Journal
JOURNAL OF BACTERIOLOGY
Volume 185, Issue 3, Pages 1101-1106Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.185.3.1101-1106.2003
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Funding
- NIAID NIH HHS [R01 AI021150, R37 AI021150, AI 21150, P01 AI037945, AI 38399, AI 37945] Funding Source: Medline
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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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