scholarly journals Biochemical-Genetic Characterization and Distribution of OXA-22, a Chromosomal and Inducible Class D β-Lactamase fromRalstonia (Pseudomonas)pickettii

2000 ◽  
Vol 44 (8) ◽  
pp. 2201-2204 ◽  
Author(s):  
Patrice Nordmann ◽  
Laurent Poirel ◽  
Maryline Kubina ◽  
Anne Casetta ◽  
Thierry Naas
Keyword(s):  
Amino Acid ◽  
Genomic Dna ◽  
Genetic Characterization ◽  
Amino Acid Identity ◽  
Clinical Isolates ◽  
Acid Identity ◽  
Ralstonia Pickettii ◽  
Class D ◽  
Biochemical Genetic ◽  
Lactamase Gene

ABSTRACT From genomic DNA of Ralstonia pickettii isolate PIC-1, a β-lactamase gene was cloned that encodes the oxacillinase OXA-22. It differs from known oxacillinases, being most closely related to OXA-9 (38% amino acid identity). The hydrolytic spectrum of OXA-22 is limited mostly to benzylpenicillin, cloxacillin, and restricted-spectrum cephalosporins. OXA-22-like genes were identified as single chromosomal copies in five other R. pickettii clinical isolates. The expression of OXA-22-like β-lactamases was inducible in R. pickettii.

scholarly journals Chromosome-Encoded Ambler Class D β-Lactamase of Shewanella oneidensis as a Progenitor of Carbapenem-Hydrolyzing Oxacillinase

2004 ◽  
Vol 48 (1) ◽  
pp. 348-351 ◽  
Author(s):  
Laurent Poirel ◽  
Claire Héritier ◽  
Patrice Nordmann
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Reference Strain ◽  
Shewanella Oneidensis ◽  
Amino Acid Identity ◽  
Gram Negative ◽  
Acid Identity ◽  
Class D ◽  
Lactamase Gene

ABSTRACT A chromosome-encoded β-lactamase gene from a Shewanella oneidensis reference strain was cloned and expressed in Escherichia coli. It encoded a carbapenem-hydrolyzing Ambler class D β-lactamase, OXA-54, that shared 92% amino acid identity with the plasmid-encoded carbapenem-hydrolyzing oxacillinase OXA-48 from Klebsiella pneumoniae. This work suggests that Shewanella spp. may produce the progenitor of oxacillinases compromising the efficacy of imipenem in clinically relevant gram-negative pathogens.

scholarly journals OXA-60, a Chromosomal, Inducible, and Imipenem-Hydrolyzing Class D β-Lactamase from Ralstonia pickettii

2004 ◽  
Vol 48 (11) ◽  
pp. 4217-4225 ◽  
Author(s):  
Delphine Girlich ◽  
Thierry Naas ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Genetic Background ◽  
Amino Acid Identity ◽  
Gene Inactivation ◽  
Acid Identity ◽  
Resistance Profile ◽  
Ralstonia Pickettii ◽  
Narrow Spectrum ◽  
Relative Contribution ◽  
Class D

ABSTRACT A chromosomally encoded oxacillinase, OXA-22, had been characterized from Ralstonia pickettii PIC-1 that did not explain by itself the resistance profile of this strain to β-lactams. Thus, further analysis of the genetic background of this species led to the identification of another oxacillinase, OXA-60, that was expressed only after β-lactam induction. This chromosomally encoded oxacillinase shared 19% amino acid identity with OXA-22. It has a narrow-spectrum hydrolysis profile that includes imipenem. OXA-60-like enzymes were identified in several R. pickettii strains. Gene inactivation and induction studies of the bla OXA-60 and bla OXA-22 genes in R. pickettii identified the relative contribution of each oxacillinase to the resistance profile of R. pickettii to β-lactams.

scholarly journals Molecular Characterization of OXA-20, a Novel Class D β-Lactamase, and Its Integron from Pseudomonas aeruginosa

1998 ◽  
Vol 42 (8) ◽  
pp. 2074-2083 ◽  
Author(s):  
Thierry Naas ◽  
Wladimir Sougakoff ◽  
Anne Casetta ◽  
Patrice Nordmann
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Clavulanic Acid ◽  
Antibiotic Resistance Gene ◽  
Amino Acid Identity ◽  
Acid Identity ◽  
Class D ◽  
Acid Protein ◽  
Amino Acid Protein

