Phylogeny of LCR‐1 and OXA‐5 with class A and class D β‐lactamases

Couture, Félix; Lachapelle, Jean; Levesque, Roger C.

doi:10.1111/j.1365-2958.1992.tb00894.x

Cited by 137 publications

(111 citation statements)

References 65 publications

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“…It contains a gene for a new class D b-lactamase (bla NPS-2 ), a tetracycline resistance module tetA(C)-tetR, which is flanked by copies of IS26, and a class 1 integron terminated by an insertion of IS6100. The bla NPS-2 gene upstream of parA encodes a b-lactamase that is, respectively, 72 % and 71 % identical to the LCR-1 blactamase of Pseudomonas aeruginosa (Couture et al, 1992) and the NPS-1 b-lactamase of plasmid pB4 from the same wastewater treatment plant (Tauch et al, 2003b;Pai & Jacoby, 2001), and thus represents a new variant of this enzyme type. The NPS-2 b-lactamase belongs to class D (COG2602), which also includes LCR-1 of P. aeruginosa and NPS-1 encoded by pB4 (Tauch et al, 2003b).…”

Section: Resultsmentioning

confidence: 99%

The complete sequences of plasmids pB2 and pB3 provide evidence for a recent ancestor of the IncP-1β group without any accessory genes

et al. 2004

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The nucleotide sequences of the broad-host-range antibiotic resistance plasmids pB2 (61 kb) and pB3 (56 kb), which were isolated from a wastewater treatment plant, were determined and analysed. Both have a nearly identical IncP-1b backbone, which diverged early from the sequenced IncP-1b plasmids R751, pB10, pJP4, pADP1 and pUO1. In contrast to the latter plasmids, the pB2 and pB3 backbone does not seem to have undergone any deletions. The complete partition gene parA is located downstream of the mating pair formation (trb) module. A 14?4 kb or 19?0 kb mobile genetic element is present between traC and parA of pB3 and pB2, respectively. This region is typical for insertions in IncP-1b plasmids, but the insertion site is unique. Both elements differ only by a duplication in pB2 of a tetA(C)-tetR-tnpA IS26 fragment. The 5 bp target site duplication and the 26 bp inverted repeats flanking the mobile genetic elements are still intact, indicating that the insertion occurred recently. The element consists of three nested transposable elements: (i) a relict of a Tn402-like transposon with a gene for a new class D b-lactamase (bla NPS-2 ); (ii) within that, another Tn402-like element with a class 1 integron harbouring the gene cassettes cmlA1 for a chloramphenicol efflux protein and aadA2 encoding a streptomycin/spectinomycin adenylyltransferase, and a copy of IS6100; (iii) into the integrase gene intI1 a tetracycline resistance module tetA(C)-tetR flanked by copies of IS26 is inserted. Interestingly, in contrast to all other IncP-1b plasmids analysed so far, the oriV region between trfA and klcA is not interrupted by accessory genes, and there is no indication that previously inserted accessory genes have subsequently been deleted. The genes kluAB are also missing in that region and should thus be considered acquired genes. These findings, together with the fact that IncP-1b plasmids acquired accessory elements at various positions in the backbone, suggest that IncP-1b plasmids without any accessory genes exist in microbial communities. They must occasionally acquire accessory genes by transposition events, resulting in those plasmids that have been found based on selectable phenotypic traits. INTRODUCTIONHorizontal gene transfer mediated by plasmids plays an important role in the evolution and adaptability of bacteria (Davison, 1999). Plasmids of the incompatibility group IncP-1 are of particular interest because they are able to self-transfer and be stably maintained in a wide range of Gram-negative bacteria . Their conjugation system even promotes transfer to Grampositive bacteria and yeasts (Trieu-Cuot et al., 1987;Sikorski et al., 1990). Given their promiscuity and high prevalence in the environment, they serve as important vectors for the horizontal mobility of accessory genes that code for degradation of pollutants, resistance to antibiotics or heavy metals, and so far unknown functions (Top et al., 2000;Heuer et al., 2002; Dröge et al., 2000). Due to the particular interest in IncP-1 plasmids, they are one of t...

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Section: Resultsmentioning

confidence: 99%

The complete sequences of plasmids pB2 and pB3 provide evidence for a recent ancestor of the IncP-1β group without any accessory genes

et al. 2004

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“…bla OXA-74 differed by two mutations, C1973T and A2183G (numbered from the first ATG codon of the coding region), from bla OXA-10 (21). These mutations cause two amino acid substitutions in OXA-74, Ala69Val and Asn76Ser (numbered according to the class D ␤-lactamase scheme [8]), respectively, compared to OXA-10. The Ala69Val substitution differentiates OXA-74 from OXA-17, identified in P. aeruginosa isolates from Turkey that also produced PER-1 and OXA-2 (11,12).…”

