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The NorM Efflux Pump of Neisseria gonorrhoeae and Neisseria meningitidis Recognizes Antimicrobial Cationic Compounds

The NorM Efflux Pump of Neisseria gonorrhoeae and Neisseria meningitidis Recognizes Antimicrobial... The NorM Efflux Pump of Neisseria gonorrhoeae and Neisseria meningitidis Recognizes Antimicrobial Cationic Compounds Corinne Rouquette-Loughlin 1 , Steven A. Dunham 2 , Michael Kuhn 2 , Jacqueline T. Balthazar 1 , and William M. Shafer 1 , 3 , * 1 Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322 2 Antibacterial Molecular Sciences, Ann Arbor Laboratories, Pfizer Global Research and Development, Ann Arbor, Michigan 48105 3 Laboratories of Microbial Pathogenesis, VA Medical Center, Decatur, Georgia 30033 ABSTRACT In Neisseria gonorrhoeae and Neisseria meningitidis , we identified a gene that would encode a protein highly similar to NorM of Vibrio parahaemolyticus (Y. Morita et al., Antimicrob. Agents Chemother. 42:1778-1782, 1998). A nonpolar insertional mutation in either the gonococcal or meningococcal norM gene resulted in increased bacterial sensitivity to compounds harboring a quaternary ammonium on an aromatic ring (e.g., ethidium bromide, acriflavine hydrochloride, 2- N -methylellipticinium, and berberine). The presence of point mutations within the −35 region of a putative norM promoter or a likely ribosome binding site resulted in an increased resistance of gonococci and meningococci to the same compounds, as well as to norfloxacin and ciprofloxacin. Structure-activity relationship studies with putative NorM substrates have found that a cationic moiety is essential for NorM recognition. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Bacteriology American Society For Microbiology

The NorM Efflux Pump of Neisseria gonorrhoeae and Neisseria meningitidis Recognizes Antimicrobial Cationic Compounds

The NorM Efflux Pump of Neisseria gonorrhoeae and Neisseria meningitidis Recognizes Antimicrobial Cationic Compounds

Journal of Bacteriology , Volume 185 (3): 1101 – Feb 1, 2003

Abstract

The NorM Efflux Pump of Neisseria gonorrhoeae and Neisseria meningitidis Recognizes Antimicrobial Cationic Compounds Corinne Rouquette-Loughlin 1 , Steven A. Dunham 2 , Michael Kuhn 2 , Jacqueline T. Balthazar 1 , and William M. Shafer 1 , 3 , * 1 Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322 2 Antibacterial Molecular Sciences, Ann Arbor Laboratories, Pfizer Global Research and Development, Ann Arbor, Michigan 48105 3 Laboratories of Microbial Pathogenesis, VA Medical Center, Decatur, Georgia 30033 ABSTRACT In Neisseria gonorrhoeae and Neisseria meningitidis , we identified a gene that would encode a protein highly similar to NorM of Vibrio parahaemolyticus (Y. Morita et al., Antimicrob. Agents Chemother. 42:1778-1782, 1998). A nonpolar insertional mutation in either the gonococcal or meningococcal norM gene resulted in increased bacterial sensitivity to compounds harboring a quaternary ammonium on an aromatic ring (e.g., ethidium bromide, acriflavine hydrochloride, 2- N -methylellipticinium, and berberine). The presence of point mutations within the −35 region of a putative norM promoter or a likely ribosome binding site resulted in an increased resistance of gonococci and meningococci to the same compounds, as well as to norfloxacin and ciprofloxacin. Structure-activity relationship studies with putative NorM substrates have found that a cationic moiety is essential for NorM recognition.

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Publisher
American Society For Microbiology
Copyright
Copyright © 2003 by the American society for Microbiology.
ISSN
0021-9193
eISSN
1098-5530
DOI
10.1128/JB.185.3.1101-1106.2003
Publisher site
See Article on Publisher Site

Abstract

The NorM Efflux Pump of Neisseria gonorrhoeae and Neisseria meningitidis Recognizes Antimicrobial Cationic Compounds Corinne Rouquette-Loughlin 1 , Steven A. Dunham 2 , Michael Kuhn 2 , Jacqueline T. Balthazar 1 , and William M. Shafer 1 , 3 , * 1 Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322 2 Antibacterial Molecular Sciences, Ann Arbor Laboratories, Pfizer Global Research and Development, Ann Arbor, Michigan 48105 3 Laboratories of Microbial Pathogenesis, VA Medical Center, Decatur, Georgia 30033 ABSTRACT In Neisseria gonorrhoeae and Neisseria meningitidis , we identified a gene that would encode a protein highly similar to NorM of Vibrio parahaemolyticus (Y. Morita et al., Antimicrob. Agents Chemother. 42:1778-1782, 1998). A nonpolar insertional mutation in either the gonococcal or meningococcal norM gene resulted in increased bacterial sensitivity to compounds harboring a quaternary ammonium on an aromatic ring (e.g., ethidium bromide, acriflavine hydrochloride, 2- N -methylellipticinium, and berberine). The presence of point mutations within the −35 region of a putative norM promoter or a likely ribosome binding site resulted in an increased resistance of gonococci and meningococci to the same compounds, as well as to norfloxacin and ciprofloxacin. Structure-activity relationship studies with putative NorM substrates have found that a cationic moiety is essential for NorM recognition.

Journal

Journal of BacteriologyAmerican Society For Microbiology

Published: Feb 1, 2003

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