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Resistance to ceftazidime in Escherichia coli associated with AcrR, MarR and PBP3 mutations and overexpression of sdiA
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Zeitschriftentitel: | Journal of Medical Microbiology |
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Personen und Körperschaften: | , , , |
In: | Journal of Medical Microbiology, 63, 2014, 1, S. 56-65 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Microbiology Society
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Schlagwörter: |
author_facet |
Tavío, María M. Aquili, Virginia D. Vila, Jordi Poveda, José B. Tavío, María M. Aquili, Virginia D. Vila, Jordi Poveda, José B. |
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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 |
doi_str_mv |
10.1099/jmm.0.063727-0 |
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Biologie |
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Microbiology Society, 2014 |
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Microbiology Society, 2014 |
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Microbiology Society |
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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. |
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container_title | Journal of Medical Microbiology |
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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 |