ArticlePLoS pathogens2012
A cytotoxic type III secretion effector of Vibrio parahaemolyticus targets vacuolar H+-ATPase subunit c and ruptures host cell lysosomes.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Key Mechanisms in Lysosome Stability, Degradation and Repair.Molecular and cellular biology · 2025Review
- Bacterial Pathogen-Mediated Suppression of Host Trafficking to Lysosomes: Fluorescence Microscopy-Based DQ-Red BSA Analysis.Bio-protocol · 2024Article
- Cationic amphiphilic drugs induce accumulation of cytolytic lysoglycerophospholipids in the lysosomes of cancer cells and block their recycling into common membrane glycerophospholipids.Molecular biology of the cell · 2024Article
- Photo-ANA enables profiling of host-bacteria protein interactions during infection.Nature chemical biology · 2023Article
- Effect of sublethal dose of chloramphenicol on biofilm formation and virulence inFrontiers in microbiology · 2023Article
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- The V-ATPases in cancer and cell death.Cancer gene therapy · 2022Review
- Genetic architecture and phenotypic landscape of deafness and onychodystrophy syndromes.Human genetics · 2022Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Epidemiologic potentials and correlational analysis of Vibrio species and virulence toxins from water sources in greater Bushenyi districts, Uganda.Scientific reports · 2021Article
- Bafilomycin A1 enhances NLRP3 inflammasome activation in human monocytes independent of lysosomal acidification.The FEBS journal · 2021Article
- A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM.Nature structural & molecular biology · 2020Article
- Type III Secretion Effector VopQ of Vibrio parahaemolyticus Modulates Central Carbon Metabolism in Epithelial Cells.mSphere · 2020Article
- Export of a Vibrio parahaemolyticus toxin by the Sec and type III secretion machineries in tandem.Nature microbiology · 2019Article
- Vibrio variations on a type three theme.Current opinion in microbiology · 2019Review
- The Transcriptional Regulator HlyU Positively Regulates Expression ofJournal of bacteriology · 2018Article
- N-Terminal Acetylation by NatB Is Required for the Shutoff Activity of Influenza A Virus PA-X.Cell reports · 2018Article
- The Outcome of theJournal of immunology (Baltimore, Md. : 1950) · 2018Article
- The Vibrio alginolyticus T3SS effectors, Val1686 and Val1680, induce cell rounding, apoptosis and lysis of fish epithelial cells.Virulence · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrio parahaemolyticus is one of the human pathogenic vibrios. During the infection of mammalian cells, this pathogen exhibits cytotoxicity that is dependent on its type III secretion system (T3SS1). VepA, an effector protein secreted via the T3SS1, plays a major role in the T3SS1-dependent cytotoxicity of V. parahaemolyticus. However, the mechanism by which VepA is involved in T3SS1-dependent cytotoxicity is unknown. Here, we found that protein transfection of VepA into HeLa cells resulted in cell death, indicating that VepA alone is cytotoxic. The ectopic expression of VepA in yeast Saccharomyces cerevisiae interferes with yeast growth, indicating that VepA is also toxic in yeast. A yeast genome-wide screen identified the yeast gene VMA3 as essential for the growth inhibition of yeast by VepA. Although VMA3 encodes subunit c of the vacuolar H(+)-ATPase (V-ATPase), the toxicity of VepA was independent of the function of V-ATPases. In HeLa cells, knockdown of V-ATPase subunit c decreased VepA-mediated cytotoxicity. We also demonstrated that VepA interacted with V-ATPase subunit c, whereas a carboxyl-terminally truncated mutant of VepA (VepAΔC), which does not show toxicity, did not. During infection, lysosomal contents leaked into the cytosol, revealing that lysosomal membrane permeabilization occurred prior to cell lysis. In a cell-free system, VepA was sufficient to induce the release of cathepsin D from isolated lysosomes. Therefore, our data suggest that the bacterial effector VepA targets subunit c of V-ATPase and induces the rupture of host cell lysosomes and subsequent cell death.
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