scholarly journals Biochemical-Genetic Analysis and Distribution of DES-1, an Ambler Class A Extended-Spectrum β-Lactamase from Desulfovibrio desulfuricans

2002 ◽  
Vol 46 (10) ◽  
pp. 3215-3222 ◽  
Author(s):  
Anne-Sophie Morin ◽  
Laurent Poirel ◽  
Francine Mory ◽  
Roger Labia ◽  
Patrice Nordmann
Keyword(s):  
Burkholderia Pseudomallei ◽  
Desulfovibrio Desulfuricans ◽  
Amino Acid Identity ◽  
Relative Molecular Mass ◽  
Prevotella Intermedia ◽  
Mature Protein ◽  
Class A ◽  
Abdominal Abscesses ◽  
Biochemical Genetic ◽  
Lactamase Gene

ABSTRACT Desulfovibrio spp. are gram-negative anaerobes phylogenetically related to Bacteroides spp., which are rarely isolated and which are mostly isolated from intra-abdominal abscesses. Desulfovibrio desulfuricans clinical isolate D3 had a clavulanic acid-inhibited β-lactam resistance profile and was resistant to some expanded-spectrum cephalosporins. A β-lactamase gene, bla DES-1, was cloned from whole-cell DNA of isolate D3 and expressed in Escherichia coli. Purified β-lactamase DES-1, with a pI value of 9.1, had a relative molecular mass of ca. 31 kDa and a mature protein of 288 amino acids. DES-1 was distantly related to Ambler class A β-lactamases and most closely related to PenA from Burkholderia pseudomallei (48% amino acid identity). It was weakly related to class A β-lactamases CblA, CepA, CfxA, and CfxA2 from other anaerobic species, Bacteroides spp. and Prevotella intermedia. Its hydrolysis spectrum included amino- and ureidopenicillins, narrow-spectrum cephalosporins, ceftriaxone, and cefoperazone. bla DES-1-like genes were not identified in phylogenetically related Desulfovibrio fairfieldensis isolates. However, they were found in some but not all D. desulfuricans strains, thus suggesting that these genes may be present in a given D. desulfuricans subspecies.

scholarly journals Genetic and Biochemical Characterization of CGB-1, an Ambler Class B Carbapenem-Hydrolyzing β-Lactamase from Chryseobacterium gleum

2002 ◽  
Vol 46 (9) ◽  
pp. 2791-2796 ◽  
Author(s):  
Samuel Bellais ◽  
Thierry Naas ◽  
Patrice Nordmann
Keyword(s):  
Reference Strain ◽  
Biochemical Characterization ◽  
Amino Acid Identity ◽  
Relative Molecular Mass ◽  
Class A ◽  
Molecular Subclass ◽  
Class B ◽  
Lactamase Gene ◽  
Chryseobacterium Gleum

ABSTRACT Chryseobacterium gleum (previously included in the Flavobacterium IIb species) is a gram-negative aerobe that is a source of nosocomial infections. An Ambler class B β-lactamase gene was cloned and expressed in Escherichia coli from reference strain C. gleum CIP 103039 that had reduced susceptibility to expanded-spectrum cephalosporins and carbapenems. The purified β-lactamase, CGB-1, with a pI value of 8.6 and a determined relative molecular mass of ca. 26 kDa, hydrolyzed penicillins; narrow- and expanded-spectrum cephalosporins; and carbapenems. CGB-1 was a novel member of the molecular subclass B1 of metallo-enzymes. It had 83 and 42% amino acid identity with IND-1 from Chryseobacterium indologenes and BlaB from C. meningosepticum, respectively. Thus, in addition to the previously characterized clavulanic acid-inhibited extended-spectrum β-lactamase CGA-1 of Ambler class A, C. gleum produces a very likely chromosome-borne class B β-lactamase.

scholarly journals Molecular and Biochemical Analysis of AST-1, a Class A β-Lactamase from Nocardia asteroides Sensu Stricto

2001 ◽  
Vol 45 (3) ◽  
pp. 878-882 ◽  
Author(s):  
Laurent Poirel ◽  
Frederic Laurent ◽  
Thierry Naas ◽  
Roger Labia ◽  
Patrick Boiron ◽  
...  
Keyword(s):  
Hydrolytic Activity ◽  
Amino Acid Identity ◽  
Sensu Stricto ◽  
Nocardia Asteroides ◽  
Relative Molecular Mass ◽  
E Coli ◽  
Class A ◽  
Activity Spectrum ◽  
Related Enzyme ◽  
Lactamase Gene

ABSTRACT A β-lactamase gene was cloned from a Nocardia asteroides sensu stricto clinical isolate. A recombinant plasmid, pAST-1, expressed the β-lactamase AST-1 in Escherichia coli JM109. Its pI was 4.8, and its relative molecular mass was 31 kDa. E. coli JM109(pAST-1) was resistant to penicillins and narrow-spectrum cephalosporins. The β-lactamase AST-1 had a restricted hydrolytic activity spectrum. Its activity was partially inhibited by clavulanic acid but not by sulbactam and tazobactam. AST-1 is an Ambler class A β-lactamase sharing 65% amino acid identity with β-lactamase FAR-1, the most closely related enzyme.

