ArticleJournal of bacteriology2007
Assembly of the MexAB-OprM multidrug pump of Pseudomonas aeruginosa: component interactions defined by the study of pump mutant suppressors.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 41 citations in OpenAlex.
- Molecular rationale for the impairment of the MexAB-OprM efflux pump by a single mutation in MexA.Computational and structural biotechnology journal · 2022Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex.Nature communications · 2020Article
- EffluxPathogens (Basel, Switzerland) · 2020Article
- Dynamics of Intact MexAB-OprM Efflux Pump: Focusing on the MexA-OprM Interface.Scientific reports · 2017Article
- Focus on the Outer Membrane Factor OprM, the Forgotten Player from Efflux Pumps Assemblies.Antibiotics (Basel, Switzerland) · 2015Review
- Mechanism of coupling drug transport reactions located in two different membranes.Frontiers in microbiology · 2015Review
- Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.Frontiers in microbiology · 2015Review
- Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa.Frontiers in microbiology · 2015Article
- Molecular Dynamics Computer Simulations of Multidrug RND Efflux Pumps.Computational and structural biotechnology journal · 2013Review
- Overcoming drug resistance with alginate oligosaccharides able to potentiate the action of selected antibiotics.Antimicrobial agents and chemotherapy · 2012Article
- Xenobiotic efflux in bacteria and fungi: a genomics update.Advances in enzymology and related areas of molecular biology · 2011Review
- Functional rotation of the transporter AcrB: insights into drug extrusion from simulations.PLoS computational biology · 2010Article
- Review
- The C-terminal domain of AcrA is essential for the assembly and function of the multidrug efflux pump AcrAB-TolC.Journal of bacteriology · 2009Article
- Assembly and transport mechanism of tripartite drug efflux systems.Biochimica et biophysica acta · 2009Review
- Assembly and channel opening in a bacterial drug efflux machine.Molecular cell · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In an effort to identify key domains of the Pseudomonas aeruginosa MexAB-OprM drug efflux system involved in component interactions, extragenic suppressors of various inactivating mutations in individual pump constituents were isolated and studied. The multidrug hypersusceptibility of P. aeruginosa expressing MexB with a mutation in a region of the protein implicated in oligomerization (G220S) was suppressed by mutations in the alpha/beta domain of MexA. MexB(G220S) showed a reduced ability to bind MexA in vivo while representative MexA suppressors (V66M and V259F) restored the MexA-MexB interaction. Interestingly, these suppressors also restored resistance in P. aeruginosa expressing OprM proteins with mutations at the proximal (periplasmic) tip of OprM that is predicted to interact with MexB, suggesting that these suppressors generally overcame defects in MexA-MexB and MexB-OprM interaction. The multidrug hypersusceptibility arising from a mutation in the helical hairpin of MexA implicated in OprM interaction (V129M) was suppressed by mutations (T198I and F439I) in the periplasmic alpha-helical barrel of OprM. Again, the MexA mutation compromised an in vivo interaction with OprM that was restored by the T198I and F439I substitutions in OprM, consistent with the hairpin domain mediating MexA binding to this region of OprM. Interestingly, these OprM suppressor mutations restored multidrug resistance in P. aeruginosa expressing MexB(G220S). Finally, the oprM(T198I) suppressor mutation enhanced the yields of all three constituents of a MexA-MexB-OprM(T198I) pump as detected in whole-cell extracts. These data highlight the importance of MexA and interactions with this adapter in promoting MexAB-OprM pump assembly and in stabilizing the pump complex.
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Registered trials
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