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dc.contributor.authorTran, Truc T.
dc.contributor.authorMishra, Nagendra Nath
dc.contributor.authorSeepersaud, Ravin
dc.contributor.authorDiaz, Lorena
dc.contributor.authorDinh, An Q.
dc.contributor.authorGarcía-De-La-Mària, Cristina
dc.contributor.authorRybak, Michael Joseph
dc.contributor.authorMiró, José María
dc.contributor.authorShelburne, Samuel A.
dc.contributor.authorShelburne, Samuel A.
dc.contributor.authorSullam, Paul M.
dc.contributor.authorBayer, Arnold S.
dc.contributor.authorArias, César A.
dc.date.accessioned2020-03-27T17:11:57Z
dc.date.available2020-03-27T17:11:57Z
dc.identifier.issn1098-6596spa
dc.identifier.urihttp://hdl.handle.net/20.500.12495/2170
dc.format.mimetypeapplication/pdfspa
dc.language.isoengspa
dc.publisherAmerican society for microbiologyspa
dc.relation.ispartofseriesAntimicrobial agents and chemotherapy, 1098-6596, Vol. 63, Nro. 2, 2019, p. e01531-18spa
dc.relation.urihttps://aac.asm.org/content/63/2/e01531-18.abstractspa
dc.titleMutations in cdsA and pgsA Correlate with Daptomycin Resistance in Streptococcus mitis and S. Oralisspa
dc.typearticlespa
dc.type.localartículospa
dc.subject.decsStreptococcus mitispa
dc.subject.decsCardiolipinasspa
dc.subject.decsDaptomicinaspa
dc.subject.keywordsCdsAspa
dc.subject.keywordsPgsAspa
dc.subject.keywordsDaptomycin resistancespa
dc.identifier.doihttps://doi.org/10.1128/AAC.01531-18spa
dc.type.hasversioninfo:eu-repo/semantics/publishedVersion
dc.publisher.journalAntimicrobial agents and chemotherapyspa
dc.identifier.instnameinstname:Universidad El Bosquespa
dc.identifier.reponamereponame: Repositorio Institucional Universidad El Bosquespa
dc.identifier.repourlrepourl:https://repositorio.unbosque.edu.cospa
dc.description.abstractenglishWe investigated the ability of several recent clinical viridans group streptococci (VGS) bloodstream isolates (Streptococcus mitis/S. oralis subgroup) from daptomycin (DAP)-naive patients to develop DAP resistance in vitro. All strains rapidly developed high-level and stable DAP resistance. Substitutions in two enzymes involved in the cardiolipin biosynthesis pathway were identified, i.e., CdsA (phosphatidate cytidylyltransferase) and PgsA (CDP-diacylglycerol-glycerol-3-phosphate-3phosphatidyltransferase). These mutations were associated with complete disappearance of phosphatidylglycerol and cardiolipin from cell membranes. DAP interactions with the cell membrane differed in isolates with PgsA versus CdsA substitutionsspa
dc.rights.localAcceso cerradospa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.accessrightshttp://purl.org/coar/access_right/c_abf328spa
dc.date.issued2019


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