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 Characterization of a Chromosomally Encoded Extended-Spectrum Class A β-Lactamase from Kluyvera cryocrescens

2001 ◽  
Vol 45 (12) ◽  
pp. 3595-3598 ◽  
Author(s):  
Jean W. Decousser ◽  
Laurent Poirel ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Reference Strain ◽  
Amino Acid Identity ◽  
Acid Identity ◽  
Class A ◽  
Extended Spectrum ◽  
Kluyvera Ascorbata ◽  
Lactamase Gene ◽  
Kluyvera Cryocrescens

ABSTRACT A chromosomally located β-lactamase gene, cloned and expressed inEscherichia coli from a reference strain of the enterobacterial species Kluyvera cryocrescens, encoded a clavulanic acid-inhibited Ambler class A enzyme, KLUC-1, with a pI value of 7.4. KLUC-1 shared 86% amino acid identity with a subgroup of plasmid-mediated CTX-M-type extended-spectrum β-lactamases (CTX-M-1, -3, -10, -11, and -12), the most closely related enzymes, and 77% amino acid identity with KLUA-1 from Kluyvera ascorbata.The substrate profile of KLUC-1 corresponded to that of CTX-M-type enzymes.

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 Characterization of CIA-1, an Ambler Class A Extended-Spectrum β-Lactamase from Chryseobacterium indologenes

2011 ◽  
Vol 56 (1) ◽  
pp. 588-590 ◽  
Author(s):  
Takehisa Matsumoto ◽  
Mika Nagata ◽  
Nau Ishimine ◽  
Kenji Kawasaki ◽  
Kazuyoshi Yamauchi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Reference Strain ◽  
Content Type ◽  
Chryseobacterium Indologenes ◽  
Esbl Gene ◽  
Class A ◽  
Extended Spectrum ◽  
Class B ◽  
Lactamase Gene

ABSTRACTAn Ambler class A β-lactamase gene,blaCIA-1, was cloned from the reference strainChryseobacterium indologenesATCC 29897 and expressed inEscherichia coliBL21. TheblaCIA-1gene encodes a novel extended-spectrum β-lactamase (ESBL) that shared 68% and 60% identities with the CGA-1 and CME-1 β-lactamases, respectively.blaCIA-1-like genes were detected from clinical isolates. In addition to the metallo-β-lactamase IND of Ambler class B,C. indologeneshas a class A ESBL gene,blaCIA-1, located on the chromosome.

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 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 Identification of a Progenitor of the CTX-M-9 Group of Extended-Spectrum β-Lactamases from Kluyvera georgiana Isolated in Guyana

2005 ◽  
Vol 49 (5) ◽  
pp. 2112-2115 ◽  
Author(s):  
Adam B. Olson ◽  
M. Silverman ◽  
David A. Boyd ◽  
Allison McGeer ◽  
Barbara M. Willey ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Chromosomal Region ◽  
Amino Acid Identity ◽  
Nucleotide Identity ◽  
Acid Identity ◽  
Extended Spectrum ◽  
M 14

ABSTRACT Chromosomal β-lactamase genes (bla KLUY) from six Kluyvera georgiana strains isolated in Guyana were cloned and expressed in Escherichia coli. KLUY-1 exhibited 100% amino acid identity with the extended-spectrum β-lactamase CTX-M-14. We also show that a 2.7-kb Kluyvera chromosomal region exhibits 99% nucleotide identity to a portion of In60 that includes bla CTX-M-9.

scholarly journals The Class A Carbapenemases BKC-1 and GPC-1 Both Originate from the Bacterial Genus Shinella

2020 ◽  
Vol 64 (12) ◽  
Author(s):  
Nicolas Kieffer ◽  
Stefan Ebmeyer ◽  
D. G. Joakim Larsson
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Comparative Genomics ◽  
Amino Acid Identity ◽  
Gene Fragment ◽  
Content Type ◽  
Acid Identity ◽  
Bacterial Genus ◽  
Class A

ABSTRACT Comparative genomics identified the environmental bacterial genus Shinella as the most likely origin of the class A carbapenemases BKC-1 and GPC-1. Available sequences and PCR analyses of additional Shinella species revealed homologous β-lactamases showing up to 85.4% and 93.3% amino acid identity to both enzymes, respectively. The genes conferred resistance to β-lactams once expressed in Escherichia coli. blaBKC-1 likely evolved from a putative ancestral Shinella gene with higher homology through duplication of a gene fragment.

scholarly journals Biochemical Sequence Analyses of GES-1, a Novel Class A Extended-Spectrum β-Lactamase, and the Class 1 Integron In52 from Klebsiella pneumoniae

2000 ◽  
Vol 44 (3) ◽  
pp. 622-632 ◽  
Author(s):  
Laurent Poirel ◽  
Isabelle Le Thomas ◽  
Thierry Naas ◽  
Amal Karim ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Amino Acid Identity ◽  
Class 1 Integron ◽  
Chloramphenicol Resistance ◽  
Acid Identity ◽  
Gene Cassettes ◽  
Class A ◽  
Extended Spectrum ◽  
Class 1

