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A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination

The emergence and spread of antibiotic resistance among Acinetobacter spp. have been investigated extensively. Most studies focused on the multiple antibiotic resistance genes located on plasmids or genomic resistance islands. On the other hand, the mechanisms controlling intrinsic resistance are st...

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Autores principales: Zhang, Gang, Leclercq, Sébastien Olivier, Tian, Jingjing, Wang, Chao, Yahara, Koji, Ai, Guomin, Liu, Shuangjiang, Feng, Jie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5313234/
https://www.ncbi.nlm.nih.gov/pubmed/28152054
http://dx.doi.org/10.1371/journal.pgen.1006602
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author Zhang, Gang
Leclercq, Sébastien Olivier
Tian, Jingjing
Wang, Chao
Yahara, Koji
Ai, Guomin
Liu, Shuangjiang
Feng, Jie
author_facet Zhang, Gang
Leclercq, Sébastien Olivier
Tian, Jingjing
Wang, Chao
Yahara, Koji
Ai, Guomin
Liu, Shuangjiang
Feng, Jie
author_sort Zhang, Gang
collection PubMed
description The emergence and spread of antibiotic resistance among Acinetobacter spp. have been investigated extensively. Most studies focused on the multiple antibiotic resistance genes located on plasmids or genomic resistance islands. On the other hand, the mechanisms controlling intrinsic resistance are still not well understood. In this study, we identified the novel subclass of aminoglycoside nucleotidyltransferase ANT(3")-II in Acinetobacter spp., which comprised numerous variants distributed among three main clades. All members of this subclass can inactivate streptomycin and spectinomycin. The three ant(3")-II genes, encoding for the three ANT(3")-II clades, are widely distributed in the genus Acinetobacter and always located in the same conserved genomic region. According to their prevalence, these genes are intrinsic in Acinetobacter baumannii, Acinetobacter pittii, and Acinetobacter gyllenbergii. We also demonstrated that the ant(3")-II genes are located in a homologous recombination hotspot and were recurrently transferred among Acinetobacter species. In conclusion, our findings demonstrated a novel mechanism of natural resistance in Acinetobacter spp., identified a novel subclass of aminoglycoside nucleotidyltransferase and provided new insight into the evolutionary history of intrinsic resistance genes.
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spelling pubmed-53132342017-03-03 A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination Zhang, Gang Leclercq, Sébastien Olivier Tian, Jingjing Wang, Chao Yahara, Koji Ai, Guomin Liu, Shuangjiang Feng, Jie PLoS Genet Research Article The emergence and spread of antibiotic resistance among Acinetobacter spp. have been investigated extensively. Most studies focused on the multiple antibiotic resistance genes located on plasmids or genomic resistance islands. On the other hand, the mechanisms controlling intrinsic resistance are still not well understood. In this study, we identified the novel subclass of aminoglycoside nucleotidyltransferase ANT(3")-II in Acinetobacter spp., which comprised numerous variants distributed among three main clades. All members of this subclass can inactivate streptomycin and spectinomycin. The three ant(3")-II genes, encoding for the three ANT(3")-II clades, are widely distributed in the genus Acinetobacter and always located in the same conserved genomic region. According to their prevalence, these genes are intrinsic in Acinetobacter baumannii, Acinetobacter pittii, and Acinetobacter gyllenbergii. We also demonstrated that the ant(3")-II genes are located in a homologous recombination hotspot and were recurrently transferred among Acinetobacter species. In conclusion, our findings demonstrated a novel mechanism of natural resistance in Acinetobacter spp., identified a novel subclass of aminoglycoside nucleotidyltransferase and provided new insight into the evolutionary history of intrinsic resistance genes. Public Library of Science 2017-02-02 /pmc/articles/PMC5313234/ /pubmed/28152054 http://dx.doi.org/10.1371/journal.pgen.1006602 Text en © 2017 Zhang et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Zhang, Gang
Leclercq, Sébastien Olivier
Tian, Jingjing
Wang, Chao
Yahara, Koji
Ai, Guomin
Liu, Shuangjiang
Feng, Jie
A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination
title A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination
title_full A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination
title_fullStr A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination
title_full_unstemmed A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination
title_short A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3")-II, is horizontally transferred among Acinetobacter spp. by homologous recombination
title_sort new subclass of intrinsic aminoglycoside nucleotidyltransferases, ant(3")-ii, is horizontally transferred among acinetobacter spp. by homologous recombination
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5313234/
https://www.ncbi.nlm.nih.gov/pubmed/28152054
http://dx.doi.org/10.1371/journal.pgen.1006602
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