ArticleInfection and immunity2008
Helicobacter pylori VacA subdomain required for intracellular toxin activity and assembly of functional oligomeric complexes.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Vacuolating Cytotoxin A (VacA) and Extracellular Vesicles inIranian journal of pathology · 2025Review
- There Are No Insurmountable Barriers: Passage of theMembranes · 2023Review
- Clinical Pathogenesis, Molecular Mechanisms of Gastric Cancer Development.Current topics in microbiology and immunology · 2023Article
- Oxidative Products of Curcumin Rather Than Curcumin Bind toMolecules (Basel, Switzerland) · 2022Article
- Exotoxin-Targeted Drug Modalities as Antibiotic Alternatives.ACS infectious diseases · 2022Review
- Functional Properties of Oligomeric and Monomeric Forms of Helicobacter pylori VacA Toxin.Infection and immunity · 2021Article
- Cryo-EM Analysis Reveals Structural Basis of Helicobacter pylori VacA Toxin Oligomerization.Journal of molecular biology · 2019Article
- Cryo-EM structures ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Intracellular Degradation of Helicobacter pylori VacA Toxin as a Determinant of Gastric Epithelial Cell Viability.Infection and immunity · 2019Article
- Determinants of Raft Partitioning of the Helicobacter pylori Pore-Forming Toxin VacA.Infection and immunity · 2018Article
- Pleiotropic cytotoxicity of VacA toxin in host cells and its impact on immunotherapy.BioImpacts : BI · 2017Review
- 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
- Subdomain 2 of the Autotransporter Pet Is the Ligand Site for Recognizing the Pet Receptor on the Epithelial Cell Surface.Infection and immunity · 2016Article
- Review
- Expression and Antigenic Evaluation of VacA Antigenic Fragment of Helicobacter Pylori.Iranian journal of basic medical sciences · 2013Article
- 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 3 institutions in 1 country.
Funding
Abstract
Helicobacter pylori VacA is a secreted pore-forming toxin that is comprised of two domains, designated p33 and p55. The p55 domain has an important role in the binding of VacA to eukaryotic cell surfaces. A total of 111 residues at the amino terminus of p55 (residues 312 to 422) are essential for the intracellular activity of VacA, which suggests that this region may constitute a subdomain with an activity distinct from cell binding. To investigate the properties of this subdomain, a small deletion mutation (targeting aspartic acid 346 and glycine 347) was introduced into the H. pylori chromosomal vacA gene. Similar to wild-type VacA, the VacA Delta346-347 mutant protein was proteolytically processed, secreted, and bound to eukaryotic cells. However, VacA Delta346-347 did not cause cell vacuolation or membrane depolarization, and it was impaired in the ability to assemble into large water-soluble oligomeric structures. Interestingly, VacA Delta346-347 was able to physically interact with wild-type VacA to form mixed oligomeric complexes, and VacA Delta346-347 inhibited wild-type vacuolating activity in a dominant-negative manner. These data indicate that the assembly of functional oligomeric VacA complexes is dependent on specific sequences, including amino acids 346 and 347, within the p55 amino-terminal subdomain.
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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.