Involvement of the gonococcal MtrE protein in the resistance of Neisseria gonorrhoeae to toxic hydrophobic agents
- 1 July 1997
- journal article
- Published by Microbiology Society in Microbiology
- Vol. 143 (7) , 2127-2133
- https://doi.org/10.1099/00221287-143-7-2127
Abstract
Summary: Low-level resistance of Neisseria gonorrhoeae to toxic hydrophobic agents (HAs), including some antibiotics, is chromosomally mediated via the multiple transferable resistance (mtr) efflux system. The gene encoding the 48.3 kDa outer-membrane protein MtrE, which is associated with the mtr phenotype, was identified and is homologous to export-associated outer-membrane proteins, including the OprM (formerly OprK) lipoprotein of Pseudomonas aeruginosa. Insertional inactivation of the mtrE gene in N. gonorrhoeae strain FA19 resulted in the loss of the outer-membrane protein, with concomitant hypersusceptibility of the mutant strain to a range of HAs. The properties of this mutant confirmed the role of MtrE in multidrug resistance mediated by an active efflux mechanism. Secondary structure predictions for MtrE indicated a largely hydrophilic protein with a single α-helical transmembrane region. A transposon-like element, similar to that found downstream of the region containing the promoters for mtrR and mtrC in Neisseria meningitidis, was identified 63 bp downstream of the mtrE gene.Keywords
Funding Information
- Joint Standing Research Committee, St Mary’s Hospital (C.A.I.) and NIH (AI-21150)
This publication has 25 references indexed in Scilit:
- Transcriptional control of the mtr efflux system of Neisseria gonorrhoeaeJournal of Bacteriology, 1995
- Resistance of Neisseria gonorrhoeae to antimicrobial hydrophobic agents is modulated by the mtrRCDE efflux systemMicrobiology, 1995
- Additive effect of tolC and rfa mutations on the hydrophobic barrier of the outer membrane of Escherichia coli K-12Journal of Bacteriology, 1994
- ABC transporters: bacterial exportersMicrobiological Reviews, 1993
- Methods and algorithms for statistical analysis of protein sequences.Proceedings of the National Academy of Sciences, 1992
- Lipoproteins in bacteriaJournal of Bioenergetics and Biomembranes, 1990
- Identification and arrangement of the DNA sequence recognized in specific transformation of Neisseria gonorrhoeae.Proceedings of the National Academy of Sciences, 1988
- A comprehensive set of sequence analysis programs for the VAXNucleic Acids Research, 1984
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978