Section: Pfge and Mlst Pfge Revealed Three Separate Clusters Of Isolmentioning

confidence: 99%

Outbreak of Pseudomonas aeruginosa Infections with PER-1 Extended-Spectrum β-Lactamase in Warsaw, Poland: Further Evidence for an International Clonal Complex

et al. 2007

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Forty-one Pseudomonas aeruginosa isolates with extended-spectrum ␤-lactamases (ESBLs) from a hospital in Warsaw, Poland, were analyzed. Thirty-seven isolates from several wards were collected over 9 months in 2003 and 2004. The isolates were recovered from patients with multiple types of infections, mostly respiratory tract and postoperative wound infections. All 41 isolates produced the PER-1 ESBL, originally observed in Turkey but recently also identified in several countries in Europe and the Far East. The bla PER-1 gene resided within the Tn1213 composite transposon, which was chromosomally located. Pulsed-field gel electrophoresis and multilocus sequence typing (MLST) revealed the presence of three separate clones among the isolates. Two of these, corresponding to sequence types (STs) ST244 and ST235, were responsible for parallel outbreaks. Apart from PER-1, all the isolates produced OXA-2 oxacillinase. ST235 isolates additionally expressed a novel enzyme, OXA-74, differing by one amino acid from the OXA-17 ESBL identified originally in PER-1-and OXA-2-positive P. aeruginosa isolates from Ankara, Turkey, in 1992. These earlier Ankara isolates with PER-1, OXA-2, and OXA-17 were also classified into ST235, which is a single-locus variant of two other STs, ST227 and ST230. ST227, ST230, and ST235 all correspond to the recently described clonal complex BG11, which seems to be internationally distributed, having spread in Turkey, Greece, Italy, Hungary, Poland, Sweden, and much of Russia. It is associated with various ␤-lactamases, including PER-1 and VIM metalloenzymes. This work further demonstrates the value of MLST of P. aeruginosa.

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“…and BLA4 indicate that they are metallo-β-lactamase proteins (Couture et al 1992). STFK motif was found in PBP3.…”

Section: Motifs Of β-Lactam Resistance Determinantsmentioning

confidence: 99%

“…STFK motif was found in PBP3. Previous studies have indicated that STFK is the most frequently found motif (Couture et al 1992) and it is characteristic of Class D β-lactamases (Couture et al 1992;Donald et al 2000). STFK along with KTG motif are well-known to be involved in the serine active-site function and regulation (Couture et al 1992;Massova & Mobashery 1998).…”

Section: Motifs Of β-Lactam Resistance Determinantsmentioning

confidence: 99%

Computational and functional analysis of β-lactam resistance in Zymomonas mobilis

et al. 2013

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Zymomonas mobilis, a Gram-negative ethanologenic non-pathogenic bacterium, is reported to exhibit resistance to high concentrations of β-lactam antibiotics. In the present study, Z. mobilis was found to be resistant to I-IV generations of cephalosporins and carbapenems, i.e. narrow, broad and extended spectrum β-lactam antibiotics. We have analysed the genome of Z. mobilis (GenBank accession No.: NC 006526) harbouring multiple genes coding for β-lactamases (BLA), β-lactamase domain containing proteins (BDP) and penicillin binding proteins (PBP). The conserved domain database analysis of BDPs predicted them to be members of metallo β-lactamase superfamily. Further, class C specific multidomain AmpC (β-lactamase C) was found in the three β-lactamases. The β-lactam resistance determinants motifs, HXHXD, KXG, SXXK, SXN, and YXN are present in the BLAs, BDPs and PBPs of Z. mobilis. The predicted theoretical pI and aliphatic index values suggested their stability. One of the PBPs, PBP2, was predicted to share functional association with rod shape determining proteins (GenBank accession Nos. YP 162095 and YP 162091). Homology modelling of three dimensional structures of the β-lactam resistance determinants and further docking studies with penicillin and other β-lactam antibiotics indicated their substrate-specificity. Semi-quantitative PCR analysis indicated that the expression of all BLAs and one BDP are induced by penicillin. Disk diffusion assay, SDS-PAGE and zymogram analysis confirms the substrate specificity of the β-lactam resistance determinants. This study gives a broader picture of the β-lactam resistance determinants of a non-pathogenic ethanologenic Z. mobilis bacterium that could have implications in laboratories since it is routinely used in many research laboratories in the world for ethanol, fructooligosaccharides, levan production and has also been reported to be present in wine and beer as a spoilage organism.

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Phylogeny of LCR‐1 and OXA‐5 with class A and class D β‐lactamases

Cited by 137 publications

References 65 publications

The complete sequences of plasmids pB2 and pB3 provide evidence for a recent ancestor of the IncP-1β group without any accessory genes

The complete sequences of plasmids pB2 and pB3 provide evidence for a recent ancestor of the IncP-1β group without any accessory genes

Outbreak of Pseudomonas aeruginosa Infections with PER-1 Extended-Spectrum β-Lactamase in Warsaw, Poland: Further Evidence for an International Clonal Complex

Computational and functional analysis of β-lactam resistance in Zymomonas mobilis

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