Evidence map›Paper›PMID 26193906›Full record

ArticleMolecular microbiology2015

Non-equivalent roles of two periplasmic subunits in the function and assembly of triclosan pump TriABC from Pseudomonas aeruginosa.

Jon W Weeks, Logan M Nickels, Abigail T Ntreh, Helen I Zgurskaya

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 32% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 22 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Jon W WeeksDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK, 73019, USA.
Logan M NickelsDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK, 73019, USA.
Abigail T NtrehDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK, 73019, USA.
Helen I ZgurskayaDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK, 73019, USA.
University of Oklahoma · US

Funding

Transport across two membranes by AcrAB-TolC complexR01AI052293 · NIAID · UNIVERSITY OF OKLAHOMA NORMAN · PI ZGURSKAYA, HELEN I · 2003 to 2024
$7.7M
Transport Across Two Membranes by AcrAB-TolC ComplexR56AI052293 · NIAID · UNIVERSITY OF OKLAHOMA · PI ZGURSKAYA, HELEN I · 2008 to 2008
$360k
NIAID NIH HHS AI052293NIAID NIH HHS R01 AI052293NIAID NIH HHS R56 AI052293
6 · The paper itself

Abstract

In Gram-negative bacteria, multidrug efflux transporters function in complexes with periplasmic membrane fusion proteins (MFPs) that enable antibiotic efflux across the outer membrane. In this study, we analyzed the function, composition and assembly of the triclosan efflux transporter TriABC-OpmH from Pseudomonas aeruginosa. We report that this transporter possesses a surprising substrate specificity that encompasses not only triclosan but the detergent SDS, which are often used together in antibacterial soaps. These two compounds interact antagonistically in a TriABC-dependent manner and negate antibacterial properties of each other. Unlike other efflux pumps that rely on a single MFP for their activities, two different MFPs, TriA and TriB, are required for triclosan/SDS resistance mediated by TriABC-OpmH. We found that analogous mutations in the α-helical hairpin and membrane proximal domains of TriA and TriB differentially affect triclosan efflux and assembly of the complex. Furthermore, our results show that TriA and TriB function as a dimer, in which TriA is primarily responsible for stabilizing interactions with the outer membrane channel, whereas TriB is important for the stimulation of the transporter. We conclude that MFPs are engaged into complexes as asymmetric dimers, in which each protomer plays a specific role.

Indexed as

Genes, MDRAmino Acid SequenceBacterial Outer Membrane ProteinsDrug Resistance, BacterialMembrane Fusion ProteinsMembrane Transport ProteinsPeriplasmProtein Structure, SecondaryPseudomonas aeruginosaSodium Dodecyl SulfateTriclosanBacterial Outer Membrane ProteinsMembrane Fusion ProteinsMembrane Transport ProteinsSodium Dodecyl SulfateTriclosan

Identifiers

PMID26193906
PMCPMC4690728
OpenAlexW2096580953

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.