a and aacA29b, were located at the 5′ and 3′ end of the bla VIM-2 gene cassette, respectively. The aacA29a and aacA29b gene cassettes were fused upstream with a 101-bp part of the 5′ end of theqacE cassette. The deduced amino acid sequence AAC(6′)-29a protein shared 96% identity with AAC(6′)-29b but only 34% identity with the aacA7-encoded AAC(6′)-I1, the closest relative of the AAC(6′)-I family enzymes. These aminoglycoside acetyltransferases had amino acid sequences much shorter (131 amino acids) than the other AAC(6′)-I enzymes (144 to 153 amino acids). They conferred resistance to amikacin, isepamicin, kanamycin, and tobramycin but not to gentamicin, netilmicin, and sisomicin.

scholarly journals qnrVC-Like Gene Located in a Novel Complex Class 1 Integron Harboring the ISCR1 Element in an Aeromonas punctata Strain from an Aquatic Environment in Shandong Province, China

2010 ◽  
Vol 54 (8) ◽  
pp. 3471-3474 ◽  
Author(s):  
Ruirui Xia ◽  
Xianhu Guo ◽  
Yuzhen Zhang ◽  
Hai Xu
Keyword(s):  
Amino Acid ◽  
Gene Cassette ◽  
Multidrug Resistant ◽  
Amino Acid Identity ◽  
Complex Class ◽  
Class 1 Integron ◽  
Class 1 ◽  
Gyrase A ◽  
Ciprofloxacin Resistance ◽  
Novel Complex

ABSTRACT A qnrVC-like gene, qnrVC4, was found in a novel complex class 1 integron gene cassette array following the ISCR1 element and bla PER-1 in a multidrug-resistant strain of the aquatic bacterium Aeromonas punctata. The deduced QnrVC4 protein sequence shares 45% to 81% amino acid identity with quinolone resistance determinants QnrB6, QnrA1, QnrS1, QnrC, QnrVC1, and QnrVC3. A Ser-83 to Ile amino acid substitution in gyrase A may be mainly responsible for ciprofloxacin resistance in this strain.

scholarly journals Integron-Located oxa-32 Gene Cassette Encoding an Extended-Spectrum Variant of OXA-2 β-Lactamase from Pseudomonas aeruginosa

2002 ◽  
Vol 46 (2) ◽  
pp. 566-569 ◽  
Author(s):  
Laurent Poirel ◽  
Patrick Gerome ◽  
Christophe De Champs ◽  
Jean Stephanazzi ◽  
Thierry Naas ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Substitution ◽  
Gene Cassette ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Class 1 Integron ◽  
Class D ◽  
Class 1

ABSTRACT Pseudomonas aeruginosa clinical isolate CY-1, which was resistant to ceftazidime, harbored a conjugative ca. 250-kb plasmid that contained a class 1 integron with two gene cassettes encoding OXA-32, an OXA-2- type β-lactamase, and the aminoglycoside acetyltransferase AAC(6′)Ib9. OXA-32 differed from OXA-2 by an Leu169Ile amino acid substitution (class D numbering). Site-directed mutagenesis established that Ile169 is responsible for resistance to ceftazidime but not to cefotaxime.

scholarly journals AAC(6′)-Iaf, a Novel Aminoglycoside 6′-N-Acetyltransferase from Multidrug-Resistant Pseudomonas aeruginosa Clinical Isolates

2009 ◽  
Vol 53 (6) ◽  
pp. 2327-2334 ◽  
Author(s):  
Tomoe Kitao ◽  
Tohru Miyoshi-Akiyama ◽  
Teruo Kirikae
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Decubitus Ulcer ◽  
Multidrug Resistant ◽  
Clinical Isolates ◽  
Upstream Region ◽  
Aminoglycoside Resistance ◽  
Class 1 Integron ◽  
Class 1 ◽  
Layer Chromatography

ABSTRACT We report here the characterization of a novel aminoglycoside resistance gene, aac(6′)-Iaf, present in two multidrug-resistant (MDR) Pseudomonas aeruginosa clinical isolates. These isolates, IMCJ798 and IMCJ799, were independently obtained from two patients, one with a urinary tract infection and the other with a decubitus ulcer, in a hospital located in the western part of Japan. Although the antibiotic resistance profiles of IMCJ798 and IMCJ799 were similar to that of MDR P. aeruginosa IMCJ2.S1, which caused outbreaks in the eastern part of Japan, the pulsed-field gel electrophoresis patterns for these isolates were different from that for IMCJ2.S1. Both IMCJ798 and IMCJ799 were found to contain a novel chromosomal class 1 integron, In123, which included aac(6′)-Iaf as the first cassette gene. The encoded protein, AAC(6′)-Iaf, was found to consist of 183 amino acids, with 91 and 87% identity to AAC(6′)-Iq and AAC(6′)-Im, respectively. IMCJ798, IMCJ799, and Escherichia coli transformants carrying a plasmid containing the aac(6′)-Iaf gene and its upstream region were highly resistant to amikacin, dibekacin, and kanamycin but not to gentamicin. The production of AAC(6′)-Iaf in these strains was confirmed by Western blot analysis. Thin-layer chromatography indicated that AAC(6′)-Iaf is a functional acetyltransferase that specifically modifies the amino groups at the 6′ positions of aminoglycosides. Collectively, these findings indicate that AAC(6′)-Iaf contributes to aminoglycoside resistance.

