VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus

Taira Matsuo, Katsuhiko Hayashi, Yuji Morita, Motohiro Koterasawa, Wakano Ogawa, Tohru Mizushima, Tomofusa Tsuchiya, Teruo Kuroda

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Genes vmeA and vmeB, encoding a multidrug efflux transporter in the halophilic bacterium Vibrio parahaemolyticus, have been cloned using a drug-hypersusceptible Escherichia coli strain as the host. Cells of E. coli KAM33 (ΔacrAB ΔydhE) carrying the vmeAB region from V. parahaemolyticus conferred much higher MICs for a variety of antimicrobial agents than did control cells. Cells possessing VmeAB under energized conditions maintained very low intracellular concentrations of ethidium. This was as expected for an energy-dependent efflux system, and supports the notion - based on sequence homology - that VmeAB belongs to the resistance nodulation cell division (RND) family of multidrug efflux transporters. It is likely that VmeAB forms functional complexes with the outer-membrane protein TolC in E. coli, because introduction of vmeAB into cells of E. coli KAM43, which lacks the tolC gene, failed to elevate the MICs for any of the antimicrobial agents tested. Therefore, a V. parahaemolyticus homologue of tolC was also cloned, designated vpoC, and was introduced together with vmeAB into cells of E. coli KAM43. The MICs of all agents tested were raised and were comparable to the values observed in E. coli KAM33 harbouring a plasmid carrying vmeAB. Finally, a vmeAB-deficient mutant of V. parahaemolyticus was constructed (designated TM3). TM3 showed slightly higher susceptibility than the parental V. parahaemolyticus to some antimicrobial agents. Survival rate of the TM3 when exposed to deoxycholate decreased compared with that of the parent.

Original languageEnglish
Pages (from-to)4129-4137
Number of pages9
JournalMicrobiology
Volume153
Issue number12
DOIs
Publication statusPublished - 2007 Dec
Externally publishedYes

Fingerprint

Vibrio parahaemolyticus
Cell Division
Escherichia coli
Anti-Infective Agents
Deoxycholic Acid
Ethidium
Sequence Homology
Genes
Membrane Proteins
Plasmids
Bacteria
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Microbiology

Cite this

Matsuo, T., Hayashi, K., Morita, Y., Koterasawa, M., Ogawa, W., Mizushima, T., ... Kuroda, T. (2007). VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus. Microbiology, 153(12), 4129-4137. https://doi.org/10.1099/mic.0.2007/009597-0

VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus. / Matsuo, Taira; Hayashi, Katsuhiko; Morita, Yuji; Koterasawa, Motohiro; Ogawa, Wakano; Mizushima, Tohru; Tsuchiya, Tomofusa; Kuroda, Teruo.

In: Microbiology, Vol. 153, No. 12, 12.2007, p. 4129-4137.

Research output: Contribution to journalArticle

Matsuo, T, Hayashi, K, Morita, Y, Koterasawa, M, Ogawa, W, Mizushima, T, Tsuchiya, T & Kuroda, T 2007, 'VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus', Microbiology, vol. 153, no. 12, pp. 4129-4137. https://doi.org/10.1099/mic.0.2007/009597-0
Matsuo T, Hayashi K, Morita Y, Koterasawa M, Ogawa W, Mizushima T et al. VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus. Microbiology. 2007 Dec;153(12):4129-4137. https://doi.org/10.1099/mic.0.2007/009597-0
Matsuo, Taira ; Hayashi, Katsuhiko ; Morita, Yuji ; Koterasawa, Motohiro ; Ogawa, Wakano ; Mizushima, Tohru ; Tsuchiya, Tomofusa ; Kuroda, Teruo. / VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus. In: Microbiology. 2007 ; Vol. 153, No. 12. pp. 4129-4137.
@article{cd53f3e55ca24362850e37ccaf615b59,
title = "VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus",
abstract = "Genes vmeA and vmeB, encoding a multidrug efflux transporter in the halophilic bacterium Vibrio parahaemolyticus, have been cloned using a drug-hypersusceptible Escherichia coli strain as the host. Cells of E. coli KAM33 (ΔacrAB ΔydhE) carrying the vmeAB region from V. parahaemolyticus conferred much higher MICs for a variety of antimicrobial agents than did control cells. Cells possessing VmeAB under energized conditions maintained very low intracellular concentrations of ethidium. This was as expected for an energy-dependent efflux system, and supports the notion - based on sequence homology - that VmeAB belongs to the resistance nodulation cell division (RND) family of multidrug efflux transporters. It is likely that VmeAB forms functional complexes with the outer-membrane protein TolC in E. coli, because introduction of vmeAB into cells of E. coli KAM43, which lacks the tolC gene, failed to elevate the MICs for any of the antimicrobial agents tested. Therefore, a V. parahaemolyticus homologue of tolC was also cloned, designated vpoC, and was introduced together with vmeAB into cells of E. coli KAM43. The MICs of all agents tested were raised and were comparable to the values observed in E. coli KAM33 harbouring a plasmid carrying vmeAB. Finally, a vmeAB-deficient mutant of V. parahaemolyticus was constructed (designated TM3). TM3 showed slightly higher susceptibility than the parental V. parahaemolyticus to some antimicrobial agents. Survival rate of the TM3 when exposed to deoxycholate decreased compared with that of the parent.",
author = "Taira Matsuo and Katsuhiko Hayashi and Yuji Morita and Motohiro Koterasawa and Wakano Ogawa and Tohru Mizushima and Tomofusa Tsuchiya and Teruo Kuroda",
year = "2007",
month = "12",
doi = "10.1099/mic.0.2007/009597-0",
language = "English",
volume = "153",
pages = "4129--4137",
journal = "Microbiology",
issn = "1350-0872",
publisher = "Society for General Microbiology",
number = "12",

