CONICET | Buscador de Institutos y Recursos Humanos

The emergence of Gram-negative clinical species harboring blaNDM-1 gene encoding themetallo-b-lactamase NDM-1 has aroused public concern worldwide. Complete sequencing of plasmidscarrying blaNDM-1 provides important information of its genetic environment and a better understandingof its spread. We characterize here a novel plasmid, pNDM229, containing blaNDM-1 isolated from acarbapenem resistant-Acinetobacter bereziniae clinical strain (HPC229) in Rosario, Argentina from animmunocompromised female inpatient. We also compare here the blaNDM-1-containing geneticplatform of pNDM229 with those present in other Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125blaNDM-1 gene encoding themetallo-b-lactamase NDM-1 has aroused public concern worldwide. Complete sequencing of plasmidscarrying blaNDM-1 provides important information of its genetic environment and a better understandingof its spread. We characterize here a novel plasmid, pNDM229, containing blaNDM-1 isolated from acarbapenem resistant-Acinetobacter bereziniae clinical strain (HPC229) in Rosario, Argentina from animmunocompromised female inpatient. We also compare here the blaNDM-1-containing geneticplatform of pNDM229 with those present in other Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125b-lactamase NDM-1 has aroused public concern worldwide. Complete sequencing of plasmidscarrying blaNDM-1 provides important information of its genetic environment and a better understandingof its spread. We characterize here a novel plasmid, pNDM229, containing blaNDM-1 isolated from acarbapenem resistant-Acinetobacter bereziniae clinical strain (HPC229) in Rosario, Argentina from animmunocompromised female inpatient. We also compare here the blaNDM-1-containing geneticplatform of pNDM229 with those present in other Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125blaNDM-1 provides important information of its genetic environment and a better understandingof its spread. We characterize here a novel plasmid, pNDM229, containing blaNDM-1 isolated from acarbapenem resistant-Acinetobacter bereziniae clinical strain (HPC229) in Rosario, Argentina from animmunocompromised female inpatient. We also compare here the blaNDM-1-containing geneticplatform of pNDM229 with those present in other Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125blaNDM-1 isolated from acarbapenem resistant-Acinetobacter bereziniae clinical strain (HPC229) in Rosario, Argentina from animmunocompromised female inpatient. We also compare here the blaNDM-1-containing geneticplatform of pNDM229 with those present in other Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125Acinetobacter bereziniae clinical strain (HPC229) in Rosario, Argentina from animmunocompromised female inpatient. We also compare here the blaNDM-1-containing geneticplatform of pNDM229 with those present in other Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125blaNDM-1-containing geneticplatform of pNDM229 with those present in other Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125Acinetobacter plasmids.The whole genome sequencing of HPC229 disclosed the presence of blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125blaNDM-1in a 44,560 bp plasmidcontaining 53 predicted ORFs, from which 31 encode proteins with BLAST scores compatible tosequences of attributed functions in databases. Phylogenetic analysis using representative N-terminalrelaxase domains from the different MOB families indicated a close affiliation of the pNDM229relaxase (TraA) to the MOBQ1 family, characteristic of broad host range plasmids. The immediategenetic environment of blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125blaNDM-1 in pNDM229 was similar to those reported previously forpNDM-BJ01-like plasmids (1). However, some differences were noted between all these plasmidsincluding variations downstream of the Tn125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125125 element such as: i) a novel copy of ISAba14-like inpNDM229, ii) an extra ISAba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125Aba125 copy in A. baumannii pAbNDM, and iii) the absence of 3´ ISAba125in pM131_NDM1 and its replacement by an ISAba11. Other relevant differences between the aboveplasmids include deletions involving a number of genes composing the blaNDM-1-containing platforms.Still, two regions are identical in all analyzed platforms which comprise from the ISAba14 elementlocated upstream of the Tn125 to blaNDM-1, and the last 134-bp of its 3?end suggesting a commonorigin for these arrangements. Interestingly, the fact that the blaNDM-1-containing Tn125 in pNDM229is bracketed by two ISAba14-like suggests that this structure forms a novel composite transposonwhich could move itself as a whole. The presence of an ISAba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.Aba11. Other relevant differences between the aboveplasmids include deletions involving a number of genes composing the blaNDM-1-containing platforms.Still, two regions are identical in all analyzed platforms which comprise from the ISAba14 elementlocated upstream of the Tn125 to blaNDM-1, and the last 134-bp of its 3?end suggesting a commonorigin for these arrangements. Interestingly, the fact that the blaNDM-1-containing Tn125 in pNDM229is bracketed by two ISAba14-like suggests that this structure forms a novel composite transposonwhich could move itself as a whole. The presence of an ISAba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.blaNDM-1-containing platforms.Still, two regions are identical in all analyzed platforms which comprise from the ISAba14 elementlocated upstream of the Tn125 to blaNDM-1, and the last 134-bp of its 3?end suggesting a commonorigin for these arrangements. Interestingly, the fact that the blaNDM-1-containing Tn125 in pNDM229is bracketed by two ISAba14-like suggests that this structure forms a novel composite transposonwhich could move itself as a whole. The presence of an ISAba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.Aba14 elementlocated upstream of the Tn125 to blaNDM-1, and the last 134-bp of its 3?end suggesting a commonorigin for these arrangements. Interestingly, the fact that the blaNDM-1-containing Tn125 in pNDM229is bracketed by two ISAba14-like suggests that this structure forms a novel composite transposonwhich could move itself as a whole. The presence of an ISAba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.125 to blaNDM-1, and the last 134-bp of its 3?end suggesting a commonorigin for these arrangements. Interestingly, the fact that the blaNDM-1-containing Tn125 in pNDM229is bracketed by two ISAba14-like suggests that this structure forms a novel composite transposonwhich could move itself as a whole. The presence of an ISAba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.blaNDM-1-containing Tn125 in pNDM229is bracketed by two ISAba14-like suggests that this structure forms a novel composite transposonwhich could move itself as a whole. The presence of an ISAba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.Aba14-like suggests that this structure forms a novel composite transposonwhich could move itself as a whole. The presence of an ISAba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.Aba14-like copy in the HPC229chromosome suggests that this novel arrangement could have been formed recently in this A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.A.bereziniae strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.strain. Finally, we propose that the mobilization of plasmids harboring blaNDM-1 amongdifferent Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.Acinetobacter hosts could account for the genetic variations (indels) observed in the abovedescribed blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.blaNDM-1-containing platforms.1-Jones et al., Antimicrob Agents Chemother. 2015.59:923-929.et al., Antimicrob Agents Chemother. 2015.59:923-929.