scholarly journals OXA-28, an Extended-Spectrum Variant of OXA-10 β-Lactamase from Pseudomonas aeruginosa and Its Plasmid- and Integron-Located Gene

2001 ◽  
Vol 45 (2) ◽  
pp. 447-453 ◽  
Author(s):  
Laurent Poirel ◽  
Delphine Girlich ◽  
Thierry Naas ◽  
Patrice Nordmann
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Variable Region ◽  
Gene Cassette ◽  
Cloning And Expression ◽  
Marginal Effect ◽  
Class 1 Integron ◽  
E Coli ◽  
Class 1 ◽  
Lactamase Gene

ABSTRACT Pseudomonas aeruginosa ED-1, isolated from a pulmonary brush of a patient hospitalized in a suburb of Paris, France, was resistant to ceftazidime and of intermediate susceptibility to ureidopenicillins and to cefotaxime. Cloning and expression of the β-lactamase gene content of this isolate in Escherichia coli DH10B identified a novel OXA-10 variant, OXA-28, with a pI value of 8.1 and a molecular mass of 29 kDa. It differed from OXA-10 by 10 amino acid changes and from OXA-13 and OXA-19 by 2 amino acid changes, including a glycine instead of tryptophan at position 164, which is likely involved in its resistance to ceftazidime. Like OXA-11, -14, -16, and -19 and as opposed to OXA-17, OXA-28 predominantly compromised ceftazidime and had only marginal effect on the MICs of aztreonam and cefotaxime in P. aeruginosa. Once expressed in E. coli, OXA-28 raised the MIC of ceftazidime to a much higher level than those of amoxicillin, cephalothin, and cefotaxime (128, 16, 8, and 4 μg/ml, respectively). OXA-28 β-lactamase had a broad spectrum of activity, including ceftazidime. Its activity was partially antagonized by clavulanic acid (50% inhibitory concentration, 10 μM) and NaCl addition. The oxa28 gene cassette was inserted in the variable region of a class 1 integron, In57, immediately downstream of an amino 6′-N-acetyltransferase gene cassette,aac(6′)Ib. The structures of the integrons carrying eitheroxa28, oxa13, or oxa19 gene cassettes were almost identical, suggesting that they may have derived from a common ancestor as a result of the common European origin of theP. aeruginosa isolates. In57 was located on a self-transferable plasmid of ca. 150 kb that was transferred fromP. aeruginosa to P. aeruginosa.

scholarly journals Characterization of a Novel Plasmid-Mediated Cephalosporinase (CMY-9) and Its Genetic Environment in an Escherichia coli Clinical Isolate

2002 ◽  
Vol 46 (8) ◽  
pp. 2427-2434 ◽  
Author(s):  
Yohei Doi ◽  
Naohiro Shibata ◽  
Keigo Shibayama ◽  
Kazunari Kamachi ◽  
Hiroshi Kurokawa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gene Cassette ◽  
Single Amino Acid ◽  
Common Region ◽  
Class 1 Integron ◽  
Class 1 ◽  
The Common ◽  
High Level

ABSTRACT An Escherichia coli strain, HKYM68, which showed resistance to broad-spectrum cephalosporins was isolated from a sputum specimen in Japan. The high-level resistance of the strain to ceftazidime, cefpirome, and moxalactam was carried by a self-transferable plasmid. The β-lactamase gene responsible for the resistance was cloned and sequenced. The deduced amino acid sequence of this gene product, CMY-9, had a single amino acid substitution (E85D), the residue reported to be part of the recognition site for the R1 side chain of β-lactams, compared with the amino acid sequence of CMY-8 and also had 78% identity with the amino acid sequence of CepH, a chromosomal cephalosporinase of Aeromonas hydrophila. A sul1-type class 1 integron containing an aacA1-orfG gene cassette was identified upstream of bla CMY-9 and ended with a truncated 3′ conserved segment. The following 2.1 kb was almost identical to the common region of integrons In6 and In7 and the integron of pSAL-1, except that orf513 encoding a putative transposase was identified instead of orf341 due to addition of a single nucleotide. bla CMY-9 was closely located downstream of the end of the common region. These observations are indicative of the exogenous derivation of bla CMY-9 from some environmental microorganisms such as aeromonads.

