Evidence map›Paper›PMID 23798441›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Vibrio effector protein, VopQ, forms a lysosomal gated channel that disrupts host ion homeostasis and autophagic flux.

Anju Sreelatha, Terry L Bennett, Hui Zheng, Qiu-Xing Jiang, 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, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022
    Article
  11. Review
  12. Review
  13. VscF in T3SS1 Helps to Translocate VPA0226 inFrontiers in cellular and infection microbiology · 2021
    Article
  14. Adaptations ofFrontiers in microbiology · 2021
    Review
  15. A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. 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

6 authors at 2 institutions in 1 country.

Anju SreelathaDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Terry L Bennett
Hui Zheng
Qiu-Xing Jiang
Kim Orth
Vincent J Starai
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
Structural study of a Kv channel in different conformations in membranesR01GM093271 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2010 to 2013
$1.2M
Obtaining 3D structures with subnanogram macromoleculesR01GM088745 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2009 to 2012
$1.0M
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-AI100913NIGMS NIH HHS R01 GM088745NIGMS NIH HHS R01-GM088745NIGMS NIH HHS R01 GM093271NIGMS NIH HHS R01-GM093271
6 · The paper itself

Abstract

Defects in normal autophagic pathways are implicated in numerous human diseases--such as neurodegenerative diseases, cancer, and cardiomyopathy--highlighting the importance of autophagy and its proper regulation. Herein we show that Vibrio parahaemolyticus uses the type III effector VopQ (Vibrio outer protein Q) to alter autophagic flux by manipulating the partitioning of small molecules and ions in the lysosome. This effector binds to the conserved Vo domain of the vacuolar-type H(+)-ATPase and causes deacidification of the lysosomes within minutes of entering the host cell. VopQ forms a gated channel ∼18 Å in diameter that facilitates outward flux of ions across lipid bilayers. The electrostatic interactions of this type 3 secretion system effector with target membranes dictate its preference for host vacuolar-type H(+)-ATPase-containing membranes, indicating that its pore-forming activity is specific and not promiscuous. As seen with other effectors, VopQ is exploiting a eukaryotic mechanism, in this case manipulating lysosomal homeostasis and autophagic flux through transmembrane permeation.

Indexed as

AutophagyIon Channel GatingBacterial ProteinsHomeostasisIonsLysosomesVibrio parahaemolyticusBacterial ProteinsIonsmicrobial pathogenesisvirulenceyeast vacuole

Identifiers

PMID23798441
PMCPMC3710849
OpenAlexW2120771856

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.