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

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


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 Vo 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 A˚ 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.

Original languageEnglish (US)
Pages (from-to)100-105
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number1
StatePublished - Jan 6 2015


  • Vesicle fusion
  • Vibrio parahaemolyticus
  • Yeast vacuole
  • vp1680

ASJC Scopus subject areas

  • General


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