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 Genetic and Biochemical Characterization of FRI-1, a Carbapenem-Hydrolyzing Class A β-Lactamase from Enterobacter cloacae

2015 ◽  
Vol 59 (12) ◽  
pp. 7420-7425 ◽  
Author(s):  
Laurent Dortet ◽  
Laurent Poirel ◽  
Samia Abbas ◽  
Saoussen Oueslati ◽  
Patrice Nordmann
Keyword(s):  
Biochemical Characterization ◽  
Enterobacter Cloacae ◽  
Conjugative Plasmid ◽  
Lower Sensitivity ◽  
Gene Encoding ◽  
Content Type ◽  
Class A ◽  
Encoding Gene ◽  
Lactamase Gene

ABSTRACTAnEnterobacter cloacaeisolate was recovered from a rectal swab from a patient hospitalized in France with previous travel to Switzerland. It was resistant to penicillins, narrow- and broad-spectrum cephalosporins, aztreonam, and carbapenems but remained susceptible to expanded-spectrum cephalosporins. Whereas PCR-based identification of the most common carbapenemase genes failed, the biochemical Carba NP test II identified an Ambler class A carbapenemase. Cloning experiments followed by sequencing identified a gene encoding a totally novel class A carbapenemase, FRI-1, sharing 51 to 55% amino acid sequence identity with the closest carbapenemase sequences. However, it shared conserved residues as a source of carbapenemase activity. Purified β-lactamase FRI-1 hydrolyzed penicillins, aztreonam, and carbapenems but spared expanded-spectrum cephalosporins. The 50% inhibitory concentrations (IC50s) of clavulanic acid and tazobactam were 10-fold higher than those found forKlebsiella pneumoniaecarbapenemase (KPC), IMI, and SME, leading to lower sensitivity of FRI-1 activity to β-lactamase inhibitors. TheblaFRI-1gene was located on a ca. 110-kb untypeable, transferable, and non-self-conjugative plasmid. A putative LysR family regulator-encoding gene at the 5′ end of the β-lactamase gene was identified, leading to inducible expression of theblaFRI-1gene.

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 PME-1, an Extended-Spectrum β-Lactamase Identified in Pseudomonas aeruginosa

2011 ◽  
Vol 55 (6) ◽  
pp. 2710-2713 ◽  
Author(s):  
Guo-Bao Tian ◽  
Jennifer M. Adams-Haduch ◽  
Tatiana Bogdanovich ◽  
Hong-Ning Wang ◽  
Yohei Doi
Keyword(s):  
Pseudomonas Aeruginosa ◽  
United Arab Emirates ◽  
Stenotrophomonas Maltophilia ◽  
Hydrolytic Activity ◽  
The United States ◽  
Amino Acid Identity ◽  
The Novel ◽  
Content Type ◽  
Class A ◽  
Extended Spectrum

ABSTRACTA novel extended-spectrum β-lactamase (ESBL) was identified in aPseudomonas aeruginosaclinical isolate obtained from a patient admitted to a hospital in Pennsylvania in 2008. The patient had a prolonged hospitalization in a hospital in Dubai, United Arab Emirates, before being transferred to the United States. The novel ESBL, designated PME-1 (Pseudomonas aeruginosaESBL 1), is a molecular class A, Bush-Jacoby-Medeiros group 2be enzyme and shared 50, 43, and 41% amino acid identity with the L2 β-lactamase ofStenotrophomonas maltophilia, CTX-M-9, and KPC-2, respectively. PME-1 conferred clinically relevant resistance to ceftazidime, cefotaxime, cefepime, and aztreonam inP. aeruginosaPAO1 but not to carbapenems. Purified PME-1 showed good hydrolytic activity against ceftazidime, cefotaxime, and aztreonam, while activity against carbapenems and cefepime could not be measured. PME-1 was inhibited well by β-lactamase inhibitors, including clavulanic acid, sulbactam, and tazobactam. TheblaPME-1gene was carried by an approximately 9-kb plasmid and flanked by tandem ISCR24elements.

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.

GPC-1, a novel class A carbapenemase detected in a clinical Pseudomonas aeruginosa isolate

2020 ◽  
Vol 75 (4) ◽  
pp. 911-916 ◽  
Author(s):  
Jennifer Schauer ◽  
Sören G Gatermann ◽  
Daniel Hoffmann ◽  
Lars Hupfeld ◽  
Niels Pfennigwerth
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Heterologous Expression ◽  
Biochemical Characterization ◽  
Resistance Mechanism ◽  
Carbapenem Resistance ◽  
Amino Acid Identity ◽  
The Novel ◽  
Bacterial Strains ◽  
Class A ◽  
Carbapenem Resistant

