Evidence map›Paper›PMID 32424122›Full record

ArticleScientific reports2020

Venturicidin A, A Membrane-active Natural Product Inhibitor of ATP synthase Potentiates Aminoglycoside Antibiotics.

Venkateswarlu Yarlagadda, Ricardo Medina, Gerard D Wright

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Discovery and characterization of a novel chromosomally encoded aminoglycosideFrontiers in cellular and infection microbiology · 2026
    Article
  5. Article
  6. Adaptation to cinnamaldehyde shapesJournal of bacteriology · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Boosting the Antibacterial Activity of Azithromycin on Multidrug-ResistantInternational journal of molecular sciences · 2023
    Article
  17. Review
  18. Inhibitors of ATP Synthase as New Antibacterial Candidates.Antibiotics (Basel, Switzerland) · 2023
    Review
  19. FInternational journal of molecular sciences · 2023
    Review
  20. 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 2 countries.

Venkateswarlu YarlagaddaDavid Braley Centre for Antibiotic Discovery, M.G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, DeGroote School of Medicine, McMaster University, 1280 Main Street West, Hamilton, Ontario, L8S 4K1, Canada.
Ricardo MedinaDepartment of Microbiology, Central University of Las Villas, Santa Clara, Villa Clara, Cuba.
Gerard D WrightDavid Braley Centre for Antibiotic Discovery, M.G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, DeGroote School of Medicine, McMaster University, 1280 Main Street West, Hamilton, Ontario, L8S 4K1, Canada. wrightge@mcmaster.ca.
McMaster University · CAUniversidad Central "Marta Abreu" de las Villas (UCLV) · CU

Funding

CIHR FRN-148463
6 · The paper itself

Abstract

Despite the remarkable advances due to the discovery and development of antimicrobials agents, infectious diseases remain the second leading cause of death worldwide. This fact underlines the importance of developing new therapeutic strategies to address the widespread antibiotic resistance, which is the major contributing factor for clinical failures of the current therapeutics. In a screen for antibiotic adjuvants, we identified a natural product from actinomycetes, venturicidin A (VentA), that potentiates the aminoglycoside antibiotic gentamicin against multidrug-resistant clinical isolates of Staphylococcus, Enterococcus, and Pseudomonas aeruginosa. Furthermore, the combination of gentamicin and VentA was bactericidal and rapidly eradicated methicillin-resistant S. aureus (MRSA). The molecular mechanism of gentamicin potentiation activity is attributed to uncoupling of ATP synthesis by VentA from electron transport presumably by blocking the proton flow through ATP synthase, which results in an elevated concentration of extracellular protons and subsequent anticipated raise in gentamicin uptake. The disruption of the proton flux was characterized by perturbed membrane potential in MRSA. These results demonstrate that inhibition of ATP synthase along with the subsequent membrane dysregulation, as shown here with VentA, complements aminoglycoside antibiotics against MDR bacteria, and that this approach may be employed to combat bacterial resistance.

Indexed as

ActinobacteriaAdenosine TriphosphateAminoglycosidesAnti-Bacterial AgentsATP Synthetase ComplexesBacterial ProteinsEnzyme InhibitorsMethicillin-Resistant Staphylococcus aureusMicrobial Sensitivity TestsPseudomonas aeruginosaVenturicidinsAdenosine TriphosphateAminoglycosidesAnti-Bacterial AgentsATP Synthetase ComplexesBacterial ProteinsEnzyme Inhibitorsventuricidin AVenturicidins

Identifiers

PMID32424122
PMCPMC7235042
OpenAlexW3024598784

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.