Resistance of Neisseria gonorrhoeae to antimicrobial hydrophobic agents is modulated by the mrtRCDE efflux system
Article Abstract:
Examination of the correlation of Neisseria gonorrhoeae mtr system with other bacterial systems that enable resistance to antimicrobial agents reveals that a transcriptional regulator mtrR-encoding mtrR gene and three serially linked mtrCDE constitute the mtr system. N. gonorrhoeae proteins that are encoded by the mtrCDE genes resemble bacterial transport/efflux proteins that enable resistance to dyes, drugs and detergents. Gonococci lose the MtrC lipoprotein and become highly susceptible to different hydrophobic agents, indicating that an MtrCDE protein-mediated efflux-based system is responsible for the ability of gonococci to resist the hydrophobic compounds with antimicrobial action.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Loss-of-function mutations in the mtr efflux system of Neisseria gonorrhoeae
Article Abstract:
Some strains of Neisseria gonorrhoeae have developed a resistance to penicillin, and structurally diverse hydrophobic agents (HAs). The resistance has been ascribed to the multiple transferable resistance (mtr) operon, which is composed of the mtrR gene, encoding cell envelope proteins MtrC-MtrD-MtrE. The study of the genetic basis of HA hypersusceptibility in BR54 and BR87 strains identified mutations in the mtrR gene that could be suppressed phenotypically by mutations in their mtrC or mtrD genes.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system
Article Abstract:
The complete nucleotide sequence of the mtrD which permits the characterization of the MtrD protein was reported. It was found that the full-length protein has a molecular mass of 114kDa which contains a 56 amino acid signal peptide. Similar amino acid sequence with that of resistance/nodulation/division proteins led to the assumption that the MtrD protein function as energy-dependent transporters of antibacterial agents and secrete bacterial products to the extracellular fluid.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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