Evidence map›Paper›PMID 17526713›Full record

ArticleJournal of bacteriology2007

Drug-induced conformational changes in multidrug efflux transporter AcrB from Haemophilus influenzae.

Vishakha Dastidar, Weimin Mao, Olga Lomovskaya, Helen I Zgurskaya

Open access · greenAbstract read
In one paragraph

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Structure and mechanism of RND-type multidrug efflux pumps.Advances in enzymology and related areas of molecular biology · 2011
    Review
  10. Article
  11. Review
  12. Mechanisms of RND multidrug efflux pumps.Biochimica et biophysica acta · 2009
    Review
  13. Review
  14. Article
  15. Article
  16. Article
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.

Vishakha DastidarDepartment of Chemistry and Biochemistry, 620 Parrington Oval, Norman, OK 73019, USA.
Weimin Mao
Olga Lomovskaya
Helen I Zgurskaya
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
NIAID NIH HHS 1-R01-AI052293NIAID NIH HHS R01 AI052293
6 · The paper itself

Abstract

In gram-negative bacteria, transporters belonging to the resistance-nodulation-cell division (RND) superfamily of proteins are responsible for intrinsic multidrug resistance. Haemophilus influenzae, a gram-negative pathogen causing respiratory diseases in humans and animals, constitutively produces the multidrug efflux transporter AcrB (AcrB(HI)). Similar to other RND transporters AcrB(HI) associates with AcrA(HI), the periplasmic membrane fusion protein, and the outer membrane channel TolC(HI). Here, we report that AcrAB(HI) confers multidrug resistance when expressed in Escherichia coli and requires for its activity the E. coli TolC (TolC(EC)) protein. To investigate the intracellular dynamics of AcrAB(HI), single cysteine mutations were constructed in AcrB(HI) in positions previously identified as important for substrate recognition. The accessibility of these strategically positioned cysteines to the hydrophilic thiol-reactive fluorophore fluorescein-5-maleimide (FM) was studied in vivo in the presence of various substrates of AcrAB(HI) and in the presence or absence of AcrA(HI) and TolC(EC). We report that the reactivity of specific cysteines with FM is affected by the presence of some but not all substrates. Our results suggest that substrates induce conformational changes in AcrB(HI).

Indexed as

Drug Resistance, Multiple, BacterialAmino Acid SubstitutionBacterial Outer Membrane ProteinsBacterial ProteinsCysteineEscherichia coliEscherichia coli ProteinsFluoresceinsHaemophilus influenzaeMembrane Transport ProteinsMutagenesis, Site-DirectedMutation, MissenseProtein ConformationBacterial Outer Membrane ProteinsBacterial ProteinsCysteineEscherichia coli Proteinsfluorescein 5-maleimideFluoresceinsMembrane Transport ProteinstolC protein, E coli

Identifiers

PMID17526713
PMCPMC1951822
OpenAlexW2111464826

What OpenQuestion holds

Textmetadata
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.