scholarly journals PER-6, an Extended-Spectrum β-Lactamase from Aeromonas allosaccharophila

2010 ◽  
Vol 54 (4) ◽  
pp. 1619-1622 ◽  
Author(s):  
Delphine Girlich ◽  
Laurent Poirel ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Amino Acid Identity ◽  
Environmental Isolate ◽  
Kinetic Properties ◽  
Seine River ◽  
Acid Identity ◽  
Extended Spectrum

ABSTRACT An Aeromonas allosaccharophila environmental isolate recovered from the Seine River (Paris, France) produced a novel extended-spectrum β-lactamase, PER-6, that shared 92% amino acid identity with the closest ß-lactamase, PER-2. The kinetic properties of PER-6 showed a slightly increased affinity for carbapenems. The bla PER-6 gene was chromosomally located and bracketed by non-transposon-related structures.

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 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 Coproduction of 16S rRNA Methyltransferase RmtD or RmtG with KPC-2 and CTX-M Group Extended-Spectrum β-Lactamases in Klebsiella pneumoniae

2013 ◽  
Vol 57 (5) ◽  
pp. 2397-2400 ◽  
Author(s):  
Maria Fernanda C. Bueno ◽  
Gabriela R. Francisco ◽  
Jessica A. O'Hara ◽  
Doroti de Oliveira Garcia ◽  
Yohei Doi
Keyword(s):  
Amino Acid ◽  
16S Rrna ◽  
Klebsiella Pneumoniae ◽  
Amino Acid Identity ◽  
Aminoglycoside Resistance ◽  
Content Type ◽  
Acid Identity ◽  
Paulo State ◽  
Extended Spectrum ◽  
High Level

ABSTRACTEightKlebsiella pneumoniaeclinical strains with high-level aminoglycoside resistance were collected from eight hospitals in São Paulo State, Brazil, in 2010 and 2011. Three of them produced an RmtD group 16S rRNA methyltransferase, RmtD1 or RmtD2. Five strains were found to produce a novel 16S rRNA methyltransferase, designated RmtG, which shared 57 to 58% amino acid identity with RmtD1 and RmtD2. Seven strains coproduced KPC-2 with or without various CTX-M group extended-spectrum β-lactamases, while the remaining strain coproduced CTX-M-2.

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 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 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 Molecular and Kinetic Comparison of the Novel Extended-Spectrum β-Lactamases CTX-M-25 and CTX-M-26

2004 ◽  
Vol 48 (12) ◽  
pp. 4829-4834 ◽  
Author(s):  
Craig J. Munday ◽  
David A. Boyd ◽  
Nigel Brenwald ◽  
Mark Miller ◽  
Jennifer M. Andrews ◽  
...  
Keyword(s):  
Amino Acid ◽  
Susceptibility Testing ◽  
Kinetic Studies ◽  
Amino Acid Identity ◽  
Amino Acid Substitutions ◽  
The Novel ◽  
Acid Identity ◽  
The United Kingdom ◽  
Extended Spectrum ◽  
Plasmid Profiling

ABSTRACT CTX-M-25 is a novel extended-spectrum β-lactamase isolated from a single Canadian Escherichia coli isolate. Susceptibility testing demonstrated that this enzyme confers resistance to both cefotaxime and ceftazidime, but the level of resistance was reduced with the addition of β-lactamase inhibitors. The bla CTX-M-25 gene was detected on a 111-kb plasmid. It is a member of the CTX-M-8 group and has the closest amino acid identity (99%; three amino acid substitutions) with CTX-M-26. The bla CTX-M-26 gene was detected on a 100-kb plasmid isolated from a Klebsiella pneumoniae strain from the United Kingdom, and plasmid profiling revealed that it showed some homology to the bla CTX-M-25-harboring plasmid. Both CTX-M genes were located downstream of ISEcp1, although the copy upstream of bla CTX-M-25 was disrupted by IS50-A. Comparative kinetic studies of recombinant CTX-M-25 and CTX-M-26 enzymes showed that CTX-M-25 has a higher level of ceftazidime hydrolysis (k cat values, 33 and 0.005 s−1 for CTX-M-25 and CTX-M-26, respectively).

scholarly journals A50 Whole-genome sequencing of African swine fever isolates from Sardinia

