ArticleBiochemistry2010
Reconstitution of Helicobacter pylori VacA toxin from purified components.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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.
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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.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- Review
- Mitochondrial Stress inAntioxidants (Basel, Switzerland) · 2026Review
- Vacuolating Cytotoxin A (VacA) and Extracellular Vesicles inIranian journal of pathology · 2025Review
- Structural Analysis of Membrane-associated Forms of Helicobacter pylori VacA Toxin.Journal of molecular biology · 2024Article
- Review
- Functional Properties of Oligomeric and Monomeric Forms of Helicobacter pylori VacA Toxin.Infection and immunity · 2021Article
- Construction and preservation of a stable and highly expressed recombinant Helicobacter pylori vacuolating cytotoxin A with apoptotic activity.BMC microbiology · 2021Article
- Cryo-EM structures ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Determinants of Raft Partitioning of the Helicobacter pylori Pore-Forming Toxin VacA.Infection and immunity · 2018Article
- A Helicobacter pylori Vacuolating Cytotoxin A: Mouse DHFR Fusion Protein Triggers Dye Release from Liposomes.Current microbiology · 2018Article
- Review
- Structural organization of membrane-inserted hexamers formed by Helicobacter pylori VacA toxin.Molecular microbiology · 2016Article
- A Nonoligomerizing Mutant Form of Helicobacter pylori VacA Allows Structural Analysis of the p33 Domain.Infection and immunity · 2016Article
- Review
- Effect of Helicobacter pylori on gastric epithelial cells.World journal of gastroenterology · 2014Review
- Helicobacter pylori membrane vesicles stimulate innate pro- and anti-inflammatory responses and induce apoptosis in Jurkat T cells.Infection and immunity · 2014Article
- The impact of autophagic processes on the intracellular fate of Helicobacter pylori: more tricks from an enigmatic pathogen?Autophagy · 2013Review
- Structural analysis of the oligomeric states of Helicobacter pylori VacA toxin.Journal of molecular biology · 2013Article
- The intermediate region of Helicobacter pylori VacA is a determinant of toxin potency in a Jurkat T cell assay.Infection and immunity · 2012Article
- Vacuolating cytotoxin A (VacA), a key toxin for Helicobacter pylori pathogenesis.Frontiers in cellular and infection microbiology · 2012Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Helicobacter pylori VacA is a pore-forming toxin that causes multiple alterations in human cells and contributes to the pathogenesis of peptic ulcer disease and gastric cancer. The toxin is secreted by H. pylori as an 88 kDa monomer (p88) consisting of two domains (p33 and p55). While an X-ray crystal structure for p55 exists and p88 oligomers have been visualized by cryo-electron microscopy, a detailed analysis of p33 has been hindered by an inability to purify this domain in an active form. In this study, we expressed and purified a recombinant form of p33 under denaturing conditions and optimized conditions for the refolding of the soluble protein. We show that refolded p33 can be added to purified p55 in trans to cause vacuolation of HeLa cells and inhibition of IL-2 production by Jurkat cells, effects identical to those produced by the p88 toxin from H. pylori. The p33 protein markedly enhances the cell binding properties of p55. Size exclusion chromatography experiments suggest that p33 and p55 assemble into a complex consistent with the size of a p88 monomer. Electron microscopy of these p33/p55 complexes reveals small rod-shaped structures that can convert to oligomeric flower-shaped structures in the presence of detergent. We propose that the oligomerization observed in these experiments mimics the process by which VacA oligomerizes when in contact with membranes of host cells.
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Registered trials
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.