Evidence map›Paper›PMID 25453092›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Vibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes.

Anju Sreelatha, Terry L Bennett, Emily M Carpinone, Kevin M O'Brien, Kamyron D Jordan, Dara L Burdette, Kim Orth, Vincent J Starai

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  6. The role ofProceedings of the National Academy of Sciences of the United States of America · 2023
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  7. Article
  8. Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. VscF in T3SS1 Helps to Translocate VPA0226 inFrontiers in cellular and infection microbiology · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Anju SreelathaDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390; and.
Terry L BennettDepartments of Microbiology and.
Emily M CarpinoneDepartments of Microbiology and.
Kevin M O'BrienDepartments of Microbiology and.
Kamyron D JordanDepartments of Microbiology and.
Dara L BurdetteDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390; and.
Kim OrthDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390; and.
Vincent J StaraiDepartments of Microbiology and Infectious Diseases, University of Georgia, Athens, GA 30602 vjstarai@uga.edu.
The University of Texas Southwestern Medical Center · USUniversity of Georgia · US

Funding

Biochemical Characterization of Yersinia Effector YopJ.R01AI056404 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2003 to 2012
$2.8M
Analysis of an orchestrated cell death mediated by Vibrio parahaemolytics T3SS1R01AI087808 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2010 to 2014
$1.9M
Bacterial inhibitors of eukaryotic membrane fusionR01AI100913 · NIAID · UNIVERSITY OF GEORGIA · PI STARAI, VINCENT JOSEPH · 2013 to 2017
$1.7M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI056404NIAID NIH HHS R01-AI056404NIAID NIH HHS R01 AI087808NIAID NIH HHS R01-AI087808NIAID NIH HHS R01 AI100913NIAID NIH HHS R01-AI100913
6 · The paper itself

Abstract

Vesicle fusion governs many important biological processes, and imbalances in the regulation of membrane fusion can lead to a variety of diseases such as diabetes and neurological disorders. Here we show that the Vibrio parahaemolyticus effector protein VopQ is a potent inhibitor of membrane fusion based on an in vitro yeast vacuole fusion model. Previously, we demonstrated that VopQ binds to the V(o) domain of the conserved V-type H(+)-ATPase (V-ATPase) found on acidic compartments such as the yeast vacuole. VopQ forms a nonspecific, voltage-gated membrane channel of 18 Å resulting in neutralization of these compartments. We now present data showing that VopQ inhibits yeast vacuole fusion. Furthermore, we identified a unique mutation in VopQ that delineates its two functions, deacidification and inhibition of membrane fusion. The use of VopQ as a membrane fusion inhibitor in this manner now provides convincing evidence that vacuole fusion occurs independently of luminal acidification in vitro.

Indexed as

Membrane FusionAcidsBacterial ProteinsElectrochemistryHydrogen-Ion ConcentrationIon ChannelsLipidsMutant ProteinsSaccharomyces cerevisiaeSNARE ProteinsVacuolar Proton-Translocating ATPasesVacuolesVibrio parahaemolyticusAcidsBacterial ProteinsIon ChannelsLipidsMutant ProteinsSNARE ProteinsVacuolar Proton-Translocating ATPasesSNAREvesicle fusionVibrio parahaemolyticusvp1680yeast vacuole

Identifiers

PMID25453092
PMCPMC4291640
OpenAlexW2070006775

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.