Evidence map›Paper›PMID 35306531›Full record

ArticleScientific reports2022

A role for the periplasmic adaptor protein AcrA in vetting substrate access to the RND efflux transporter AcrB.

Ilyas Alav, Vassiliy N Bavro, Jessica M A Blair

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. 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
1.3field-weighted citation impact, top 22% 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, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Proteome Changes Induced by Iprodione Exposure in the Pesticide-TolerantInternational journal of molecular sciences · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

3 authors at 2 institutions in 1 country.

Ilyas AlavInstitute of Microbiology and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Vassiliy N BavroSchool of Life Sciences, University of Essex, Colchester, CO4 3SQ, UK. v.bavro@essex.ac.uk.
Jessica M A BlairInstitute of Microbiology and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham, B15 2TT, UK. j.m.a.blair@bham.ac.uk.
University of Birmingham · GBUniversity of Essex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M01116X/1Biotechnology and Biological Sciences Research Council BB/M02623X/1Biotechnology and Biological Sciences Research Council BB/N002776/1
6 · The paper itself

Abstract

Tripartite resistance-nodulation-division (RND) efflux pumps, such as AcrAB-TolC of Salmonella Typhimurium, contribute to antibiotic resistance and comprise an inner membrane RND-transporter, an outer membrane factor, and a periplasmic adaptor protein (PAP). The role of the PAP in the assembly and active transport process remains poorly understood. Here, we identify the functionally critical residues involved in PAP-RND-transporter binding between AcrA and AcrB and show that the corresponding RND-binding residues in the closely related PAP AcrE, are also important for its interaction with AcrB. We also report a residue in the membrane-proximal domain of AcrA, that when mutated, differentially affects the transport of substrates utilising different AcrB efflux channels, namely channels 1 and 2. This supports a potential role for the PAP in sensing the substrate-occupied state of the proximal binding pocket of the transporter and substrate vetting. Understanding the PAP's role in the assembly and function of tripartite RND pumps can guide novel ways to inhibit their function to combat antibiotic resistance.

Indexed as

Escherichia coli ProteinsMembrane Transport ProteinsAdaptor Proteins, Signal TransducingAnti-Bacterial AgentsATP-Binding Cassette, Sub-Family C ProteinsBacterial Outer Membrane ProteinsBiological TransportPeriplasmSalmonella typhimuriumAdaptor Proteins, Signal TransducingAnti-Bacterial AgentsATP-Binding Cassette, Sub-Family C ProteinsBacterial Outer Membrane ProteinsEscherichia coli ProteinsMembrane Transport Proteins

Identifiers

PMID35306531
PMCPMC8934357
OpenAlexW4221081027

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.