Matches in SemOpenAlex for { <https://semopenalex.org/work/W2981600465> ?p ?o ?g. }
Showing items 1 to 70 of
70
with 100 items per page.
- W2981600465 abstract "Abstract Background The YycFG system is an essential two-component regulatory system involved in cell wall homeostasis associated with the development of daptomycin (DAP) resistance in E. faecium. Importantly, the standard combination of DAP plus β-lactam is ineffective against strains harboring mutations in yycFG. Transcriptional profiling identified a cluster of two genes (xpaC and telA) that is upregulated in the presence of a YycGS333L substitution. xpaC and telA are annotated as 5-bromo-4-chloroindolyl phosphate hydrolysis and tellurite resistance proteins, respectively. Here, we aimed to determine the contribution of xpaC and telA in DAP resistance. Methods Non-polar in-frame deletions of xpaC/telA and complementation of xpaC were performed in clinical strain E. faecium R446RIF. All mutants were characterized by PFGE and sequencing of the open reading frames to confirm the deletion. DAP MIC determination was performed by Etest on Mueller–Hinton agar. Binding of DAP was evaluated using BODIPY-labeled DAP (BDP-DAP). Cell membrane phospholipid microdomains were visualized using 10-N-nonyl acridine orange. All assays were compared with a DAP-susceptible clinical E. faecium strain S447. Results R446RIFΔ telA and R446RIFΔ xpaCtelA did not alter DAP MICs in R446RIF (24–32 μg/mL). However, deletion of xpaC alone (R446RIFΔ xpaC) markedly decreased DAP MIC 8 fold (to 4 μg/mL). R446RIFΔ telA and R446RIFΔ xpaCtelA exhibited similar binding of BDP-DAP compared with parental R446RIF. In contrast, R446RIFΔ xpaC exhibited increased binding of the antibiotic molecule to the cell membrane, similar to that of DAP-susceptible S447. Complementation of xpaC restored DAP MIC to 32–48 µg/mL and decrease binding of DAP. NAO staining of S447, R446RIF, R446RIFΔ telA, R446RIFΔ xpaCtelA, and R446RIFΔ xpaC:: xpaC displayed septal and polar distribution. In stark contrast, R446RIFΔ xpaC showed a redistribution of phospholipid microdomains away from the septa. Conclusion XpaC is a key contributor to DAP binding and phospholipid architecture of E. faecium but only in the presence of an intact TelA. The xpaC and telA gene cluster is a novel mediator of DAP-resistance in E. faecium via theYycFG system and independent of the LiaFSR system Disclosures All authors: No reported disclosures." @default.
- W2981600465 created "2019-11-01" @default.
- W2981600465 creator A5012936100 @default.
- W2981600465 creator A5027587575 @default.
- W2981600465 creator A5056575626 @default.
- W2981600465 creator A5075229057 @default.
- W2981600465 creator A5080138941 @default.
- W2981600465 date "2019-10-01" @default.
- W2981600465 modified "2023-09-30" @default.
- W2981600465 title "601. TelA and XpaC Are Novel Mediators of Daptomycin Resistance in Enterococcus faecium" @default.
- W2981600465 doi "https://doi.org/10.1093/ofid/ofz360.670" @default.
- W2981600465 hasPublicationYear "2019" @default.
- W2981600465 type Work @default.
- W2981600465 sameAs 2981600465 @default.
- W2981600465 citedByCount "0" @default.
- W2981600465 crossrefType "journal-article" @default.
- W2981600465 hasAuthorship W2981600465A5012936100 @default.
- W2981600465 hasAuthorship W2981600465A5027587575 @default.
- W2981600465 hasAuthorship W2981600465A5056575626 @default.
- W2981600465 hasAuthorship W2981600465A5075229057 @default.
- W2981600465 hasAuthorship W2981600465A5080138941 @default.
- W2981600465 hasBestOaLocation W29816004651 @default.
- W2981600465 hasConcept C104317684 @default.
- W2981600465 hasConcept C153911025 @default.
- W2981600465 hasConcept C167625842 @default.
- W2981600465 hasConcept C2777677444 @default.
- W2981600465 hasConcept C2778651397 @default.
- W2981600465 hasConcept C2778980435 @default.
- W2981600465 hasConcept C2779489039 @default.
- W2981600465 hasConcept C47289529 @default.
- W2981600465 hasConcept C501593827 @default.
- W2981600465 hasConcept C523546767 @default.
- W2981600465 hasConcept C54355233 @default.
- W2981600465 hasConcept C55493867 @default.
- W2981600465 hasConcept C71924100 @default.
- W2981600465 hasConcept C86803240 @default.
- W2981600465 hasConcept C89423630 @default.
- W2981600465 hasConceptScore W2981600465C104317684 @default.
- W2981600465 hasConceptScore W2981600465C153911025 @default.
- W2981600465 hasConceptScore W2981600465C167625842 @default.
- W2981600465 hasConceptScore W2981600465C2777677444 @default.
- W2981600465 hasConceptScore W2981600465C2778651397 @default.
- W2981600465 hasConceptScore W2981600465C2778980435 @default.
- W2981600465 hasConceptScore W2981600465C2779489039 @default.
- W2981600465 hasConceptScore W2981600465C47289529 @default.
- W2981600465 hasConceptScore W2981600465C501593827 @default.
- W2981600465 hasConceptScore W2981600465C523546767 @default.
- W2981600465 hasConceptScore W2981600465C54355233 @default.
- W2981600465 hasConceptScore W2981600465C55493867 @default.
- W2981600465 hasConceptScore W2981600465C71924100 @default.
- W2981600465 hasConceptScore W2981600465C86803240 @default.
- W2981600465 hasConceptScore W2981600465C89423630 @default.
- W2981600465 hasLocation W29816004651 @default.
- W2981600465 hasLocation W29816004652 @default.
- W2981600465 hasOpenAccess W2981600465 @default.
- W2981600465 hasPrimaryLocation W29816004651 @default.
- W2981600465 hasRelatedWork W13323693 @default.
- W2981600465 hasRelatedWork W15764473 @default.
- W2981600465 hasRelatedWork W17659408 @default.
- W2981600465 hasRelatedWork W18221546 @default.
- W2981600465 hasRelatedWork W18739995 @default.
- W2981600465 hasRelatedWork W20309204 @default.
- W2981600465 hasRelatedWork W4255431 @default.
- W2981600465 hasRelatedWork W5320784 @default.
- W2981600465 hasRelatedWork W5512804 @default.
- W2981600465 hasRelatedWork W6680445 @default.
- W2981600465 isParatext "false" @default.
- W2981600465 isRetracted "false" @default.
- W2981600465 magId "2981600465" @default.
- W2981600465 workType "article" @default.