Biochemical and genetic characterization of the β-lactamases of Y. aldovae, Y. bercovieri, Y. frederiksenii and ‘Y. ruckeri’ strains

Schiefer, Andrea; Wiegand, Irith; Sherwood, Kimberley Jane; Wiedemann, B.; Stock, Ingo

doi:10.1016/j.ijantimicag.2004.08.020

Cited by 13 publications

(14 citation statements)

References 20 publications

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“…The band at 29 kDa corresponded to Bla-B (AmpC) as indicated by its specific inhibition with aztreonam. The molecular weight of inducible cephalosporinases or AmpC of other species namely Y. enterocolitica [32], Y. aldovae , Y. bercovieri, Y. ruckeri and Y. frederiksenii [15], and Serratia marcescens [33], has however been reported to be in the range of 34–40 kDa. The 29 kDa as found in the present study was similar to 29 kDa AmpC of Vibrio fischeri [34] and Y. enterocolitica biovar 1A [20].…”

Section: Resultsmentioning

confidence: 99%

“…This information has been inferred from MIC data of β-lactam antibiotics. Schiefer et al [15] recently characterized β-lactamases of Y. frederiksenii, Y. bercovieri, Y. aldovae and Y. ruckeri and reported that except for Y. frederiksenii , all expressed only an AmpC β-lactamase. Mammeri et al [16] cloned and sequenced the complete ampC gene of Y. ruckeri and found that it shared low level of identity with the known chromosomal and plasmid AmpC enzymes of closely related members, viz ., Enterobacter cloacae, E. aerogenes and Citrobacter freundii .…”

Section: Introductionmentioning

confidence: 99%

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Characteristics of β-lactamases and their genes (blaA and blaB) in Yersinia intermedia and Y. frederiksenii

et al. 2007

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Background: The presence of β-lactamases in Y. enterocolitica has been reported to vary with serovars, biovars and geographical origin of the isolates. An understanding of the β-lactamases in other related species is important for an overall perception of antibiotic resistance in yersiniae. The objective of this work was to study the characteristics of β-lactamases and their genes in strains of Y. intermedia and Y. frederiksenii, isolated from clinical and non-clinical sources in India.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characteristics of β-lactamases and their genes (blaA and blaB) in Yersinia intermedia and Y. frederiksenii

et al. 2007

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“…To detect plasmid-encoded AmpC enzymes in species that lack a chromosomally encoded AmpC ␤-lactamase, such as Klebsiella spp. and P. mirabilis, degenerated bla AmpC -specific primers were used (21). CMY family-specific primers were used for non-Citrobacter freundii strains, and PCR was carried out as described previously (8).…”

Section: Methodsmentioning

confidence: 99%

Detection of Extended-Spectrum Beta-Lactamases among Enterobacteriaceae by Use of Semiautomated Microbiology Systems and Manual Detection Procedures