scholarly journals A Predominant Multidrug-Resistant Salmonella enterica Serovar Saintpaul Clonal Line in German Turkey and Related Food Products

2010 ◽  
Vol 76 (11) ◽  
pp. 3657-3667 ◽  
Author(s):  
Janine Beutlich ◽  
Irene Rodr�guez ◽  
Andreas Schroeter ◽  
Annemarie K�sbohrer ◽  
Reiner Helmuth ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Food Products ◽  
Gene Cassette ◽  
Multidrug Resistant ◽  
Resistance Pattern ◽  
Clonal Line ◽  
Class 1 Integron ◽  
Pathogenic Potential ◽  
Class 1 ◽  
Plasmid Profiling

ABSTRACT Recently, Salmonella enterica subsp. enterica serovar Saintpaul has increasingly been observed in several countries, including Germany. However, the pathogenic potential and epidemiology of this serovar are not very well known. This study describes biological attributes of S. Saintpaul isolates obtained from turkeys in Germany based on characterization of their pheno- and genotypic properties. Fifty-five S. Saintpaul isolates from German turkeys and turkey-derived food products isolated from 2000 to 2007 were analyzed by using antimicrobial agent, organic solvent, and disinfectant susceptibility tests, isoelectric focusing, detection of resistance determinants, plasmid profiling, pulsed-field gel electrophoresis (PFGE), and hybridization experiments. These isolates were compared to an outgroup consisting of 24 S. Saintpaul isolates obtained from humans and chickens in Germany and from poultry and poultry products (including turkeys) in Netherlands. A common core resistance pattern was detected for 27 German turkey and turkey product isolates. This pattern included resistance (full or intermediate) to ampicillin, amoxicillin-clavulanic acid, gentamicin, kanamycin, nalidixic acid, streptomycin, spectinomycin, and sulfamethoxazole and intermediate resistance or decreased susceptibility to ciprofloxacin (MIC, 2 or 1 μg/ml, respectively) and several third-generation cephalosporins (including ceftiofur and cefoxitin [MIC, 4 to 2 and 16 to 2 μg/ml, respectively]). These isolates had the same core resistance genotype, with bla TEM-1, aadB, aadA2, sul1, a Ser83→Glu83 mutation in the gyrA gene, and a chromosomal class 1 integron carrying the aadB-aadA2 gene cassette. Their XbaI, BlnI, and combined XbaI-BlnI PFGE patterns revealed levels of genetic similarity of 93, 75, and 90%, respectively. This study revealed that a multiresistant S. Saintpaul clonal line is widespread in turkeys and turkey products in Germany and was also detected among German human fecal and Dutch poultry isolates.

scholarly journals In99, an In100-related integron, its occurrence and prevalence in clinical Pseudomonas aeruginosa strains from a central region of Portugal

2006 ◽  
Vol 135 (3) ◽  
pp. 502-504 ◽  
Author(s):  
T. CAETANO ◽  
S. FERREIRA ◽  
A. P. MONDEGO ◽  
A. CORREIA ◽  
S. MENDO
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Resistance Genes ◽  
Central Region ◽  
Clinical Isolates ◽  
Aminoglycoside Resistance ◽  
Class 1 Integron ◽  
Class 1 ◽  
Aminoglycoside Resistance Genes

In99, a possible ancestor of In100, is a class 1 integron associated with carbenicillinase (blaPSE) and aminoglycoside resistance genes [aac(6′)-Ib and aadA2]. In99 was present in 8 of 81 clinical isolates of Pseudomonas aeruginosa from unrelated patients collected in different years. The strains fell into two clonal groups and exhibited resistance to β-lactams and aminoglycosides.

scholarly journals Class 1 Integron-Associated Tobramycin-Gentamicin Resistance in Campylobacter jejuni Isolated from the Broiler Chicken House Environment

2002 ◽  
Vol 46 (11) ◽  
pp. 3660-3664 ◽  
Author(s):  
Margie D. Lee ◽  
Susan Sanchez ◽  
Martha Zimmer ◽  
Umelaalim Idris ◽  
Mark E. Berrang ◽  
...  
Keyword(s):  
Resistance Gene ◽  
Campylobacter Jejuni ◽  
Broiler Chicken ◽  
Aminoglycoside Resistance ◽  
Class 1 Integron ◽  
Integrase Gene ◽  
Conserved Sequence ◽  
Chicken House ◽  
Class 1 ◽  
Gentamicin Resistance

ABSTRACT Using PCR, we screened 105 isolates of poultry-associated Campylobacter jejuni for the presence of class 1 integrons. Of those isolates, 21% (22 of 105) possessed the integrase gene, but only 5 isolates produced an amplicon in a 5′-3′ conserved sequence PCR directed toward amplification of the resistance cassettes. DNA sequencing demonstrated that all five isolates possessed the aminoglycoside resistance gene, aacA4.

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