scholarly journals Biochemical-Genetic Analysis and Distribution of FAR-1, a Class A β-Lactamase from Nocardia farcinica

1999 ◽  
Vol 43 (7) ◽  
pp. 1644-1650 ◽  
Author(s):  
Frederic Laurent ◽  
Laurent Poirel ◽  
Thierry Naas ◽  
El Bachir Chaibi ◽  
Roger Labia ◽  
...  
Keyword(s):  
Burkholderia Cepacia ◽  
Recombinant Strain ◽  
Inhibitory Concentration ◽  
Amino Acid Identity ◽  
Significant Activity ◽  
Mature Protein ◽  
Low Level ◽  
Class A ◽  
Nocardia Farcinica ◽  
Biochemical Genetic

ABSTRACTFrom genomic DNA of the clinical isolateNocardia farcinicaVIC, a 1.6-kbSau3AI fragment was cloned and expressed inEscherichia coliJM109. The recombinant strain expressed a β-lactamase (pI, 4.6), FAR-1, which conferred high levels of resistance to amoxicillin, piperacillin, ticarcillin, and cephalothin. The hydrolysis constants (kcat,Km,Ki, and 50% inhibitory concentration) confirmed the MIC results and showed that FAR-1 activity is inhibited by clavulanic acid and at a low level by tazobactam and sulbactam. Moreover, FAR-1 β-lactamase hydrolyzes aztreonam (at a low level) without significant activity against ceftazidime, cefotaxime and imipenem. FAR-1 mature protein of molecular mass ca 32 kDa, has less than 60% amino acid identity with any other class A β-lactamases, being most closely related to PEN-A fromBurkholderia cepacia(52%). AblaFAR-1-like gene was found in all studiedN. farcinicastrains, underlining the constitutive origin of this gene.

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

2002 ◽  
Vol 46 (11) ◽  
pp. 3401-3405 ◽  
Author(s):  
Sophie Vimont ◽  
Laurent Poirel ◽  
Thierry Naas ◽  
Patrice Nordmann
Keyword(s):  
Reference Strain ◽  
Klebsiella Oxytoca ◽  
Amino Acid Identity ◽  
Relative Molecular Mass ◽  
Antibiotic Resistant ◽  
Class A ◽  
Kluyvera Ascorbata ◽  
Lactamase Gene ◽  
Proteus Penneri ◽  
Erwinia Persicina

ABSTRACT From whole-cell DNA of an enterobacterial Erwinia persicina reference strain that displayed a penicillinase-related antibiotic-resistant phenotype, a β-lactamase gene was cloned and expressed in Escherichia coli. It encoded a clavulanic-acid-inhibited Ambler class A β-lactamase, ERP-1, with a pI value of 8.1 and a relative molecular mass of ca. 28 kDa. ERP-1 shared 45 to 50% amino acid identity with the most closely related enzymes, the chromosomally encoded enzymes from Citrobacter koseri, Kluyvera ascorbata, Kluyvera cryocrescens, Klebsiella oxytoca, Proteus vulgaris, Proteus penneri, Rahnella aquatilis, Serratia fonticola, Yersinia enterocolitica, and the plasmid-mediated enzymes CTX-M-8 and CTX-M-9. The substrate profile of the noninducible ERP-1 was similar to that of these β-lactamases. ERP-1 is the first extended-spectrum β-lactamase from an enterobacterial species that is plant associated and plant pathogenic.

scholarly journals Identification of the Novel Narrow-Spectrum β-Lactamase SCO-1 in Acinetobacter spp. from Argentina

2007 ◽  
Vol 51 (6) ◽  
pp. 2179-2184 ◽  
Author(s):  
Laurent Poirel ◽  
Stéphane Corvec ◽  
Melina Rapoport ◽  
Pauline Mugnier ◽  
Alejandro Petroni ◽  
...  
Keyword(s):  
Amino Acid Identity ◽  
The Novel ◽  
Gene Encoding ◽  
Class A ◽  
Narrow Spectrum ◽  
A Value ◽  
Acinetobacter Spp ◽  
Encoding Gene ◽  
High Level ◽  
Lactamase Gene

ABSTRACT By studying the β-lactamase content of several Acinetobacter spp. isolates from Argentina, producing the expanded-spectrum β-lactamases (ESBL) VEB-1a or PER-2, a novel Ambler class A β-lactamase gene was identified. It encoded the narrow-spectrum β-lactamase SCO-1, whose activity was inhibited by clavulanic acid. SCO-1 hydrolyzes penicillins at a high level and cephalosporins and carbapenems at a very low level. β-Lactamase SCO-1 was identified from unrelated VEB-1a-positive or PER-2-positive Acinetobacter spp. isolates recovered from three hospitals. The bla SCO-1 gene was apparently located on a plasmid of ca. 150 kb from all cases but was not associated with any ESBL-encoding gene. The G+C content of the bla SCO gene was 52%, a value that does not correspond to that of the A. baumannii genome (39%). β-Lactamase SCO-1 shares 47% amino acid identity with CARB-5 and ca. 40% with the enzymes TEM, SHV, and CTX-M. A gene encoding a putative resolvase was identified downstream of the bla SCO-1 gene, but its precise way of acquisition remains to be determined.