et al. 2007

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Three commercially available microbiology identification and susceptibility testing systems were compared with regard to their ability to detect extended-spectrum ␤-lactamase (ESBL) production in Enterobacteriaceae, i.e., the Phoenix Automated Microbiology System (BD Diagnostic Systems, Sparks, MD), the VITEK 2 System (bioMérieux, Marcy l'Etoile, France), and the MicroScan WalkAway-96 System (Dade Behring, Inc., West Sacramento, CA), using routine testing panels. One hundred fifty putative ESBL producers were distributed blindly to three participating laboratories. Conventional phenotypic confirmatory tests such as the disk approximation method, the CLSI double-disk synergy test, and the Etest ESBL were also evaluated. Biochemical and molecular characterization of ␤-lactamases performed at an independent laboratory was used as the reference method. One hundred forty-seven isolates of Escherichia coli, Klebsiella pneumoniae, Klebsiella oxytoca, Enterobacter cloacae, Enterobacter aerogenes, Citrobacter freundii, Serratia marcescens, Proteus mirabilis, Proteus vulgaris, and Morganella morganii were investigated. Of these isolates, 85 were identified as ESBL producers by the reference method. The remaining isolates were identified as non-ESBL producers; they were either hyperproducers of their chromosomal AmpC, Koxy, or SHV enzymes or lacked any detectable ␤-lactamase activity. The system with the highest sensitivity for the detection of ESBLs was the Phoenix (99%), followed by the VITEK 2 (86%) and the MicroScan (84%); however, specificity was more variable, ranging from 52% (Phoenix) to 78% (VITEK 2). The performance of the semiautomated systems differed widely with the species investigated. The sensitivities of the conventional test methods ranged from 93 to 94%. The double-disk synergy test showed the highest specificity and positive predictive value among all test methods, i.e., 97% and 98%, respectively.In the Enterobacteriaceae, resistance to ␤-lactams is mainly due to ␤-lactamases that hydrolytically cleave the ␤-lactam ring, thus rendering the antibiotic inactive. A strategy to prevent hydrolysis caused by wide-spread ␤-lactamases, like the TEM-1 and SHV-1 enzymes, was the development of intrinsically stable ␤-lactams, such as the extended-spectrum cephalosporins. However, plasmid-encoded derivatives of these enzymes that show an enhanced spectrum of catalytic activity have been known since the early 1980s (7). Due to alterations at the active site caused by specific point mutations, these extended spectrum-␤-lactamases (ESBLs) are also able to hydrolyze oxyimino-␤-cephalosporins (e.g., cefotaxime, cefpodoxime, ceftazidime) and aztreonam (6). In addition to the large number of ESBL-TEM and -SHV variants, other plasmid-encoded ESBL such as CTX-M enzymes (http://www .lahey.org/studies/) are now frequently reported (13). The successful spread of ESBLs in a wide range of Enterobacteriaceae can be attributed to the fact that the genes coding for ESBLs are often located on self-transmissible or mobilizable broadh...

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“…1b). Sequence analysis of the blaB gene of Y. enterocolitica biovar 1A strain showed 96% nucleotide sequence identity with that of Y. enterocolitica 8081, biovar 1B and Y. enterocolitica IP97, biovar 2 (Seoane et al, 1992), and 88% with Y. bercovieri ATCC 43970 ampC gene (Schiefer et al, 2005), whereas sequence homology with other members of the genus Yersinia (Y. aldovae and Y. ruckeri) was relatively low (56-61%) (Schiefer et al, 2005). A previous investigation of Y. enterocolitica biovar 1A strains also suggested a lack of heterogeneity in Bla-B as identical expression of the enzyme was seen in all the strains by the double disc-diffusion test (Sharma et al, 2004).…”

Section: Pcr Amplification Rflp and Sequence Comparison Of Blabmentioning

confidence: 96%

Molecular characterization of Î²-lactamase genesblaAandblaBofYersinia enterocoliticabiovar 1A

Sharma

Mittal

Mallik

et al. 2006

FEMS Microbiology Letters

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The beta-lactamase genes blaA and blaB were detected by PCR amplification in strains of Yersinia enterocolitica biovar 1A isolated from India, Germany, France and the USA. Both genes were detected in all strains. Polymerase chain reaction-restriction fragment length polymorphism revealed genetic heterogeneity in blaA but not in blaB. Cluster analysis of blaA restriction profiles grouped the strains into three groups. The blaA gene of Y. enterocolitica biovar 1A showed a high degree of sequence homology to that of Y. enterocolitica 8081 (biovar 1B) and Y. enterocolitica Y-56 (biovar 4), whereas homology was low with class A beta-lactamase genes of other members of the family Enterobacteriaceae. The pI 8.7 of enzyme Bla-A of Y. enterocolitica biovar 1A was similar to that of biovars 2, 3 and 4. The enzyme Bla-B focused at 6.8 and 7.1, indicating that biovar 1A strains produced a 'B-like' enzyme. This is the first study to have investigated the genetic heterogeneity of the beta-lactamase genes of Y. enterocolitica.

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Biochemical and genetic characterization of the β-lactamases of Y. aldovae, Y. bercovieri, Y. frederiksenii and ‘Y. ruckeri’ strains

Cited by 13 publications

References 20 publications

Characteristics of β-lactamases and their genes (blaA and blaB) in Yersinia intermedia and Y. frederiksenii

Characteristics of β-lactamases and their genes (blaA and blaB) in Yersinia intermedia and Y. frederiksenii

Detection of Extended-Spectrum Beta-Lactamases among Enterobacteriaceae by Use of Semiautomated Microbiology Systems and Manual Detection Procedures

Molecular characterization of Î²-lactamase genesblaAandblaBofYersinia enterocoliticabiovar 1A

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