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

Fernando Gil, Francisco Ipinza, Juan Fuentes, Robinson Fumeron, José M. Villarreal, Alexis Aspée, Guido C. Mora, Claudio C. Vásquez, Claudia Saavedra

Resultado de la investigación: Article

43 Citas (Scopus)

Resumen

Porins are channels that enable passive diffusion of hydrophilic solutes, nutrients and toxins through the outer bacterial membrane. This explains in part the ability of Gram-negative microorganisms to grow in several different environments, as well as their drug resistance. OmpD is an outer membrane channel that works with the inner membrane pump YddG to expel methyl viologen (MV) from Salmonella enterica serovar Typhimurium; this occurs independently of SmvA, also involved in MV resistance. On the other hand, ΔtolC strains show increased MV resistance when compared to wild-type cells, suggesting that there may be other porin(s) that could function with SmvA to pump MV out of S. typhimurium. A strong candidate is OmpW. Here we show that ΔompW strains of S. typhimurium are 2.5-fold more sensitive to MV than the wild-type strain. Transcriptional fusions replacing ompW by lacZ show that ompW is induced at least 2-fold in the presence of MV. This result was observed both at the mRNA and protein levels, suggesting that ompW participates in MV resistance. In addition, ΔsmvAΔompW strains are not fully complemented by smvA, suggesting that OmpW may function through an independent pathway different from that used by SmvA to move MV outside the cell.

Idioma originalEnglish
Páginas (desde-hasta)529-536
Número de páginas8
PublicaciónResearch in Microbiology
Volumen158
N.º6
DOI
EstadoPublished - 1 jul 2007

Huella dactilar

Porins
Paraquat
Salmonella enterica
Genes
Membranes
Serogroup
Ion Channels
Drug Resistance
Food
Messenger RNA

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Citar esto

Gil, Fernando ; Ipinza, Francisco ; Fuentes, Juan ; Fumeron, Robinson ; Villarreal, José M. ; Aspée, Alexis ; Mora, Guido C. ; Vásquez, Claudio C. ; Saavedra, Claudia. / The ompW (porin) gene mediates methyl viologen (paraquat) efflux in Salmonella enterica serovar Typhimurium. En: Research in Microbiology. 2007 ; Vol. 158, N.º 6. pp. 529-536.
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abstract = "Porins are channels that enable passive diffusion of hydrophilic solutes, nutrients and toxins through the outer bacterial membrane. This explains in part the ability of Gram-negative microorganisms to grow in several different environments, as well as their drug resistance. OmpD is an outer membrane channel that works with the inner membrane pump YddG to expel methyl viologen (MV) from Salmonella enterica serovar Typhimurium; this occurs independently of SmvA, also involved in MV resistance. On the other hand, ΔtolC strains show increased MV resistance when compared to wild-type cells, suggesting that there may be other porin(s) that could function with SmvA to pump MV out of S. typhimurium. A strong candidate is OmpW. Here we show that ΔompW strains of S. typhimurium are 2.5-fold more sensitive to MV than the wild-type strain. Transcriptional fusions replacing ompW by lacZ show that ompW is induced at least 2-fold in the presence of MV. This result was observed both at the mRNA and protein levels, suggesting that ompW participates in MV resistance. In addition, ΔsmvAΔompW strains are not fully complemented by smvA, suggesting that OmpW may function through an independent pathway different from that used by SmvA to move MV outside the cell.",
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The ompW (porin) gene mediates methyl viologen (paraquat) efflux in Salmonella enterica serovar Typhimurium. / Gil, Fernando; Ipinza, Francisco; Fuentes, Juan; Fumeron, Robinson; Villarreal, José M.; Aspée, Alexis; Mora, Guido C.; Vásquez, Claudio C.; Saavedra, Claudia.

En: Research in Microbiology, Vol. 158, N.º 6, 01.07.2007, p. 529-536.

Resultado de la investigación: Article

TY - JOUR

T1 - The ompW (porin) gene mediates methyl viologen (paraquat) efflux in Salmonella enterica serovar Typhimurium

AU - Gil, Fernando

AU - Ipinza, Francisco

AU - Fuentes, Juan

AU - Fumeron, Robinson

AU - Villarreal, José M.

AU - Aspée, Alexis

AU - Mora, Guido C.

AU - Vásquez, Claudio C.

AU - Saavedra, Claudia

PY - 2007/7/1

Y1 - 2007/7/1

N2 - Porins are channels that enable passive diffusion of hydrophilic solutes, nutrients and toxins through the outer bacterial membrane. This explains in part the ability of Gram-negative microorganisms to grow in several different environments, as well as their drug resistance. OmpD is an outer membrane channel that works with the inner membrane pump YddG to expel methyl viologen (MV) from Salmonella enterica serovar Typhimurium; this occurs independently of SmvA, also involved in MV resistance. On the other hand, ΔtolC strains show increased MV resistance when compared to wild-type cells, suggesting that there may be other porin(s) that could function with SmvA to pump MV out of S. typhimurium. A strong candidate is OmpW. Here we show that ΔompW strains of S. typhimurium are 2.5-fold more sensitive to MV than the wild-type strain. Transcriptional fusions replacing ompW by lacZ show that ompW is induced at least 2-fold in the presence of MV. This result was observed both at the mRNA and protein levels, suggesting that ompW participates in MV resistance. In addition, ΔsmvAΔompW strains are not fully complemented by smvA, suggesting that OmpW may function through an independent pathway different from that used by SmvA to move MV outside the cell.

AB - Porins are channels that enable passive diffusion of hydrophilic solutes, nutrients and toxins through the outer bacterial membrane. This explains in part the ability of Gram-negative microorganisms to grow in several different environments, as well as their drug resistance. OmpD is an outer membrane channel that works with the inner membrane pump YddG to expel methyl viologen (MV) from Salmonella enterica serovar Typhimurium; this occurs independently of SmvA, also involved in MV resistance. On the other hand, ΔtolC strains show increased MV resistance when compared to wild-type cells, suggesting that there may be other porin(s) that could function with SmvA to pump MV out of S. typhimurium. A strong candidate is OmpW. Here we show that ΔompW strains of S. typhimurium are 2.5-fold more sensitive to MV than the wild-type strain. Transcriptional fusions replacing ompW by lacZ show that ompW is induced at least 2-fold in the presence of MV. This result was observed both at the mRNA and protein levels, suggesting that ompW participates in MV resistance. In addition, ΔsmvAΔompW strains are not fully complemented by smvA, suggesting that OmpW may function through an independent pathway different from that used by SmvA to move MV outside the cell.

KW - Methyl viologen

KW - OmpW

KW - Porin

KW - Salmonella typhimurium

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U2 - 10.1016/j.resmic.2007.05.004

DO - 10.1016/j.resmic.2007.05.004

M3 - Article

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AN - SCOPUS:34547498442

VL - 158

SP - 529

EP - 536

JO - Research in Microbiology

JF - Research in Microbiology

SN - 0923-2508

IS - 6

ER -