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Functional study of the novel multidrug efflux pump KexD from Klebsiella pneumoniae.
Gene. 2012 May 01; 498(2):177-82.GENE

Abstract

We cloned a gene, kexD, that provides a multidrug-resistant phenotype from multidrug-resistant Klebsiella pneumoniae MGH78578. The deduced amino acid sequence of KexD is similar to that of the inner membrane protein, RND-type multidrug efflux pump. Introduction of the kexD gene into Escherichia coli KAM32 resulted in a MIC that was higher for erythromycin, novobiocin, rhodamine 6G, tetraphenylphosphonium chloride, and ethidium bromide than that of the control. Intracellular ethidium bromide levels in E. coli cells carrying the kexD gene were lower than that in the control cells under energized conditions, suggesting that KexD is a component of an energy-dependent efflux pump. RND-type pumps typically consist of three components: an inner membrane protein, a periplasmic protein, and an outer membrane protein. We discovered that KexD functions with a periplasmic protein, AcrA, from E. coli and K. pneumoniae, but not with the periplasmic proteins KexA and KexG from K. pneumoniae. KexD was able to utilize either TolC of E. coli or KocC of K. pneumoniae as an outer membrane component. kexD mRNA was not detected in K. pneumoniae MGH78578 or ATCC10031. We isolated erythromycin-resistant mutants from K. pneumoniae ATCC10031, and some showed a multidrug-resistant phenotype similar to the drug resistance pattern of KexD. Two strains of multidrug-resistant mutants were investigated for kexD expression; kexD mRNA levels were increased in these strains. We conclude that changing kexD expression can contribute to the occurrence of multidrug-resistant K. pneumoniae.

Authors+Show Affiliations

Department of Molecular Microbiology, Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, Okayama University, Tsushima, Okayama 700-8530, Japan. wogawa@pharm.okayama-u.ac.jpNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22391093

Citation

Ogawa, Wakano, et al. "Functional Study of the Novel Multidrug Efflux Pump KexD From Klebsiella Pneumoniae." Gene, vol. 498, no. 2, 2012, pp. 177-82.
Ogawa W, Onishi M, Ni R, et al. Functional study of the novel multidrug efflux pump KexD from Klebsiella pneumoniae. Gene. 2012;498(2):177-82.
Ogawa, W., Onishi, M., Ni, R., Tsuchiya, T., & Kuroda, T. (2012). Functional study of the novel multidrug efflux pump KexD from Klebsiella pneumoniae. Gene, 498(2), 177-82. https://doi.org/10.1016/j.gene.2012.02.008
Ogawa W, et al. Functional Study of the Novel Multidrug Efflux Pump KexD From Klebsiella Pneumoniae. Gene. 2012 May 1;498(2):177-82. PubMed PMID: 22391093.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Functional study of the novel multidrug efflux pump KexD from Klebsiella pneumoniae. AU - Ogawa,Wakano, AU - Onishi,Motoyasu, AU - Ni,Ruiting, AU - Tsuchiya,Tomofusa, AU - Kuroda,Teruo, Y1 - 2012/02/25/ PY - 2011/08/29/received PY - 2012/02/06/revised PY - 2012/02/08/accepted PY - 2012/3/7/entrez PY - 2012/3/7/pubmed PY - 2012/5/30/medline SP - 177 EP - 82 JF - Gene JO - Gene VL - 498 IS - 2 N2 - We cloned a gene, kexD, that provides a multidrug-resistant phenotype from multidrug-resistant Klebsiella pneumoniae MGH78578. The deduced amino acid sequence of KexD is similar to that of the inner membrane protein, RND-type multidrug efflux pump. Introduction of the kexD gene into Escherichia coli KAM32 resulted in a MIC that was higher for erythromycin, novobiocin, rhodamine 6G, tetraphenylphosphonium chloride, and ethidium bromide than that of the control. Intracellular ethidium bromide levels in E. coli cells carrying the kexD gene were lower than that in the control cells under energized conditions, suggesting that KexD is a component of an energy-dependent efflux pump. RND-type pumps typically consist of three components: an inner membrane protein, a periplasmic protein, and an outer membrane protein. We discovered that KexD functions with a periplasmic protein, AcrA, from E. coli and K. pneumoniae, but not with the periplasmic proteins KexA and KexG from K. pneumoniae. KexD was able to utilize either TolC of E. coli or KocC of K. pneumoniae as an outer membrane component. kexD mRNA was not detected in K. pneumoniae MGH78578 or ATCC10031. We isolated erythromycin-resistant mutants from K. pneumoniae ATCC10031, and some showed a multidrug-resistant phenotype similar to the drug resistance pattern of KexD. Two strains of multidrug-resistant mutants were investigated for kexD expression; kexD mRNA levels were increased in these strains. We conclude that changing kexD expression can contribute to the occurrence of multidrug-resistant K. pneumoniae. SN - 1879-0038 UR - https://www.unboundmedicine.com/medline/citation/22391093/Functional_study_of_the_novel_multidrug_efflux_pump_KexD_from_Klebsiella_pneumoniae_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0378-1119(12)00210-7 DB - PRIME DP - Unbound Medicine ER -