Comparative genomic analysis of <i>Acinetobacter</i> spp. plasmids originating from clinical settings and environmental habitats

Bacteria belonging to the genus <i>Acinetobacter</i> have become of clinical importance over the last decade due to the development of a multi-resistant phenotype and their ability to survive under multiple environmental conditions. The development of these traits among <i>Acinetob...

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Autores principales: Salto, Ileana Paula, Torres Tejerizo, Gonzalo Arturo, Wibberg, Daniel, Pühler, Alfred, Schlüter, Andreas, Pistorio, Mariano
Formato: Articulo
Lenguaje:Inglés
Publicado: 2018
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/104526
http://hdl.handle.net/11336/96690
https://www.nature.com/articles/s41598-018-26180-3
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Sumario:Bacteria belonging to the genus <i>Acinetobacter</i> have become of clinical importance over the last decade due to the development of a multi-resistant phenotype and their ability to survive under multiple environmental conditions. The development of these traits among <i>Acinetobacter</i> strains occurs frequently as a result of plasmid-mediated horizontal gene transfer. In this work, plasmids from nosocomial and environmental <i>Acinetobacter</i> spp. collections were separately sequenced and characterized. Assembly of the sequenced data resulted in 19 complete replicons in the nosocomial collection and 77 plasmid contigs in the environmental collection. Comparative genomic analysis showed that many of them had conserved backbones. Plasmid coding sequences corresponding to plasmid specific functions were bioinformatically and functionally analyzed. Replication initiation protein analysis revealed the predominance of the Rep_3 superfamily. The phylogenetic tree constructed from all <i>Acinetobacter</i> Rep_3 superfamily plasmids showed 16 intermingled clades originating from nosocomial and environmental habitats. Phylogenetic analysis of relaxase proteins revealed the presence of a new sub-clade named MOBQ<sub>Aci</sub>, composed exclusively of <i>Acinetobacter</i> relaxases. Functional analysis of proteins belonging to this group showed that they behaved differently when mobilized using helper plasmids belonging to different incompatibility groups.