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Antimicrobial Agents and Chemotherapy, July 1998, p. 1778-1782, Vol. 42, No. 7
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

NorM, a Putative Multidrug Efflux Protein, of Vibrio parahaemolyticus and Its Homolog in Escherichia coli

Yuji Morita,1 Kazuyo Kodama,1 Sumiko Shiota,1 Tomoyuki Mine,1 Atsuko Kataoka,1 Tohru Mizushima,1 and Tomofusa Tsuchiya1,2,*

Department of Microbiology, Faculty of Pharmaceutical Sciences,1 and Gene Research Center,2 Okayama University, Tsushima, Okayama 700-8530, Japan

Received 17 February 1998/Returned for modification 27 March 1998/Accepted 6 May 1998

We found that cells of Vibrio parahaemolyticus possess an energy-dependent efflux system for norfloxacin. We cloned a gene for a putative norfloxacin efflux protein from the chromosomal DNA of V. parahaemolyticus by using an Escherichia coli mutant lacking the major multidrug efflux system AcrAB as the host and sequenced the gene (norM). Cells of E. coli transformed with a plasmid carrying the norM gene showed elevated energy-dependent efflux of norfloxacin. The transformants showed elevated resistance not only to norfloxacin and ciprofloxacin but also to the structurally unrelated compounds ethidium, kanamycin, and streptomycin. These results suggest that this is a multidrug efflux system. The hydropathy pattern of the deduced amino acid sequence of NorM suggested the presence of 12 transmembrane domains. The deduced primary structure of NorM showed 57% identity and 88% similarity with that of a hypothetical E. coli membrane protein, YdhE. No reported drug efflux protein in the sequence databases showed significant sequence similarity with NorM. Thus, NorM seems to be a novel type of multidrug efflux protein. We cloned the ydhE gene from E. coli. Cells of E. coli transformed with the cloned ydhE gene showed elevated resistance to norfloxacin, ciprofloxacin, acriflavine, and tetraphenylphosphonium ion, but not to ethidium, when MICs were measured. Thus, it seems that NorM and YdhE differ somehow in substrate specificity.

* Corresponding author. Mailing address: Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, Tsushima, Okayama 700-8530, Japan. Phone and Fax: 81-86-251-7957. E-mail: tsuchiya{at}pharm.okayama-u.ac.jp.

Antimicrobial Agents and Chemotherapy, July 1998, p. 1778-1782, Vol. 42, No. 7
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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