author_facet Tavío, María M.
Aquili, Virginia D.
Vila, Jordi
Poveda, José B.
Tavío, María M.
Aquili, Virginia D.
Vila, Jordi
Poveda, José B.
author Tavío, María M.
Aquili, Virginia D.
Vila, Jordi
Poveda, José B.
spellingShingle Tavío, María M.
Aquili, Virginia D.
Vila, Jordi
Poveda, José B.
Journal of Medical Microbiology
Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
Microbiology (medical)
General Medicine
Microbiology
author_sort tavío, maría m.
spelling Tavío, María M. Aquili, Virginia D. Vila, Jordi Poveda, José B. 0022-2615 1473-5644 Microbiology Society Microbiology (medical) General Medicine Microbiology http://dx.doi.org/10.1099/jmm.0.063727-0 <jats:p>The mechanisms responsible for the increase in ceftazidime MIC in two <jats:italic>Escherichia coli in vitro</jats:italic> selected mutants, Caz/20-1 and Caz/20-2, were studied. OmpF loss and overexpression of <jats:italic>acrB</jats:italic>, <jats:italic>acrD</jats:italic> and <jats:italic>acrF</jats:italic> that were associated with <jats:italic>acrR</jats:italic> and <jats:italic>marR</jats:italic> mutations and <jats:italic>sdiA</jats:italic> overexpression, together with mutations A233T and I332V in FtSI (PBP3) resulted in ceftazidime resistance in Caz/20-2, multiplying by 128-fold the ceftazidime MIC in the parental clinical isolate PS/20. Absence of detectable β-lactamase hydrolytic activity in the crude extract of Caz/20-2 was observed, and coincided with Q191K and P209S mutations in AmpC and a nucleotide substitution at −28 in the <jats:italic>ampC</jats:italic> promoter, whereas β-lactamase hydrolytic activity in crude extracts of PS/20 and Caz/20-1 strains was detected. Nevertheless, a fourfold increase in ceftazidime MIC in Caz/20-1 compared with that in PS/20 was due to the increased transcript level of <jats:italic>acrB</jats:italic> derived from <jats:italic>acrR</jats:italic> mutation. The two Caz mutants and PS/20 showed the same mutations in AmpG and ParE.</jats:p> Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA Journal of Medical Microbiology
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title Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_unstemmed Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_full Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_fullStr Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_full_unstemmed Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_short Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_sort resistance to ceftazidime in escherichia coli associated with acrr, marr and pbp3 mutations and overexpression of sdia
topic Microbiology (medical)
General Medicine
Microbiology
url http://dx.doi.org/10.1099/jmm.0.063727-0
publishDate 2014
physical 56-65
description <jats:p>The mechanisms responsible for the increase in ceftazidime MIC in two <jats:italic>Escherichia coli in vitro</jats:italic> selected mutants, Caz/20-1 and Caz/20-2, were studied. OmpF loss and overexpression of <jats:italic>acrB</jats:italic>, <jats:italic>acrD</jats:italic> and <jats:italic>acrF</jats:italic> that were associated with <jats:italic>acrR</jats:italic> and <jats:italic>marR</jats:italic> mutations and <jats:italic>sdiA</jats:italic> overexpression, together with mutations A233T and I332V in FtSI (PBP3) resulted in ceftazidime resistance in Caz/20-2, multiplying by 128-fold the ceftazidime MIC in the parental clinical isolate PS/20. Absence of detectable β-lactamase hydrolytic activity in the crude extract of Caz/20-2 was observed, and coincided with Q191K and P209S mutations in AmpC and a nucleotide substitution at −28 in the <jats:italic>ampC</jats:italic> promoter, whereas β-lactamase hydrolytic activity in crude extracts of PS/20 and Caz/20-1 strains was detected. Nevertheless, a fourfold increase in ceftazidime MIC in Caz/20-1 compared with that in PS/20 was due to the increased transcript level of <jats:italic>acrB</jats:italic> derived from <jats:italic>acrR</jats:italic> mutation. The two Caz mutants and PS/20 showed the same mutations in AmpG and ParE.</jats:p>
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author Tavío, María M., Aquili, Virginia D., Vila, Jordi, Poveda, José B.