ABSTRACT The Pseudomonas aeruginosa Mus clinical isolate produces OXA-18, a pI 5.5 class D extended-spectrum β-lactamase totally inhibited by clavulanic acid (L. N. Philippon, T. Naas, A.-T. Bouthors, V. Barakett, and P. Nordmann, Antimicrob. Agents Chemother. 41:2188–2195, 1997). A second β-lactamase was cloned, and the recombinant Escherichia coli clone pPL10 expressed a pI 7.4 β-lactamase which conferred high levels of amoxicillin and ticarcillin resistance and which was partially inhibited by clavulanic acid. The 2.5-kb insert from pPL10 was sequenced, and a 266-amino-acid protein (OXA-20) was deduced; this protein has low amino acid identity with most of the class D β-lactamases except OXA-2, OXA-15, and OXA-3 (75% amino acid identity with each). OXA-20 is a restricted-spectrum oxacillinase and is unusually inhibited by clavulanic acid. OXA-20 is a peculiar β-lactamase because its translation initiates with a TTG (leucine) codon, which is rarely used as a translational origin in bacteria. Exploration of the genetic environment of oxa20revealed the presence of the following integron features: (i) a second antibiotic resistance gene, aacA4; (ii) anintI1 gene; and (iii) two 59-base elements, each associated with either oxa20 or aacA4. This integron is peculiar because it lacks the 3′ conserved region, and therefore is not a sul1-associated integron like most of them, and because its 3′ end is located within tnpR, a gene involved in the transposition of Tn5393, a gram-negative transposon.P. aeruginosa Mus produces two novel and unrelated oxacillinases, OXA-18 and OXA-20, both of which are inhibited by clavulanic acid.

scholarly journals Characterization of a Naturally Occurring Class D β-Lactamase from Achromobacter xylosoxidans

2008 ◽  
Vol 52 (6) ◽  
pp. 1952-1956 ◽  
Author(s):  
Yohei Doi ◽  
Laurent Poirel ◽  
David L. Paterson ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Amino Acid Identity ◽  
Burkholderia Cenocepacia ◽  
Achromobacter Xylosoxidans ◽  
Acid Identity ◽  
Low Level ◽  
Narrow Spectrum ◽  
Naturally Occurring ◽  
Class D

ABSTRACT A chromosomally encoded class D β-lactamase, OXA-114, was characterized from Achromobacter xylosoxidans strain CIP69598. β-Lactamase OXA-114 shared 56% amino acid identity with the naturally occurring class D β-lactamase of Burkholderia cenocepacia and 42% identity with the acquired oxacillinases OXA-9 and OXA-18. OXA-114 has a narrow-spectrum hydrolysis profile, although it includes imipenem, at a very low level. PCR and sequencing revealed that bla OXA-114-like genes were identified in all A. xylosoxidans strains tested (n = 5), indicating that this β-lactamase is naturally occurring in that species. Induction experiments with imipenem and cefoxitin did not show inducibility of bla OXA-114 expression.

scholarly journals Association of the Extended-Spectrum β-Lactamase Gene blaTLA-1 with a Novel ISCR Element, ISCR20

2010 ◽  
Vol 54 (9) ◽  
pp. 4026-4028 ◽  
Author(s):  
Beatrice Berçot ◽  
Laurent Poirel ◽  
Jesus Silva-Sanchez ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Mexico City ◽  
Insertion Sequence ◽  
Amino Acid Identity ◽  
Gene Encoding ◽  
Acid Identity ◽  
Promoter Sequences ◽  
Extended Spectrum ◽  
Lactamase Gene

ABSTRACT The bla TLA-1 gene encoding an extended-spectrum β-lactamase was identified in 11 enterobacterial isolates from Mexico City, Mexico. This gene was located on different plasmids and plasmid types with different sizes and incompatibility groups. It was associated with a novel insertion sequence, ISCR20, encoding a putative transposase that shared only 20% amino acid identity with the most closely related transposase of ISCR1. The ISCR20 element provided specific promoter sequences for expression of the bla TLA-1 gene.

scholarly journals Genetic Characterization of Resistance to Extended-Spectrum β-Lactams in Klebsiella oxytoca Isolates Recovered from Patients with Septicemia at Hospitals in the Stockholm Area

1999 ◽  
Vol 43 (5) ◽  
pp. 1294-1297 ◽  
Author(s):  
Shang Wei Wu ◽  
Kathrine Dornbusch ◽  
Göran Kronvall
Keyword(s):  
Amino Acid ◽  
Dna Sequencing ◽  
Amino Acid Residue ◽  
Genetic Characterization ◽  
Consensus Sequence ◽  
Klebsiella Oxytoca ◽  
Clinical Isolates ◽  
Amino Acid Residues ◽  
Lactamase Gene

ABSTRACT Two β-lactamase gene regions were characterized by DNA sequencing in eight clinical isolates of Klebsiella oxytoca. Thebla OXY-2a region encoded a β-lactamase nearly identical to OXY-2 (one amino acid residue substituted) and conferred aztreonam and cefuroxime resistance on the K. oxytoca isolates. Overproduction of OXY-2a was caused by a G-to-A substitution of the fifth nucleotide in the −10 consensus sequence ofbla OXY-2a. Thebla OXY-1a was identified in a susceptible strain, and the OXY-1a enzyme differed from OXY-1 by two amino acid residues.

scholarly journals Chromosome-Encoded Ambler Class A β-Lactamase of Kluyvera georgiana, a Probable Progenitor of a Subgroup of CTX-M Extended-Spectrum β-Lactamases

2002 ◽  
Vol 46 (12) ◽  
pp. 4038-4040 ◽  
Author(s):  
Laurent Poirel ◽  
Peter Kämpfer ◽  
Patrice Nordmann
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Reference Strain ◽  
Amino Acid Identity ◽  
Acid Identity ◽  
Class A ◽  
Extended Spectrum ◽  
Lactamase Gene