}

TY - JOUR

T1 - VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus

AU - Matsuo, Taira

AU - Hayashi, Katsuhiko

AU - Morita, Yuji

AU - Koterasawa, Motohiro

AU - Ogawa, Wakano

AU - Mizushima, Tohru

AU - Tsuchiya, Tomofusa

AU - Kuroda, Teruo

PY - 2007/12

Y1 - 2007/12

N2 - Genes vmeA and vmeB, encoding a multidrug efflux transporter in the halophilic bacterium Vibrio parahaemolyticus, have been cloned using a drug-hypersusceptible Escherichia coli strain as the host. Cells of E. coli KAM33 (ΔacrAB ΔydhE) carrying the vmeAB region from V. parahaemolyticus conferred much higher MICs for a variety of antimicrobial agents than did control cells. Cells possessing VmeAB under energized conditions maintained very low intracellular concentrations of ethidium. This was as expected for an energy-dependent efflux system, and supports the notion - based on sequence homology - that VmeAB belongs to the resistance nodulation cell division (RND) family of multidrug efflux transporters. It is likely that VmeAB forms functional complexes with the outer-membrane protein TolC in E. coli, because introduction of vmeAB into cells of E. coli KAM43, which lacks the tolC gene, failed to elevate the MICs for any of the antimicrobial agents tested. Therefore, a V. parahaemolyticus homologue of tolC was also cloned, designated vpoC, and was introduced together with vmeAB into cells of E. coli KAM43. The MICs of all agents tested were raised and were comparable to the values observed in E. coli KAM33 harbouring a plasmid carrying vmeAB. Finally, a vmeAB-deficient mutant of V. parahaemolyticus was constructed (designated TM3). TM3 showed slightly higher susceptibility than the parental V. parahaemolyticus to some antimicrobial agents. Survival rate of the TM3 when exposed to deoxycholate decreased compared with that of the parent.

AB - Genes vmeA and vmeB, encoding a multidrug efflux transporter in the halophilic bacterium Vibrio parahaemolyticus, have been cloned using a drug-hypersusceptible Escherichia coli strain as the host. Cells of E. coli KAM33 (ΔacrAB ΔydhE) carrying the vmeAB region from V. parahaemolyticus conferred much higher MICs for a variety of antimicrobial agents than did control cells. Cells possessing VmeAB under energized conditions maintained very low intracellular concentrations of ethidium. This was as expected for an energy-dependent efflux system, and supports the notion - based on sequence homology - that VmeAB belongs to the resistance nodulation cell division (RND) family of multidrug efflux transporters. It is likely that VmeAB forms functional complexes with the outer-membrane protein TolC in E. coli, because introduction of vmeAB into cells of E. coli KAM43, which lacks the tolC gene, failed to elevate the MICs for any of the antimicrobial agents tested. Therefore, a V. parahaemolyticus homologue of tolC was also cloned, designated vpoC, and was introduced together with vmeAB into cells of E. coli KAM43. The MICs of all agents tested were raised and were comparable to the values observed in E. coli KAM33 harbouring a plasmid carrying vmeAB. Finally, a vmeAB-deficient mutant of V. parahaemolyticus was constructed (designated TM3). TM3 showed slightly higher susceptibility than the parental V. parahaemolyticus to some antimicrobial agents. Survival rate of the TM3 when exposed to deoxycholate decreased compared with that of the parent.

UR - http://www.scopus.com/inward/record.url?scp=37449013355&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=37449013355&partnerID=8YFLogxK

U2 - 10.1099/mic.0.2007/009597-0

DO - 10.1099/mic.0.2007/009597-0

M3 - Article

C2 - 18048926

AN - SCOPUS:37449013355

VL - 153

SP - 4129

EP - 4137

JO - Microbiology

JF - Microbiology

SN - 1350-0872

IS - 12

ER -