author_facet Tavío, María M., Aquili, Virginia D., Vila, Jordi, Poveda, José B., Tavío, María M., Aquili, Virginia D., Vila, Jordi, Poveda, José B.
author_sort tavío, maría m.
container_issue 1
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description <jats:p>The mechanisms responsible for the increase in ceftazidime MIC in two <jats:italic>Escherichia coli in vitro</jats:italic> selected mutants, Caz/20-1 and Caz/20-2, were studied. OmpF loss and overexpression of <jats:italic>acrB</jats:italic>, <jats:italic>acrD</jats:italic> and <jats:italic>acrF</jats:italic> that were associated with <jats:italic>acrR</jats:italic> and <jats:italic>marR</jats:italic> mutations and <jats:italic>sdiA</jats:italic> overexpression, together with mutations A233T and I332V in FtSI (PBP3) resulted in ceftazidime resistance in Caz/20-2, multiplying by 128-fold the ceftazidime MIC in the parental clinical isolate PS/20. Absence of detectable β-lactamase hydrolytic activity in the crude extract of Caz/20-2 was observed, and coincided with Q191K and P209S mutations in AmpC and a nucleotide substitution at −28 in the <jats:italic>ampC</jats:italic> promoter, whereas β-lactamase hydrolytic activity in crude extracts of PS/20 and Caz/20-1 strains was detected. Nevertheless, a fourfold increase in ceftazidime MIC in Caz/20-1 compared with that in PS/20 was due to the increased transcript level of <jats:italic>acrB</jats:italic> derived from <jats:italic>acrR</jats:italic> mutation. The two Caz mutants and PS/20 showed the same mutations in AmpG and ParE.</jats:p>
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spelling Tavío, María M. Aquili, Virginia D. Vila, Jordi Poveda, José B. 0022-2615 1473-5644 Microbiology Society Microbiology (medical) General Medicine Microbiology http://dx.doi.org/10.1099/jmm.0.063727-0 <jats:p>The mechanisms responsible for the increase in ceftazidime MIC in two <jats:italic>Escherichia coli in vitro</jats:italic> selected mutants, Caz/20-1 and Caz/20-2, were studied. OmpF loss and overexpression of <jats:italic>acrB</jats:italic>, <jats:italic>acrD</jats:italic> and <jats:italic>acrF</jats:italic> that were associated with <jats:italic>acrR</jats:italic> and <jats:italic>marR</jats:italic> mutations and <jats:italic>sdiA</jats:italic> overexpression, together with mutations A233T and I332V in FtSI (PBP3) resulted in ceftazidime resistance in Caz/20-2, multiplying by 128-fold the ceftazidime MIC in the parental clinical isolate PS/20. Absence of detectable β-lactamase hydrolytic activity in the crude extract of Caz/20-2 was observed, and coincided with Q191K and P209S mutations in AmpC and a nucleotide substitution at −28 in the <jats:italic>ampC</jats:italic> promoter, whereas β-lactamase hydrolytic activity in crude extracts of PS/20 and Caz/20-1 strains was detected. Nevertheless, a fourfold increase in ceftazidime MIC in Caz/20-1 compared with that in PS/20 was due to the increased transcript level of <jats:italic>acrB</jats:italic> derived from <jats:italic>acrR</jats:italic> mutation. The two Caz mutants and PS/20 showed the same mutations in AmpG and ParE.</jats:p> Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA Journal of Medical Microbiology
spellingShingle Tavío, María M., Aquili, Virginia D., Vila, Jordi, Poveda, José B., Journal of Medical Microbiology, Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA, Microbiology (medical), General Medicine, Microbiology
title Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_full Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_fullStr Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_full_unstemmed Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_short Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
title_sort resistance to ceftazidime in escherichia coli associated with acrr, marr and pbp3 mutations and overexpression of sdia
title_unstemmed Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
topic Microbiology (medical), General Medicine, Microbiology
url http://dx.doi.org/10.1099/jmm.0.063727-0