Identification of a Chromosome-Borne Expanded-Spectrum Class A β-Lactamase from
            <i>Erwinia persicina</i>

Vimont, Sophie; Poirel, Laurent; Naas, Thierry; Nordmann, Patrice

doi:10.1128/aac.46.11.3401-3405.2002

Cited by 19 publications

(16 citation statements)

References 30 publications

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“…In fact, PLA-1 had stronger hydrolytic activity than TEM-1 not only against penicillins but also against cephalosporins, including the extended-spectrum cephalosporins, and aztreonam (21). The catalytic efficiency of PLA-1 against cefotaxime was similar to the efficiencies observed for the chromosomal ␤-lactamases of Proteus penneri (16), Rahnella aquatilis (3), and E. persicina (35), whereas the efficiency against cefepime, which was rarely tested in the previous studies, was significantly higher than that observed for R. aquatilis (3) and resembled that displayed by plasmid-mediated CTX-M type ␤-lactamases such as CTX-M-18 (30). As the extended substrate profile of class A ␤-lactamases has previously been shown to be related to specific amino acid residues at defined positions, we analyzed the protein sequences of the ␤-lactamases of Raoutella spp.…”

Section: Discussionsupporting

confidence: 48%

Genetic and Biochemical Characterization of the Chromosomal Class A β-Lactamases of Raoultella (formerly Klebsiella ) planticola and Raoultella ornithinolytica

Estelle

Poirel

Leflon‐Guibout

et al. 2004

Antimicrob Agents Chemother

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Enterobacterial strains of Raoultella spp. display a penicillinase-related ␤-lactam resistance pattern suggesting the presence of a chromosomal bla gene. From whole-cell DNA of Raoultella planticola strain ATCC 33531 T and Raoultella ornithinolytica strain ATCC 31898 T , bla genes were cloned and expressed into Escherichia coli. Each gene encoded an Ambler class A ␤-lactamase, named PLA-1 and ORN-1 for R. planticola and R. ornithinolytica, respectively. These ␤-lactamases (291 amino acids), with the same pI value of 7.8, had a shared amino acid identity of 94%, 37 to 47% identity with the majority of the chromosome-encoded class A ␤-lactamases previously described for Enterobacteriaceae, and 66 to 69% identity with the two ␤-lactamases LEN-1 and SHV-1 from Klebsiella pneumoniae. However, the highest identity percentage (69 to 71%) was found with the plasmid-mediated ␤-lactamase TEM-1. PLA-1, which displayed very strong hydrolytic activity against penicillins, also displayed significant hydrolytic activity against cefepime and, to a lesser extent, against cefotaxime and aztreonam, but there was no hydrolytic activity against ceftazidime. Such a substrate profile suggests that the Raoultella ␤-lactamases PLA-1 and ORN-1 should be classified into the group 2be of the ␤-lactamase classification of K. Bush, G. A. Jacoby, and A. A. Medeiros (Antimicrob. Agents Chemother. 39:1211-1233, 1995). The highly homologous regions upstream of the bla PLA-1A and bla ORN-1A genes comprised a nucleotide sequence identical to the ؊35 region and another one very close to the ؊10 region of the bla LEN-1 gene. From now on, as the bla gene sequences of the most frequent Raoultella and Klebsiella species are available, the bla gene amplification method can be used to differentiate these species from each other, which the biochemical tests currently carried out in the clinical laboratory are unable to do.Klebsiella planticola and Klebsiella terrigena were identified in 1981, and Klebsiella ornithinolytica was identified in 1989 (2, 12, 32). The first two species were primarily associated with botanical and aquatic environments, whereas the third one, which was formerly known as ornithine-positive Klebsiella oxytoca, was first identified from clinical samples (2, 12, 32). The differentiation of these three species from the other Klebsiella species was based on biochemical reactions, growth temperatures, pigment production, GϩC content, and DNA-DNA hybridization (2, 12, 32). However, these three species have recently been reclassified in a new genus, the Raoultella genus, on the basis of the 16S rDNA and rpoB gene sequence analysis of enteric bacteria (8,19). In spite of this phylogenetic advance, the routine biochemical tests used in the clinical laboratory are not capable of distinguishing between Klebsiella spp., particularly K. oxytoca, and Raoutella spp. To demonstrate the involvement of Raoultella spp. in infectious diseases, the use of particular methods was required. Thus, by using particular biochemical tests and differential grow...

