Outer membrane proteins responsible for multiple drug resistance in Pseudomonas aeruginosa

@article{Masuda1995OuterMP,
  title={Outer membrane proteins responsible for multiple drug resistance in Pseudomonas aeruginosa},
  author={Nobuhisa Masuda and Eiko Sakagawa and Satoshi Ohya},
  journal={Antimicrobial Agents and Chemotherapy},
  year={1995},
  volume={39},
  pages={645 - 649}
}
Three types of multiple-drug-resistant mutants which were phenotypically similar to previously described nalB, nfxB, and nfxC mutants were isolated from Pseudomonas aeruginosa PAO1 and two clinical isolates. Type 1 (nalB-type) mutants showed cross-resistance to meropenem, cephems, and quinolones. They overproduced an outer membrane protein with an apparent molecular mass of 50 kDa (OprM). Type 2 (nfxB-type) mutants showed cross-resistance to quinolones and new cephems, i.e., cefpirome and… Expand
OprK and OprM define two genetically distinct multidrug efflux systems in Pseudomonas aeruginosa
TLDR
These experiments demonstrated the existence of two genetically distinct efflux systems in P. aeruginosa and the identities of the operons encoding the twoefflux systems and their physiological roles are discussed. Expand
C-Terminal Region of Pseudomonas aeruginosa Outer Membrane Porin OprD Modulates Susceptibility to Meropenem
TLDR
Results show that the C-terminal portion of OprD, in particular, loop L7, was responsible for the unusual meropenem hypersusceptibility, and it is proposed that shortening of putative loops L7 of the OPRD porin by 2 amino acid residues sufficiently opens the porin channel to allow optimal penetration of mer Openem and increase its activity. Expand
Molecular studies of the structure-function relationships of Psuedomonas aeruginosa OprM : an outer membrane protein associated with efflux
Pseudomonas aeruginosa demonstrates high intrinsic resistance to multiple classes of structurally unrelated antimicrobial agents. This broad-spectrum resistance is primarily due to a combination ofExpand
Purification of a 54-kilodalton protein (OprJ) produced in NfxB mutants of Pseudomonas aeruginosa and production of a monoclonal antibody specific to OprJ
TLDR
The results suggest that OprJ is newly produced in NfxB mutants of P. aeruginosa and is involved in fluoroquinolone resistance specific to NFXB, and it appears that the MAb to Oprj should aid in detection of the N FXB mutation in P. Aerug inosa. Expand
The outer membrane protein OprM of Pseudomonas aeruginosa is encoded by oprK of the mexA-mexB-oprK multidrug resistance operon
TLDR
Estimation of chromosomal DNA of several Tn5 insertion OprM-deficient mutants with primers specific to each gene of the mex operon revealed that the transposon had inserted into mexB in one instance and into oprK in two others, indicating that OprK is, in fact, not encoded by the meX operon, which is thus renamed mexA-mexB-oprM. Expand
Resistance and Virulence of Pseudomonas aeruginosa Clinical Strains Overproducing the MexCD-OprJ Efflux Pump
TLDR
Data show that, while rather infrequent among P. aeruginosa strains with low-level resistance to ciprofloxacin, MexCD-OprJ-overproducing mutants may be isolated after single therapy with fluoroquinolones and may be pathogenic. Expand
Differential Impact of MexB Mutations on Substrate Selectivity of the MexAB-OprM Multidrug Efflux Pump of Pseudomonas aeruginosa
TLDR
It appears that either proper assembly of the MexAB-OprM trimer is necessary for OprM interaction or OPRM association with an unstable MexB trimer might stabilize it, thereby restoring activity. Expand
Insertion Mutagenesis and Membrane Topology Model of the Pseudomonas aeruginosa Outer Membrane Protein OprM
  • Kendy K. Y. Wong, R. W. Hancock
  • Biology, Medicine
  • Journal of bacteriology
  • 2000
TLDR
An OprM topology model with 16 beta strands was proposed using data from insertion mutagenesis by cloning of a foreign epitope from the circumsporozoite form of the malarial parasite Plasmodium falciparum into 11 sites. Expand
Influence of the TonB Energy-Coupling Protein on Efflux-Mediated Multidrug Resistance in Pseudomonas aeruginosa
TLDR
