Evidence map›Paper›PMID 28720734›Full record

ArticlemBio2017

Lack of AcrB Efflux Function Confers Loss of Virulence on

Xuan Wang-Kan, Jessica M A Blair, Barbara Chirullo, Jonathan Betts, Roberto M La Ragione, Alasdair Ivens, Vito Ricci, Timothy J Opperman, Laura J V Piddock

Open access · goldAbstract read
In one paragraph

Article in mBio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

73 citing papers in PubMed, 126 citations in OpenAlex.

  1. Review
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  10. Article
  11. Decoding the evolutionary history of ST30Frontiers in microbiology · 2025
    Article
  12. The AcrAB efflux pump contributes to the virulence of EnteroaggregativeFrontiers in cellular and infection microbiology · 2025
    Article
  13. Dual role ofiMetaOmics · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 3 countries.

Xuan Wang-KanInstitute of Microbiology and Infection, College of Medical and Dental Sciences, The University of Birmingham, Birmingham, United Kingdom.
Jessica M A BlairInstitute of Microbiology and Infection, College of Medical and Dental Sciences, The University of Birmingham, Birmingham, United Kingdom.ORCID 0000-0001-6904-4253
Barbara ChirulloUnit of Prophylaxis and Control of Bacterial Zoonoses, Department of Veterinary Public Health and Food Safety, Istituto Superiore di Sanità, Rome, Italy.
Jonathan BettsSchool of Veterinary Medicine, Faculty of Health and Medical Sciences, University of Surrey, Guildford, United Kingdom.
Roberto M La RagioneSchool of Veterinary Medicine, Faculty of Health and Medical Sciences, University of Surrey, Guildford, United Kingdom.
Alasdair IvensCentre for Immunity, Infection and Evolution, University of Edinburgh, Edinburgh, United Kingdom.
Vito RicciInstitute of Microbiology and Infection, College of Medical and Dental Sciences, The University of Birmingham, Birmingham, United Kingdom.
Timothy J OppermanMicrobiotix, Inc., Anti-Infectives R&D, Worcester, Massachusetts, USA.
Laura J V PiddockInstitute of Microbiology and Infection, College of Medical and Dental Sciences, The University of Birmingham, Birmingham, United Kingdom l.j.v.piddock@bham.ac.uk.ORCID 0000-0003-1460-473X
University of Birmingham · GBUniversity of Surrey · GBCentre for Immunity, Infection and Evolution · GBIstituto Superiore di Sanità · ITMicrobiotix (United States) · US

Funding

Biotechnology and Biological Sciences Research Council BB/L024209/1
6 · The paper itself

Abstract

AcrAB-TolC is the paradigm resistance-nodulation-division (RND) multidrug resistance efflux system in Gram-negative bacteria, with AcrB being the pump protein in this complex. We constructed a nonfunctional AcrB mutant by replacing D408, a highly conserved residue essential for proton translocation. Western blotting confirmed that the AcrB D408A mutant had the same native level of expression of AcrB as the parental strain. The mutant had no growth deficiencies in rich or minimal medium. However, compared with wild-type SL1344, the mutant had increased accumulation of Hoechst 33342 dye and decreased efflux of ethidium bromide and was multidrug hypersusceptible. The D408A mutant was attenuated

Indexed as

AnimalsBacterial ProteinsBenzimidazolesBiological TransportDisease Models, AnimalEndocytosisEpithelial CellsEthidiumGene Expression ProfilingGene Expression Regulation, BacterialGenes, BacterialGenomic IslandsLepidopteraMembrane Transport ProteinsMiceMutant ProteinsAcrB protein, Salmonella entericaBacterial ProteinsBenzimidazolesbisbenzimide ethoxide trihydrochlorideEthidiumMembrane Transport ProteinsMutant ProteinsVirulence FactorsAcrBeffluxmotilitySalmonellaSalmonella pathogenicity islandSPItranscriptomevirulence

Identifiers

PMID28720734
PMCPMC5516257
OpenAlexW2738189268

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.