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Section: Discussionsupporting

confidence: 48%

Genetic and Biochemical Characterization of the Chromosomal Class A β-Lactamases of Raoultella (formerly Klebsiella ) planticola and Raoultella ornithinolytica

Estelle

Poirel

Leflon‐Guibout

et al. 2004

Antimicrob Agents Chemother

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“…The tiny ESBL2 cluster comprises three representative enzymes (ERP-1, DES-1, and BES-1) and a single putative enzyme (Desulfovibrio desulfuricans). ERP-1 (from Erwinia persicina) was the first enterobacterial extended-spectrum ␤-lactamase to be shown to be pathogenic to plants (37). The kinetic parameters of the ERP-1 enzyme place it in group 2be (Table 1).…”

Section: Toca P Vulgaris R Aquatilis and S Fonticola)mentioning

confidence: 99%

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

Slama²,

et al. 2016

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SUMMARYFor medical biologists, sequencing has become a commonplace technique to support diagnosis. Rapid changes in this field have led to the generation of large amounts of data, which are not always correctly listed in databases. This is particularly true for data concerning class A β-lactamases, a group of key antibiotic resistance enzymes produced by bacteria. Many genomes have been reported to contain putative β-lactamase genes, which can be compared with representative types. We analyzed several hundred amino acid sequences of class A β-lactamase enzymes for phylogenic relationships, the presence of specific residues, and cluster patterns. A clear distinction was first made between dd-peptidases and class A enzymes based on a small number of residues (S70, K73, P107, 130SDN132, G144, E166, 234K/R, 235T/S, and 236G [Ambler numbering]). Other residues clearly separated two main branches, which we named subclasses A1 and A2. Various clusters were identified on the major branch (subclass A1) on the basis of signature residues associated with catalytic properties (e.g., limited-spectrum β-lactamases, extended-spectrum β-lactamases, and carbapenemases). For subclass A2 enzymes (e.g., CfxA, CIA-1, CME-1, PER-1, and VEB-1), 43 conserved residues were characterized, and several significant insertions were detected. This diversity in the amino acid sequences of β-lactamases must be taken into account to ensure that new enzymes are accurately identified. However, with the exception of PER types, this diversity is poorly represented in existing X-ray crystallographic data.

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“…As observed in TEM-1, TEM-2, LEN-1, OXY-1, and OXY-2 ␤-lactamases, an Ala residue was found in position 237. On the other hand, some TEM-type and SHV-type extended-spectrum ␤-lactamases, CTX-M variants, and chromosome-encoded enzymes of Kluyvera ascorbata (KLUA-1), Kluyvera cryocrescens (KLUC-1), Kluyvera georgiana (KLUG-1), P. vulgaris (RO104), S. fonticola (CUV), C. sedlakii (Sed-1), Citrobacter diversus (CdiA), R. aquatilis (RHAN-1), and Erwinia persinica (ERP-1) possess a Ser residue in this position, which is involved in extended activity towards cefuroxime and extended-broad-spectrum cephalosporins (2,9,12,19,20,21,23,28). Moreover, HER-1 possess two cysteines in positions 77 and 123 as in TEM and SHV ␤-lactamases and as in few others; a disulfide bridge is also likely to be present in the E. hermannii ␤-lactamase.…”

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confidence: 99%

Molecular and Biochemical Characterization of a Novel Class A β-Lactamase (HER-1) from Escherichia hermannii

Beauchef-Havard

Arlet

Gautier³

et al. 2003

Antimicrob Agents Chemother

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Escherichia hermannii showed a low level of resistance to amoxicillin and ticarcillin, reversed by clavulanate, and a moderate susceptibility to piperacillin but was susceptible to all cephalosporins. A bla gene was cloned and encoded a typical class A ␤-lactamase (HER-1, pI 7.5), which shares 45, 44, 41, and 40% amino acid identity with other ␤-lactamases, AER-1 from Aeromonas hydrophila, MAL-1/Cko-1 from Citrobacter koseri, and TEM-1 and LEN-1, respectively. No ampR gene was detected. Only penicillins were efficiently hydrolyzed, and no hydrolysis was observed for cefuroxime and broad-spectrum cephalosporins. Sequencing of the bla gene in 12 other strains showed 98 to 100% identity with bla HER-1 .

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Identification of a Chromosome-Borne Expanded-Spectrum Class A β-Lactamase from Erwinia persicina

Cited by 19 publications

References 30 publications

Genetic and Biochemical Characterization of the Chromosomal Class A β-Lactamases of Raoultella (formerly Klebsiella ) planticola and Raoultella ornithinolytica

Genetic and Biochemical Characterization of the Chromosomal Class A β-Lactamases of Raoultella (formerly Klebsiella ) planticola and Raoultella ornithinolytica

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

Molecular and Biochemical Characterization of a Novel Class A β-Lactamase (HER-1) from Escherichia hermannii

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