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

DSpace/Manakin Repository

Show simple item record

dc.creator Cameranesi, Marcela
dc.creator Morán-Barrio, Jorgelina
dc.creator Limansky, Adriana S.
dc.creator Repizo, Guillermo Daniel
dc.creator Viale, Alejandro M.
dc.date.accessioned 2021-03-10T17:57:13Z
dc.date.available 2021-03-10T17:57:13Z
dc.date.issued 2018-01-26
dc.identifier.issn 1664-302X
dc.identifier.uri http://hdl.handle.net/2133/20110
dc.description Members 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.description Para 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.sponsorship Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT): PICT-2011-1020 y PICT-2012-0680 es
dc.description.sponsorship Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET): PIP 1055 es
dc.description.sponsorship Ministerio de Ciencia, Tecnología e Innovación Productiva (MINCTIP) es
dc.format application/pdf
dc.format.extent 1-14
dc.language.iso eng es
dc.publisher Frontiers Media es
dc.rights openAccess es
dc.rights.uri https://creativecommons.org/licenses/by/4.0/ *
dc.subject Acinetobacter baumannii es
dc.subject blaOXA-58 es
dc.subject Carbapenems Resistance es
dc.subject XerC/D es
dc.subject Site-specific Recombination es
dc.subject Antimicrobial Resistance Plasmids es
dc.title 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 es
dc.type publishedVersion
dc.rights.holder Universidad Nacional de Rosario es
dc.rights.holder Cameranesi, Marcela es
dc.rights.holder Morán-Barrio, Jorgelina es
dc.rights.holder Limansky, Adriana S. es
dc.rights.holder Repizo, Guillermo Daniel es
dc.rights.holder Viale, Alejandro M. es
dc.relation.publisherversion https://doi.org/10.3389/fmicb.2018.00066 es
dc.relation.publisherversion https://www.frontiersin.org/articles/10.3389/fmicb.2018.00066/full es
dc.rights.text Attribution 4.0 International (CC BY 4.0) es
dc.citation.title Frontiers in Microbiology
dc.citation.volume 9
dc.description.fil Fil: Cameranesi, Marcela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.
dc.description.fil Fil: Cameranesi, Marcela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.fil Fil: 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.fil Fil: Morán-Barrio, Jorgelina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.fil Fil: 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.fil Fil: Limansky, Adriana S. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.fil Fil: 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.fil Fil: Repizo, Guillermo Daniel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.fil Fil: 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.fil Fil: Viale, Alejandro M. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.


Files in this item

The following license files are associated with this item:

This item appears in the following Collection(s)

Show simple item record

openAccess Except where otherwise noted, this item's license is described as openAccess

My Account


Search DSpace


Browse