Evidence map›Paper›PMID 26787896›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Aminoacyl β-naphthylamides as substrates and modulators of AcrB multidrug efflux pump.

Alfred D Kinana, Attilio V Vargiu, Thithiwat May, Hiroshi Nikaido

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 87 citations in OpenAlex.

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  10. Emergence of Rarely Reported Extensively Drug-ResistantAntibiotics (Basel, Switzerland) · 2024
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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 2 institutions in 2 countries.

Alfred D KinanaDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202;
Attilio V VargiuDepartment of Physics, University of Cagliari, 09042 Monserrato, Italy.
Thithiwat MayDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202;
Hiroshi NikaidoDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202; nhiroshi@berkeley.edu.
University of California, Berkeley · USUniversity of Cagliari · IT

Funding

BIOCHEMISTRY OF BACTERIAL CELL MEMBRANESR01AI009644 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI NIKAIDO, HIROSHI · 1985 to 2015
$9.7M
BIOCHEMISTRY OF BACTERIAL CELL MEMBRANESR37AI009644 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI NIKAIDO, HIROSHI · 1991 to 2000
$467k
NIAID NIH HHS AI-009644NIAID NIH HHS R01 AI009644NIAID NIH HHS R37 AI009644
6 · The paper itself

Abstract

Efflux pumps of the resistance-nodulation division superfamily, such as AcrB, make a major contribution to multidrug resistance in Gram-negative bacteria. Inhibitors of such pumps would improve the efficacy of antibiotics, and ameliorate the crisis in health care caused by the prevalence of multidrug resistant Gram-negative pathogens. Phenylalanyl-arginine β-naphthylamide (PAβN), is a well-known inhibitor of AcrB and its homologs. However, its mechanism of inhibition is not clear. Because the hydrolysis of PAβN in Escherichia coli was nearly entirely dependent on an aminopeptidase, PepN, expression of PepN in periplasm allowed us to carry out a quantitative determination of PAβN efflux kinetics through the determination of its periplasmic concentrations by quantitation of the first hydrolysis product, phenylalanine, after a short period of treatment. We found that PAβN is efficiently pumped out by AcrB, with a sigmoidal kinetics. We also examined the behavior of PAβN homologs, Ala β-naphthylamide, Arg β-naphthylamide, and Phe β-naphthylamide, as substrates of AcrB and as modulators of nitrocefin efflux through AcrB. Furthermore, molecular dynamics simulations indicated that the mode of binding of these compounds to AcrB affects the modulatory activity on the efflux of other substrates. These results, and the finding that PAβN changes the nitrocefin kinetics into a sigmoidal one, suggested that PAβN inhibited the efflux of other drugs by binding to the bottom of the distal binding pocket, the so-called hydrophobic trap, and also by interfering with the binding of other drug substrates to the upper part of the binding pocket.

Indexed as

ATP-Binding Cassette, Sub-Family C ProteinsEscherichia coli ProteinsKineticsNaphthalenesSubstrate Specificity2-naphthylamideAcrB protein, E coliATP-Binding Cassette, Sub-Family C ProteinsEscherichia coli ProteinsNaphthalenesefflux inhibitorsmolecular dynamics simulationsPhe-Arg-β-naphthylamideRND transporters

Identifiers

PMID26787896
PMCPMC4747751
OpenAlexW2267817589

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.