Evidence map›Paper›PMID 39869656›Full record

ArticlePLoS computational biology2025

Specificity and tunability of efflux pumps: A new role for the proton gradient?

Matthew Gerry, Duncan Kirby, Boian S Alexandrov, Dvira Segal, Anton Zilman

Abstract read
In one paragraph

Article in PLoS computational biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
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

5 authors.

Matthew GerryDepartment of Physics, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0003-0367-3094
Duncan KirbyDepartment of Physics, University of Toronto, Toronto, Ontario, Canada.
Boian S AlexandrovTheoretical Division, Los Alamos National Laboratory, Los Alamos, New Mexico, United States of America.ORCID 0000-0001-8636-4603
Dvira SegalChemical Physics Theory Group, Department of Chemistry and Centre for Quantum Information and Quantum Control, University of Toronto, Toronto, Ontario, Canada.
Anton ZilmanDepartment of Physics, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0002-8523-6703

Funding

NSERC Canada Graduate Scholarship–DoctoralU.S. Department of Energy 89233218CNA000001
6 · The paper itself

Abstract

Efflux pumps that transport antibacterial drugs out of bacterial cells have broad specificity, commonly leading to broad spectrum resistance and limiting treatment strategies for infections. It remains unclear how efflux pumps can maintain this broad spectrum specificity to diverse drug molecules while limiting the efflux of other cytoplasmic content. We have investigated the origins of this broad specificity using theoretical models informed by the experimentally determined structural and kinetic properties of efflux pumps. We developed a set of mathematical models describing operation of efflux pumps as a discrete cyclic stochastic process across a network of states characterizing pump conformations and the presence/absence of bound ligands and protons. These include a minimal three-state model that lends itself to clear analytic calculations as well as a five-state model that relaxes some of the simpler model's most strict assumptions. We found that the pump specificity is determined not solely by the drug affinity to the pump-as is commonly assumed-but it is also directly affected by the periplasmic pH and the transmembrane potential. Therefore, changes to the proton concentration gradient and voltage drop across the membrane can influence how effective the pump is at extruding a particular drug molecule. Furthermore, we found that while both the proton concentration gradient across the membrane and the transmembrane potential contribute to the thermodynamic force driving the pump, their effects on the efflux enter not strictly in a combined proton motive force. Rather, they have two distinguishable effects on the overall throughput. These results highlight the unexpected effects of thermodynamic driving forces out of equilibrium and illustrate how efflux pump structure and function are conducive to the emergence of multidrug resistance.

Indexed as

Membrane Transport ProteinsModels, BiologicalProton-Motive ForceAnti-Bacterial AgentsHydrogen-Ion ConcentrationProtonsAnti-Bacterial AgentsMembrane Transport ProteinsProtons

Identifiers

PMID39869656
PMCPMC11798531

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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.