2019 ◽  
Vol 5 (Supplement_1) ◽  
Author(s):  
C Torresi ◽  
F Granberg ◽  
L Bertolotti ◽  
A Oggiano ◽  
B Colitti ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Data ◽  
Temporal Distribution ◽  
African Swine Fever ◽  
Amino Acid Identity ◽  
Genotype I ◽  
Acid Identity ◽  
Wide Range ◽  
Intergenic Sequences ◽  
Genes Encoding

Abstract In order to assess the molecular epidemiology of African swine fever (ASF) in Sardinia, we analyzed a wide range of isolates from wild and domestic pigs over a 31-year period (1978–2009) by genotyping sequence data from the genes encoding the p54 and the p72 proteins and the CVR. On this basis, the analysis of the B602L gene revealed a minor difference, placing the Sardinian isolates into two clusters according to their temporal distribution. As an extension of this study, in order to achieve a higher level of discrimination, three further variable genome regions, namely p30, CD2v, and I73R/I329L, of a large number of isolates collected from outbreaks in the years 2002–14 have been investigated. Sequence analysis of the CD2v region revealed a temporal subdivision of the viruses into two subgroups. These data, together with those from the B602L gene analysis, demonstrated that the viruses circulating in Sardinia belong to p72/genotype I, but since 1990 have undergone minor genetic variations in respect to its ancestor, thus making it impossible to trace isolates, enabling a more accurate assessment of the origin of outbreaks, and extending knowledge of virus evolution. To solve this problem, we have sequenced and annotated the complete genome of nine ASF isolates collected in Sardinia between 1978 and 2012. This was achieved using sequence data determined by next-generation sequencing. The results showed a very high identity with range of nucleotide similarity among isolates of 99.5 per cent to 99.9 per cent. The ASF virus (ASFV) genomes were composed of terminal inverted repeats and conserved and non-conserved ORFs. Among the conserved ORFs, B385R, H339R, and O61R-p12 showed 100 per cent amino acid identity. The same was true for the hypervariable ORFs, with regard to X69R, DP96R, DP60R, EP153R, B407L, I10L, and L60L genes. The EP402R and B602L genes showed, as expected, an amino acid identity range of 98.5 per cent to 100 per cent and 91 per cent to 100 per cent, respectively. In addition, all of the isolates displayed variable intergenic sequences. As a whole, the results from our studies confirmed a remarkable genetic stability of the ASFV/p72 genotype I viruses circulating in Sardinia.

Characterization and Induction of Two Cytochrome P450 Genes, CYP6AE28 and CYP6AE30, in Cnaphalocrocis medinalis: Possible Involvement in Metabolism of Rice Allelochemicals

2010 ◽  
Vol 65 (11-12) ◽  
pp. 719-725 ◽  
Author(s):  
Xiaoli Liu ◽  
Jun Chen ◽  
Zhifan Yang
Keyword(s):  
Amino Acid ◽  
Rice Variety ◽  
Amino Acid Identity ◽  
Cnaphalocrocis Medinalis ◽  
Amino Acid Residues ◽  
Acid Identity ◽  
Rice Leaf Folder ◽  
Cytochrome P450 Genes ◽  
Molecular Masses ◽  
Lepidoptera Pyralidae

Two cDNAs specific for P450 genes, CYP6AE28 and CYP6AE30, have been isolated from the rice leaf folder Cnaphalocrocis medinalis Guenée (Lepidoptera: Pyralidae). Both cDNApredicted proteins have 504 amino acid residues in length, but with molecular masses of 60177 Dalton for CYP6AE28 and 60020 Dalton for CYP6AE30, and theoretical pI values of 8.49 for CYP6AE28 and 8.56 for CYP6AE30, respectively. Both putative proteins contain the conserved structural and functional domains characteristic of all CYP6 members. CYP6AE28 and CYP6AE30 show 52% amino acid identity to each other; both of them have 49 - 56% identities with CYP6AE1, Cyp6ae12, and CYP6AE14. Phylogenetic analysis showed that the two P450s are grouped in the lineage containing some of the CYP6AE members, CYP6B P450s and CYP321A1. The transcripts of CYP6AE28 and CYP6AE30 were found to be induced in response to TKM-6, a rice variety with high resistance to C. medinalis. The results suggest that the two P450s may play important roles in adaptation to the host plant rice. This is the first report of P450 genes cloned in C. medinalis

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