Abstract Objectives To investigate the carbapenem resistance mechanism of a carbapenem-resistant clinical Pseudomonas aeruginosa isolate. Methods A carbapenem-resistant P. aeruginosa isolate was recovered from a tracheal swab from a patient of a general ward in central Germany. Various phenotypic tests confirmed production of a carbapenemase that could not be identified further by PCR. A novel bla gene was identified by WGS and its carbapenemase activity was verified by heterologous expression in an Escherichia coli cloning strain. Kinetic parameters of the novel β-lactamase were determined by spectrophotometric measurements using purified enzyme. Results WGS confirmed the presence of a novel class A carbapenemase. The novel bla gene was named GPC-1 (GPC standing for German Pseudomonas Carbapenemase) and exhibited 77% amino acid identity to BKC-1. WGS also showed that blaGPC-1 was located on the chromosome surrounded by multiple ISs as part of a 26 kb genetic island. Heterologous expression of GPC-1 in E. coli TOP10 led to increased MICs of penicillins, oxyimino-cephalosporins, aztreonam and imipenem, but not of meropenem or ertapenem. Spectrophotometric measurements supported the MIC studies, but detected a slight hydrolysis of ertapenem and meropenem when using high concentrations of purified enzyme. Conclusions The biochemical characterization of GPC-1 emphasizes the ongoing emergence of novel carbapenemases. Strains expressing a weak carbapenemase like GPC-1 might go unrecognized by routine diagnostics due to low MICs for the bacterial strains producing such enzymes.

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 Genetics and Expression of the Carbapenem-Hydrolyzing Oxacillinase Gene blaOXA-23 in Acinetobacter baumannii

2007 ◽  
Vol 51 (4) ◽  
pp. 1530-1533 ◽  
Author(s):  
Stéphane Corvec ◽  
Laurent Poirel ◽  
Thierry Naas ◽  
Henri Drugeon ◽  
Patrice Nordmann
Keyword(s):  
Acinetobacter Baumannii ◽  
The Novel ◽  
Gene Encoding ◽  
Promoter Sequences ◽  
Insertion Elements ◽  
Genetic Structures ◽  
Lactamase Gene

ABSTRACT The genetic structures surrounding the plasmid-carried bla OXA-23 oxacillinase gene, encoding resistance to carbapenems, were studied in Acinetobacter baumannii. ISAba1 and the novel element ISAba4 were detected upstream of the bla OXA-23 gene, providing promoter sequences for its expression. These insertion elements were likely involved in transposition processes at the origin of acquisition of this β-lactamase gene.

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 Characterization of IMI-1 beta-lactamase, a class A carbapenem-hydrolyzing enzyme from Enterobacter cloacae.

1996 ◽  
Vol 40 (9) ◽  
pp. 2080-2086 ◽  
Author(s):  
B A Rasmussen ◽  
K Bush ◽  
D Keeney ◽  
Y Yang ◽  
R Hare ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Clavulanic Acid ◽  
Regulatory Protein ◽  
Enterobacter Cloacae ◽  
Amino Acid Sequences ◽  
Beta Lactamase ◽  
Gene Encoding ◽  
Class A ◽  
Lactamase Gene

In 1984, a year prior to the U.S. approval of imipenem for clinical use, a wound isolate and a bile isolate of Enterobacter cloacae were obtained from two patients in a California hospital. These isolates were resistant to imipenem, penicillins, and inhibitor combinations; early cephalosporins such as cephalothin, cefamandole, and cefoxitin; and cefoperazone. However, they were susceptible (MICs, < 4 micrograms/ml) to cefotaxime, ceftriaxone, ceftazidime, and moxalactam. Both strains produced an apparent TEM-1 beta-lactamase; an inducible NmcA-type imipenem-hydrolyzing beta-lactamase, IMI-1, with a pl of 7.05; and an inducible beta-lactamase with a pI of 8.1, typical of an E. cloacae AmpC beta-lactamase. Purified IMI-1 hydrolyzed imipenem and benzylpenicillin at modest rates, but more slowly than cephaloridine. The enzyme was inhibited by clavulanic acid and tazobactam. EDTA did not inhibit the cephaloridine-hydrolyzing activity. The beta-lactamase gene encoding IMI-1, imiA1, was cloned from E. cloacae 1413B. Sequence analysis identified the imiA1 gene as encoding a class A serine beta-lactamase. Both the imiA1 DNA and encoded amino acid sequences shared greater than 95% identity with the NmcA gene and its encoded protein. DNA sequence analysis also identified a gene upstream of imiA1 that shares > 95% identity with nmcR and that may encode a regulatory protein. In conclusion, IMI-1, a carbapenem-hydrolyzing beta-lactamase inhibited by clavulanic acid, was identified as a group 2f, class A, carbapenem-hydrolyzing cephalosporinase.

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