ABSTRACT Klebsiella pneumoniae ORI-1 was isolated in 1998 in France from a rectal swab of a 1-month-old girl who was previously hospitalized in Cayenne Hospital, Cayenne, French Guiana. This strain harbored a ca. 140-kb nontransferable plasmid, pTK1, that conferred an extended-spectrum cephalosporin resistance profile antagonized by the addition of clavulanic acid, tazobactam, or imipenem. The gene for GES-1 (Guiana extended-spectrum β-lactamase) was cloned, and its protein was expressed in Escherichia coli DH10B, where this pI-5.8 β-lactamase of a ca. 31-kDa molecular mass conferred resistance to oxyimino cephalosporins (mostly to ceftazidime). GES-1 is weakly related to the other plasmid-located Ambler class A extended-spectrum β-lactamases (ESBLs). The highest percentage of amino acid identity was obtained with the carbenicillinase GN79 from Proteus mirabilis; with YENT, a chromosome-borne penicillinase fromYersinia enterocolitica; and with L-2, a chromosome-borne class A cephalosporinase from Stenotrophomonas maltophilia(36% amino acid identity each). However, a dendrogram analysis showed that GES-1 clustered within a class A ESBL subgroup together with ESBLs VEB-1 and PER-1. Sequencing of a 7,098-bp DNA fragment from plasmid pTK1 revealed that the GES-1 gene was located on a novel class 1 integron named In52 that was characterized by (i) a 5′ conserved segment containing an intI1 gene possessing two putative promoters, P1 and P2, for coordinated expression of the downstream antibiotic resistance genes and an attI1 recombination site; (ii) five antibiotic gene cassettes, bla GES-1,aac(6′)Ib′ (gentamicin resistance and amikacin susceptibility), dfrXVb (trimethoprim resistance), a novel chloramphenicol resistance gene (cmlA4), andaadA2 (streptomycin-spectinomycin resistance); and (iii) a 3′ conserved segment consisting of qacEΔ1 andsulI. The bla GES-1 andaadA2 gene cassettes were peculiar, since they lacked a typical 59-base element. This work identified the second class A ESBL gene of a non-TEM, non-SHV series which was located in the plasmid and integron, thus providing it additional means for its spread and its expression.

scholarly journals Chromosome-Borne Class A BOR-1 β-Lactamase of Bordetella bronchiseptica and Bordetella parapertussis

2005 ◽  
Vol 49 (6) ◽  
pp. 2565-2567 ◽  
Author(s):  
Marie-Frédérique Lartigue ◽  
Laurent Poirel ◽  
Nicolas Fortineau ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Clavulanic Acid ◽  
Stenotrophomonas Maltophilia ◽  
Amino Acid Identity ◽  
Bordetella Bronchiseptica ◽  
Bordetella Parapertussis ◽  
Acid Identity ◽  
Class A ◽  
Lactamase Gene ◽  
Reference Strains

ABSTRACT A narrow-spectrum clavulanic acid-inhibited class A β-lactamase, BOR-1, was identified in a Bordetella bronchiseptica clinical isolate. It shared 45% amino acid identity with L-2 from Stenotrophomonas maltophilia. An identical β-lactamase gene was found in B. bronchiseptica and Bordetella parapertussis reference strains that may contribute only in part to their resistance phenotype.

scholarly journals EBR-1, a Novel Ambler Subclass B1 β-Lactamase from Empedobacter brevis

2002 ◽  
Vol 46 (10) ◽  
pp. 3223-3227 ◽  
Author(s):  
Samuel Bellais ◽  
Delphine Girlich ◽  
Amal Karim ◽  
Patrice Nordmann
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Identity ◽  
Clinical Strain ◽  
Relative Molecular Mass ◽  
Gram Negative ◽  
Acid Identity ◽  
Molecular Subclass ◽  
Class B ◽  
Lactamase Gene

ABSTRACT Empedobacter brevis (formerly designated Flavobacterium breve) is a gram-negative aerobe involved in nosocomial infections. The Ambler class B β-lactamase gene bla EBR-1 was cloned and expressed in Escherichia coli from E. brevis clinical strain ASS-1, which had reduced susceptibility to expanded-spectrum cephalosporins and carbapenems. Purified β-lactamase EBR-1 hydrolyzed penicillins, cephalosporins, and carbapenems efficiently but not aztreonam. Kinetic parameters of EBR-1 were similar to those of class B enzymes such as BlaB, IND-2, and GOB-1 identified from other Flavobacteriaceae species, except for meropenem, which was more hydrolyzed by β-lactamase GOB-1. EBR-1, with a pI of 8.0 and a relative molecular mass of ca. 25 kDa, was classified in functional subgroup 3a, which includes most of the class B β-lactamases. EBR-1, which belongs to molecular subclass B1 of metalloenzymes, shares 58, 57, and 42% amino acid identity with the most closely related β-lactamases, IND-1/IND-2 from Chryseobacterium indologenes, CGB-1 from Chryseobacterium gleum, and BlaB from Chryseobacterium meningosepticum, respectively.

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