TonB plays an important role in both intrinsic and acquired antibiotic resistance in P. aeruginosa, and the drug susceptibility of amexAB-oprM deletion strain was increased following deletion of tonB, suggesting that TonB may also influence antibiotic resistance mediated by determinants other than MexAB-OprM. Expand
Nucleotide sequence analysis of a gene from Burkholderia (Pseudomonas) cepacia encoding an outer membrane lipoprotein involved in multiple antibiotic resistance
TLDR
The finding of multiple antibiotic resistance in B. cepacia as a result of an antibiotic efflux pump is surprising because it has long been believed that resistance in this organism is caused by impermeability to antibiotics. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 24 REFERENCES
Mutations producing resistance to norfloxacin in Pseudomonas aeruginosa
TLDR
Two genetically distinct classes of norfloxacin-resistant Pseudomonas aeruginosa PAO4009 mutants were isolated spontaneously and it was suggested that the norfl oxacin resistance mechanism in the nfxB mutant might be an alteration in outer membrane permeability to norflxacin. Expand
Cross-resistance to meropenem, cephems, and quinolones in Pseudomonas aeruginosa
TLDR
The data suggest that overproduction of OprM is associated with cross-resistance to meropenem, cephems, and quinolones in P. aeruginosa. Expand
Outer membrane permeability in Pseudomonas aeruginosa: comparison of a wild-type with an antibiotic-supersusceptible mutant
TLDR
It was observed that levels of benzylpenicillin below the minimal inhibitory concentration for mutant Z61 failed to induce beta-lactamase production, consistent with the idea of low outer membrane permeability being caused by a low proportion of open functional porins in the outer membrane as the reason for the high natural antibiotic resistance of wild-type P, aeruginosa strains. Expand
Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon
TLDR
It is suggested that ORFA-ORFB-oprK (ORFC)-dependent drug efflux contributes to multiple antibiotic resistance in P. aeruginosa, and the designation mexAB (multiple efflux) for ORFAB is proposed. Expand
Salicylate-inducible antibiotic resistance in Pseudomonas cepacia associated with absence of a pore-forming outer membrane protein
TLDR
Findings suggest that OpcS is a selective, antibiotic-permeable porin which can be suppressed by growth in the presence of salicylate, and which was permeable to chloramphenicol but not to penicillin G. Expand
Genetic and physiological characterization of ciprofloxacin resistance in Pseudomonas aeruginosa PAO
TLDR
It is concluded that ciprofloxacin resistance in P. aeruginosa PAO2 can occur by mutation in the nalB gene or the gene for DNA gyrase A (formerly nalA), and there is an effect on permeability. Expand
Outer membrane protein H1 of Pseudomonas aeruginosa: involvement in adaptive and mutational resistance to ethylenediaminetetraacetate, polymyxin B, and gentamicin
It is well established that Pseudomonas aeruginosa cells grown in Mg2+-deficient medium acquire nonmutational resistance to the chelator ethylenediaminetetraacetate and to the cationic antibioticExpand
New norfloxacin resistance gene in Pseudomonas aeruginosa PAO
TLDR
The nfxC is a new norfloxacin resistance gene that affects outer membrane permeability to quinolones and other antimicrobial agents. Expand
Resistance of Pseudomonas aeruginosa PAO to nalidixic acid and low levels of beta-lactam antibiotics: mapping of chromosomal genes
  • M. Rella, D. Haas
  • Biology, Medicine
  • Antimicrobial Agents and Chemotherapy
  • 1982
TLDR
In nalB mutants, DNA replication showed wild- type sensitivity to nalidixic acid, whereas carbenicillin-induced filamentation required higher drug levels than in the wild-type strain, Thus, n alB mutations appear to decrease cell permeability to some antibiotics. Expand
Transient carbapenem resistance induced by salicylate in Pseudomonas aeruginosa associated with suppression of outer membrane protein D2 synthesis
TLDR
Results indicate that salicylate suppresses the synthesis of OprD and therefore reduces the antipseudomonal activity of carbapenems, which indicates that meropenem can pass through the outer membrane via both the D2 channel and another undefined route(s). Expand
...
1
2
3
...