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Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI
The amikacin resistance gene aphA6 was first detected in the nosocomial pathogen Acinetobacter baumannii and subsequently in other genera. Analysis of 133 whole-genome sequences covering the taxonomic diversity of Acinetobacter spp. detected aphA6 in the chromosome of 2 isolates of A. guillouiae, wh...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society of Microbiology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4212838/ https://www.ncbi.nlm.nih.gov/pubmed/25336457 http://dx.doi.org/10.1128/mBio.01972-14 |
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author | Yoon, Eun-Jeong Goussard, Sylvie Touchon, Marie Krizova, Lenka Cerqueira, Gustavo Murphy, Cheryl Lambert, Thierry Grillot-Courvalin, Catherine Nemec, Alexandr Courvalin, Patrice |
author_facet | Yoon, Eun-Jeong Goussard, Sylvie Touchon, Marie Krizova, Lenka Cerqueira, Gustavo Murphy, Cheryl Lambert, Thierry Grillot-Courvalin, Catherine Nemec, Alexandr Courvalin, Patrice |
author_sort | Yoon, Eun-Jeong |
collection | PubMed |
description | The amikacin resistance gene aphA6 was first detected in the nosocomial pathogen Acinetobacter baumannii and subsequently in other genera. Analysis of 133 whole-genome sequences covering the taxonomic diversity of Acinetobacter spp. detected aphA6 in the chromosome of 2 isolates of A. guillouiae, which is an environmental species, 1 of 8 A. parvus isolates, and 5 of 34 A. baumannii isolates. The gene was also present in 29 out of 36 A. guillouiae isolates screened by PCR, indicating that it is ancestral to this species. The P(native) promoter for aphA6 in A. guillouiae and A. parvus was replaced in A. baumannii by P(aphA6), which was generated by use of the insertion sequence ISAba125, which brought a −35 sequence. Study of promoter strength in Escherichia coli and A. baumannii indicated that P(aphA6) was four times more potent than P(native). There was a good correlation between aminoglycoside MICs and aphA6 transcription in A. guillouiae isolates that remained susceptible to amikacin. The marked topology differences of the phylogenetic trees of aphA6 and of the hosts strongly support its recent direct transfer within Acinetobacter spp. and also to evolutionarily remote bacterial genera. Concomitant expression of aphA6 must have occurred because, contrary to the donors, it can confer resistance to the new hosts. Mobilization and expression of aphA6 via composite transposons and the upstream IS-generating hybrid P(aphA6), followed by conjugation, seems the most plausible mechanism. This is in agreement with the observation that, in the recipients, aphA6 is carried by conjugative plasmids and flanked by IS that are common in Acinetobacter spp. Our data indicate that resistance genes can also be found in susceptible environmental bacteria. |
format | Online Article Text |
id | pubmed-4212838 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American Society of Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42128382014-11-03 Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI Yoon, Eun-Jeong Goussard, Sylvie Touchon, Marie Krizova, Lenka Cerqueira, Gustavo Murphy, Cheryl Lambert, Thierry Grillot-Courvalin, Catherine Nemec, Alexandr Courvalin, Patrice mBio Research Article The amikacin resistance gene aphA6 was first detected in the nosocomial pathogen Acinetobacter baumannii and subsequently in other genera. Analysis of 133 whole-genome sequences covering the taxonomic diversity of Acinetobacter spp. detected aphA6 in the chromosome of 2 isolates of A. guillouiae, which is an environmental species, 1 of 8 A. parvus isolates, and 5 of 34 A. baumannii isolates. The gene was also present in 29 out of 36 A. guillouiae isolates screened by PCR, indicating that it is ancestral to this species. The P(native) promoter for aphA6 in A. guillouiae and A. parvus was replaced in A. baumannii by P(aphA6), which was generated by use of the insertion sequence ISAba125, which brought a −35 sequence. Study of promoter strength in Escherichia coli and A. baumannii indicated that P(aphA6) was four times more potent than P(native). There was a good correlation between aminoglycoside MICs and aphA6 transcription in A. guillouiae isolates that remained susceptible to amikacin. The marked topology differences of the phylogenetic trees of aphA6 and of the hosts strongly support its recent direct transfer within Acinetobacter spp. and also to evolutionarily remote bacterial genera. Concomitant expression of aphA6 must have occurred because, contrary to the donors, it can confer resistance to the new hosts. Mobilization and expression of aphA6 via composite transposons and the upstream IS-generating hybrid P(aphA6), followed by conjugation, seems the most plausible mechanism. This is in agreement with the observation that, in the recipients, aphA6 is carried by conjugative plasmids and flanked by IS that are common in Acinetobacter spp. Our data indicate that resistance genes can also be found in susceptible environmental bacteria. American Society of Microbiology 2014-10-21 /pmc/articles/PMC4212838/ /pubmed/25336457 http://dx.doi.org/10.1128/mBio.01972-14 Text en Copyright © 2014 Yoon et al. http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license (http://creativecommons.org/licenses/by-nc-sa/3.0/) , which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Yoon, Eun-Jeong Goussard, Sylvie Touchon, Marie Krizova, Lenka Cerqueira, Gustavo Murphy, Cheryl Lambert, Thierry Grillot-Courvalin, Catherine Nemec, Alexandr Courvalin, Patrice Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI |
title | Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI |
title_full | Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI |
title_fullStr | Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI |
title_full_unstemmed | Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI |
title_short | Origin in Acinetobacter guillouiae and Dissemination of the Aminoglycoside-Modifying Enzyme Aph(3′)-VI |
title_sort | origin in acinetobacter guillouiae and dissemination of the aminoglycoside-modifying enzyme aph(3′)-vi |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4212838/ https://www.ncbi.nlm.nih.gov/pubmed/25336457 http://dx.doi.org/10.1128/mBio.01972-14 |
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