scholarly journals Constitutive Expression of a Chromosomal Class A (BJM Group 2) β-Lactamase in Xanthomonas campestris

2004 ◽  
Vol 48 (1) ◽  
pp. 209-215 ◽  
Author(s):  
Shu-Fen Weng ◽  
Juey-Wen Lin ◽  
Chih-Hung Chen ◽  
Yih-Yuan Chen ◽  
Yi-Hsuan Tseng ◽  
...  
Keyword(s):  
Amino Acid ◽  
Xanthomonas Campestris ◽  
Southern Hybridization ◽  
Constitutive Expression ◽  
Structural Features ◽  
Amino Acid Identity ◽  
Upstream Region ◽  
Class A ◽  
Group 2 ◽  
Lactamase Gene

ABSTRACT Sequencing of the upstream region of the β-lactamase gene from Xanthomonas campestris pv. campestris 11 (bla XCC-1) revealed the cognate ampR1 gene (289 amino acids, 31 kDa). It runs divergently from bla XCC-1 with a 100-bp intergenic region (IG) containing partially overlapped promoters with structural features typical of the bla-ampR IG. The deduced AmpR1 protein shows significant identity in amino acid sequence and conserved motifs with AmpR proteins of other species, e.g., of Pseudomonas aeruginosa (58.2% amino acid identity). Results of insertional mutation, complementation tests, and β-lactamase assays suggested that expression of bla XCC-1 was constitutive and dependent on AmpR1. Four bla genes and two ampR genes are present in the fully sequenced X. campestris pv. campestris ATCC 33913 genome, with XCC3039 and XCC3040 considered the analogues of bla XCC-1 and ampR1, respectively. An ampR1 homologue was detected by Southern hybridization in the ampicillin-resistant Xanthomonas strains, which appear to express β-lactamase constitutively. Although the significance remains to be studied, constitutive expression of β-lactamase by a widespread bacterial genus raises environmental concerns regarding the dissemination of resistance genes.

scholarly journals Molecular and Biochemical Characterization of the Chromosome-Encoded Class A β-Lactamase BCL-1 from Bacillus clausii

2007 ◽  
Vol 51 (11) ◽  
pp. 4009-4014 ◽  
Author(s):  
Delphine Girlich ◽  
Roland Leclercq ◽  
Thierry Naas ◽  
Patrice Nordmann
Keyword(s):  
Escherichia Coli ◽  
Biochemical Characterization ◽  
Amino Acid Identity ◽  
Acid Identity ◽  
Class A ◽  
Bacillus Clausii ◽  
Its Gene ◽  
Lactamase Gene ◽  
Reference Strains

ABSTRACT A chromosomal β-lactamase gene from Bacillus clausii NR, which is used as a probiotic, was cloned and expressed in Escherichia coli. It encodes a clavulanic acid-susceptible Ambler class A β-lactamase, BCL-1, with a pI of 5.5 and a molecular mass of ca. 32 kDa. It shares 91% and 62% amino acid identity with the chromosomally encoded PenP penicillinases from B. clausii KSM-K16 and Bacillus licheniformis, respectively. The hydrolytic profile of this β-lactamase includes penicillins, narrow-spectrum cephalosporins, and cefpirome. This chromosome-encoded enzyme was inducible in B. clausii, and its gene is likely related to upstream-located regulatory genes that share significant identity with those reported to be upstream of the penicillinase gene of B. licheniformis. The bla BCL-1 gene was located next to the known chromosomal aadD2 gene and the erm34 gene, which encode resistance to aminoglycosides and macrolides, respectively. Similar genes were found in a collection of B. clausii reference strains.

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 Cloning and Expression of Class A β-Lactamase Gene blaABPS in Burkholderia pseudomallei

2002 ◽  
Vol 46 (4) ◽  
pp. 1132-1135 ◽  
Author(s):  
Terence K. M. Cheung ◽  
P. L. Ho ◽  
Patrick C. Y. Woo ◽  
K. Y. Yuen ◽  
P. Y. Chau
Keyword(s):  
Escherichia Coli ◽  
Sequence Analysis ◽  
Yersinia Enterocolitica ◽  
Isoelectric Point ◽  
Burkholderia Pseudomallei ◽  
Cloning And Expression ◽  
Conserved Motifs ◽  
Class A ◽  
Lactamase Gene

ABSTRACT The β-lactamase gene blaA BPS in Burkholderia pseudomallei was cloned and expressed in Escherichia coli. BPS-1 is a cephalosporinase with an isoelectric point of 7.7. Sequence analysis of BPS-1 revealed conserved motifs typical of class A β-lactamases and a relationship to the PenA (in B. cepacia) and BlaI (in Yersinia enterocolitica) lineages.

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.

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