Evidence map›Paper›PMID 25338022›Full record

ArticlePloS one2014

High-throughput screening of dipeptide utilization mediated by the ABC transporter DppBCDF and its substrate-binding proteins DppA1-A5 in Pseudomonas aeruginosa.

Daniel Pletzer, Corinne Lafon, Yvonne Braun, Thilo Köhler, Malcolm G P Page, Michael Mourez, Helge Weingart

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

37 citing papers in PubMed, 54 citations in OpenAlex.

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  16. Targeting theFrontiers in microbiology · 2022
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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

7 authors at 4 institutions in 3 countries.

Daniel PletzerJacobs University Bremen, School of Engineering and Science, Bremen, Germany.
Corinne LafonSanofi-Aventis R&D, Infectious Diseases Therapeutic Unit, Toulouse, France.
Yvonne BraunJacobs University Bremen, School of Engineering and Science, Bremen, Germany.
Thilo KöhlerDepartment of Microbiology and Molecular Medicine and Service of Infectious Diseases, University Hospital Geneva, Geneva, Switzerland.
Malcolm G P PageBasilea Pharmaceutica International Ltd, Basel, Switzerland.
Michael MourezSanofi-Aventis R&D, Infectious Diseases Therapeutic Unit, Toulouse, France.
Helge WeingartJacobs University Bremen, School of Engineering and Science, Bremen, Germany.
Constructor University · DESanofi (France) · FRBasilea Pharmaceutica (Switzerland) · CHUniversity Hospital of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, we show that the dppBCDF operon of Pseudomonas aeruginosa PA14 encodes an ABC transporter responsible for the utilization of di/tripeptides. The substrate specificity of ABC transporters is determined by its associated substrate-binding proteins (SBPs). Whereas in E. coli only one protein, DppA, determines the specificity of the transporter, five orthologous SBPs, DppA1-A5 are present in P. aeruginosa. Multiple SBPs might broaden the substrate specificity by increasing the transporter capacity. We utilized the Biolog phenotype MicroArray technology to investigate utilization of di/tripeptides in mutants lacking either the transport machinery or all of the five SBPs. This high-throughput method enabled us to screen hundreds of dipeptides with various side-chains, and subsequently, to determine the substrate profile of the dipeptide permease. The substrate spectrum of the SBPs was elucidated by complementation of a penta mutant, deficient of all five SBPs, with plasmids carrying individual SBPs. It became apparent that some dipeptides were utilized with different affinity for each SBP. We found that DppA2 shows the highest flexibility on substrate recognition and that DppA2 and DppA4 have a higher tendency to utilize tripeptides. DppA5 was not able to complement the penta mutant under our screening conditions. Phaseolotoxin, a toxic tripeptide inhibiting the enzyme ornithine carbamoyltransferase, is also transported into P. aeruginosa via the DppBCDF permease. The SBP DppA1, and with much greater extend DppA3, are responsible for delivering the toxin to the permease. Our results provide a first overview of the substrate pattern of the ABC dipeptide transport machinery in P. aeruginosa.

Indexed as

High-Throughput Screening AssaysATP-Binding Cassette TransportersBacterial ProteinsCarrier ProteinsDipeptidesGene OrderGenetic LociMutationNitrogenOperonPseudomonas aeruginosaSubstrate SpecificityATP-Binding Cassette TransportersBacterial ProteinsCarrier ProteinsDipeptidesNitrogen

Identifiers

PMID25338022
PMCPMC4206461
OpenAlexW1970581996

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.