The ompW (porin) gene mediates methyl viologen (paraquat) efflux in Salmonella enterica serovar Typhimurium

Gil, Fernando; Ipinza, Francisco; Fuentes, Juan A.; Fumeron, Robinson; Villarreal, José Miguel; Aspée, Alexis; Mora, Gabriela; Vásquez, Claudio C.; Saavedra, Claudia P.

doi:10.1016/j.resmic.2007.05.004

Cited by 54 publications

(55 citation statements)

References 29 publications

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“…Additionally, the overexpression of OmpW was previously observed in another spontaneous Shigella boydii azithromycinresistant mutant obtained in the absence of PAbN (Gomes et al, 2013b). These data suggest the role of OmpW as an extrusion way of azithromycin as has been proposed for other substances (Gil et al, 2007). The overexpression of OmpW might be a collateral reflection of alterations of series of metabolic cascades.…”

Section: Chromosomal Efflux Pumpssupporting

confidence: 60%

Macrolide resistance mechanisms inEnterobacteriaceae: Focus on azithromycin

Gomes

Martínez-Puchol

Palma

et al. 2016

Critical Reviews in Microbiology

116

120

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Section: Chromosomal Efflux Pumpssupporting

confidence: 60%

Macrolide resistance mechanisms inEnterobacteriaceae: Focus on azithromycin

Gomes

Martínez-Puchol

Palma

et al. 2016

Critical Reviews in Microbiology

116

120

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“…Since the majority of known EmrE substrates are antimicrobial QCC, it was essential to confirm if the newly identified OmpW also conferred QCC resistance when overaccumulated with EmrE. A previous study demonstrated that overexpression of ompW in Salmonella enterica serovar Typhimurium contributed to MV resistance (28). MV is a QCC herbicide and a well-known substrate of EmrE; therefore, this compound was selected for further drug resistance assays.…”

Section: Resultsmentioning

confidence: 99%

“…This approach served as an ideal screening method to identify whether an OMP was associated with EmrE efflux, since it avoided the use of QCC potentially transported by other redundant multidrug efflux systems that possess overlapping substrate profiles (such as AcrAB-TolC and MdfA) (9,16). OmpW was one of the most likely candidates prior to these studies, based on its involvement in host MV resistance and osmotic tolerance in other Gram-negative bacteria (28,29,30,31). Taken altogether, this study provides the first evidence of OMP association with EmrE-mediated host drug resistance.…”

Section: Discussionmentioning

confidence: 99%

Outer Membrane Protein OmpW Participates with Small Multidrug Resistance Protein Member EmrE in Quaternary Cationic Compound Efflux

2014

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In Escherichia coli, the small multidrug resistance (SMR) transporter protein EmrE confers host resistance to a broad range of toxic quaternary cation compounds (QCC) via proton motive force in the plasma membrane. Biologically produced QCC also act as EmrE osmoprotectant substrates within the cell and participate in host pH regulation and osmotic tolerance. Although E. coli EmrE is one of the most well-characterized SMR members, it is unclear how the substrates it transports into the periplasm escape across the outer membrane (OM) in Gram-negative bacteria. We tested the hypothesis that E. coli EmrE relies on an unidentified OM protein (OMP) to complete the extracellular release of its QCC. Eleven OMP candidates were screened using an alkaline phenotypic growth assay to identify OMP involvement in EmrE-mediated QCC efflux. E. coli single-gene deletion strains were transformed with plasmid-carried copies of emrE to detect reduced-growth and rescued-growth phenotypes under alkaline conditions. Among the 11 candidates, only the ⌬ompW strain showed rescued alkaline growth tolerance when transformed with pEmrE, supporting the corresponding protein's involvement in EmrE osmoprotectant efflux. Coexpression of plasmids carrying the ompW and emrE genes transformed into the E. coli ⌬ompW and ⌬emrE strains demonstrated a functional complementation restoring the original alkaline loss-of-growth phenotype. Methyl viologen drug resistance assays of pEmrE and pOmpW plasmid-complemented E. coli ⌬ompW and wild-type strains found higher host drug resistance than with other plasmid combinations. This study confirms our hypothesis that the porin OmpW participates in the efflux of EmrE-specific substrates across the OM.

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“…Recently, we performed proteomic analysis of the NT80 membrane fraction and found that stearyl alcohol induced expression of OmpW family proteins (unpublished data). OmpW is involved in protecting bacteria from various environmental stresses (Nandi et al, 2005;Gil et al, 2007). Thus, it is possible that stearyl-alcohol-induced OmpW expression may also help in maintaining cell viability.…”

Section: Discussionmentioning

confidence: 99%

EliA is required for inducing the stearyl alcohol-mediated expression of secretory proteins and production of polyester in Ralstonia sp. NT80

et al. 2016

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Addition of stearyl alcohol to the culture medium of Ralstonia sp. NT80 induced expression of a significant amount of secretory lipase. Comparative proteomic analysis of extracellular proteins from NT80 cells grown in the presence or absence of stearyl alcohol revealed that stearyl alcohol induced expression of several secretory proteins including lipase, haemolysin-coregulated protein and nucleoside diphosphate kinase. Expression of these secreted proteins was upregulated at the transcriptional level. Stearyl alcohol also induced the synthesis of polyhydroxyalkanoate. Secretory protein EliA was required for all these responses of NT80 cells to stearyl alcohol. Accordingly, the effects of stearyl alcohol were significantly reduced in the eliA deletion mutant cells of NT80 (DeliA). The remaining concentration of stearyl alcohol in the culture supernatant of the wild-type cells, but not that in the culture supernatant of the DeliA cells, clearly decreased during the course of growth. These observed phenotypes of the DeliA mutant were rescued by gene complementation. The results suggested that EliA is essential for these cells to respond to stearyl alcohol, and that it plays an important role in the recognition and assimilation of stearyl alcohol by NT80 cells.

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The ompW (porin) gene mediates methyl viologen (paraquat) efflux in Salmonella enterica serovar Typhimurium

Cited by 54 publications

References 29 publications

Macrolide resistance mechanisms inEnterobacteriaceae: Focus on azithromycin

Macrolide resistance mechanisms inEnterobacteriaceae: Focus on azithromycin

Outer Membrane Protein OmpW Participates with Small Multidrug Resistance Protein Member EmrE in Quaternary Cationic Compound Efflux

EliA is required for inducing the stearyl alcohol-mediated expression of secretory proteins and production of polyester in Ralstonia sp. NT80

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