Site-specific recombination at XerC/D sites mediates the formation and resolution of plasmid co-integrates carrying a blaOXA-58- and TnaphA6-resistance module in Acinetobacter baumannii

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dc.citation.titleFrontiers in Microbiology
dc.citation.volume9
dc.creatorCameranesi, María Marcela
dc.creatorMorán Barrio, Jorgelina
dc.creatorLimansky, Adriana S.
dc.creatorRepizo, Guillermo Daniel
dc.creatorViale, Alejandro M.
dc.date.accessioned2021-03-10T17:57:13Z
dc.date.available2021-03-10T17:57:13Z
dc.date.issued2018-01-26
dc.descriptionMembers of the genus Acinetobacter possess distinct plasmid types which provide effective platforms for the acquisition, evolution, and dissemination of antimicrobial resistance structures. Many plasmid-borne resistance structures are bordered by short DNA sequences providing potential recognition sites for the host XerC and XerD site-specific tyrosine recombinases (XerC/D-like sites). However, whether these sites are active in recombination and how they assist the mobilization of associated resistance structures is still poorly understood. Here we characterized the plasmids carried by Acinetobacter baumannii Ab242, a multidrug-resistant clinical strain belonging to the ST104 (Oxford scheme) which produces an OXA-58 carbapenem-hydrolyzing class-D β-lactamase (CHDL). Plasmid sequencing and characterization of replication, stability, and adaptive modules revealed the presence in Ab242 of three novel plasmids lacking self-transferability functions which were designated pAb242_9, pAb242_12, and pAb242_25, respectively. Among them, only pAb242_25 was found to carry an adaptive module encompassing an ISAba825-blaOXA-58 arrangement accompanied by a TnaphA6 transposon, the whole structure conferring simultaneous resistance to carbapenems and aminoglycosides. Ab242 plasmids harbor several XerC/D-like sites, with most sites found in pAb242_25 located in the vicinity or within the adaptive module described above. Electrotransformation of susceptible A. nosocomialis cells with Ab242 plasmids followed by imipenem selection indicated that the transforming plasmid form was a co-integrate resulting from the fusion of pAb242_25 and pAb242_12. Further characterization by cloning and sequencing studies indicated that a XerC/D site in pAb242_25 and another in pAb242_12 provided the active sister pair for the inter-molecular site-specific recombination reaction mediating the fusion of these two plasmids. Moreover, the resulting co-integrate was found also to undergo intra-molecular resolution at the new pair of XerC/D sites generated during fusion thus regenerating the original pAb242_25 and pAb242_12 plasmids. These observations provide the irst evidence indicating that XerC/D-like sites in A. baumannii plasmids can provide active pairs for site-specific recombination mediating inter-molecular fusions and intra molecular resolutions. The overall results shed light on the evolutionary dynamics of A. baumannii plasmids and the underlying mechanisms of dissemination of genetic structures responsible for carbapenem and other antibiotics resistance among the Acinetobacter clinical population.es
dc.descriptionPara citar este articulo: Cameranesi MM, Morán-Barrio J, Limansky AS, Repizo GD and Viale AM (2018) Site-Specific Recombination at XerC/D Sites Mediates the Formation and Resolution of Plasmid Co-integrates Carrying a blaOXA-58- and TnaphA6-Resistance Module in Acinetobacter baumannii. Front. Microbiol. 9:66. doi: 10.3389/fmicb.2018.00066
dc.description.filFil: Cameranesi, María Marcela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.
dc.description.filFil: Cameranesi, María Marcela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: Morán Barrio, Jorgelina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.
dc.description.filFil: Morán Barrio, Jorgelina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: Limansky, Adriana S. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.
dc.description.filFil: Limansky, Adriana S. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: Repizo, Guillermo Daniel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.
dc.description.filFil: Repizo, Guillermo Daniel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: Viale, Alejandro M. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.
dc.description.filFil: Viale, Alejandro M. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT): PICT-2011-1020 y PICT-2012-0680es
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET): PIP 1055es
dc.description.sponsorshipMinisterio de Ciencia, Tecnología e Innovación Productiva (MINCTIP)es
dc.formatapplication/pdf
dc.format.extent1-14
dc.identifier.issn1664-302X
dc.identifier.urihttp://hdl.handle.net/2133/20110
dc.language.isoenges
dc.publisherFrontiers Mediaes
dc.relation.publisherversionhttps://doi.org/10.3389/fmicb.2018.00066es
dc.relation.publisherversionhttps://www.frontiersin.org/articles/10.3389/fmicb.2018.00066/fulles
dc.rightsopenAccesses
dc.rights.holderUniversidad Nacional de Rosarioes
dc.rights.holderCameranesi, María Marcelaes
dc.rights.holderMorán-Barrio, Jorgelinaes
dc.rights.holderLimansky, Adriana S.es
dc.rights.holderRepizo, Guillermo Danieles
dc.rights.holderViale, Alejandro M.es
dc.rights.textAttribution 4.0 International (CC BY 4.0)es
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subjectAcinetobacter baumanniies
dc.subjectblaOXA-58es
dc.subjectCarbapenems Resistancees
dc.subjectXerC/Des
dc.subjectSite-specific Recombinationes
dc.subjectAntimicrobial Resistance Plasmidses
dc.titleSite-specific recombination at XerC/D sites mediates the formation and resolution of plasmid co-integrates carrying a blaOXA-58- and TnaphA6-resistance module in Acinetobacter baumanniies
dc.typepublishedVersion

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