ABSTRACT A chromosome-encoded β-lactamase gene, cloned and expressed in Escherichia coli from Kluyvera georgiana reference strain CUETM 4246-74 (DSM 9408), encoded the extended-spectrum β-lactamase KLUG-1, which shared 99% amino acid identity with the plasmid-mediated β-lactamase CTX-M-8. This work provides further evidence that Kluyvera spp. may be the progenitor(s) of CTX-M-type β-lactamases.

scholarly journals Oxacillinase-Mediated Resistance to Cefepime and Susceptibility to Ceftazidime in Pseudomonas aeruginosa

2001 ◽  
Vol 45 (6) ◽  
pp. 1615-1620 ◽  
Author(s):  
Daniel Aubert ◽  
Laurent Poirel ◽  
Jacqueline Chevalier ◽  
Sophie Leotard ◽  
Jean-Marie Pages ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Identity ◽  
Class 1 Integron ◽  
Acid Identity ◽  
Resistance Phenotype ◽  
Class D ◽  
Class 1 ◽  
Efflux Mechanism

ABSTRACT Pseudomonas aeruginosa clinical isolate SOF-1 was resistant to cefepime and susceptible to ceftazidime. This resistance phenotype was explained by the expression of OXA-31, which shared 98% amino acid identity with a class D β-lactamase, OXA-1. Theoxa-31 gene was located on a ca. 300-kb nonconjugative plasmid and on a class 1 integron. No additional efflux mechanism for cefepime was detected in P. aeruginosa SOF-1. Resistance to cefepime and susceptibility to ceftazidime in P. aeruginosawere conferred by OXA-1 as well.

scholarly journals Heterogeneity of AmpC Cephalosporinases ofHafnia alvei Clinical Isolates Expressing Inducible or Constitutive Ceftazidime Resistance Phenotypes

2000 ◽  
Vol 44 (11) ◽  
pp. 3220-3223 ◽  
Author(s):  
Delphine Girlich ◽  
Thierry Naas ◽  
Samuel Bellais ◽  
Laurent Poirel ◽  
Amal Karim ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Identity ◽  
Clinical Isolates ◽  
Hafnia Alvei ◽  
Acid Identity ◽  
Genetic Environment ◽  
Low Level ◽  
High Level

ABSTRACT Ten unrelated Hafnia alvei clinical isolates were grouped according to either their low-level and inducible cephalosporinase production or their high-level and constitutive cephalosporinase production phenotype. Their AmpC sequences shared 85 to 100% amino acid identity. The immediate genetic environment ofampC genes was conserved in H. alvei isolates but was different from that found in other ampC-possessing enterobacterial species.

scholarly journals Analysis of rodent platelet glycoprotein IIb: evidence for evolutionarily conserved domains and alternative proteolytic processing

Blood ◽  
1990 ◽  
Vol 75 (6) ◽  
pp. 1282-1289 ◽  
Author(s):  
M Poncz ◽  
PJ Newman
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Dna Sequence ◽  
Genomic Dna ◽  
Amino Acid Identity ◽  
Dna Sequence Analysis ◽  
Amino Acid Residues ◽  
Acid Identity ◽  
Heavy Chains ◽  
Genomic Dna Sequence

Abstract Recently, the full-length primary amino acid sequence for human glycoproteins (GP) IIb and IIIa have been derived from their respective cDNAs. Potential functional domains within these proteins have been proposed based primarily on homology with similar domains in other proteins having known biologic function. To further understand the relationship between structure and function of the platelet fibrinogen receptor, we have begun comparative studies of the human GPIIb/IIIa receptor with the corresponding rodent receptor. The rodent rGPIIb/IIIa receptor differs from the human receptor, having low affinity for R.G.D- containing oligopeptides and not binding at all to the C-terminus of the gamma chain of human fibrinogen. We describe the structure of rodent platelet GPIIb derived from a combination of peptide sequencing, and cDNA and partial genomic DNA sequence analysis. The initial transcript is 1037 amino acid residues, having 78% amino acid identity with its 1039 residue human analog. Both heavy chains have the N- terminal sequence L.N.L.D, agreeing with the consensus derived from other integrin family alpha heavy chains. All 18 cysteine residues occur at positions conserved in human GPIIb and the vitronectin receptor alpha subunit VNR alpha. The putative calcium-binding domains of the GPIIbs have a high level of amino acid identity (92%), supporting the supposition that these regions have a critical biologic role. The final 48 C-terminal amino acid residues of the heavy chain of rodent GPIIb share only 56% identity with its human counterpart, and the proposed cleavage site of human GPIIb into its heavy and light chains is not present in the rodent sequence. Although we demonstrate that rodent GPIIb is split into two subunits during its maturation, this process either involves a different recognition sequence in the rodent or occurs at a different site. Finally, partial genomic DNA sequence analysis indicates that there are at least two rodent GPIIb genes: a normal gene, containing introns in positions similar to those in the human gene, and a processed pseudogene. The human haploid genome contains only a single GPIIb gene.

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