ArticleJournal of molecular biology2013
Structural analysis of the oligomeric states of Helicobacter pylori VacA toxin.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.
- Association of Helicobacter pylori vacA genotypes and peptic ulcer in Iranian population: a systematic review and meta-analysis.BMC gastroenterology · 2020Pooled it
- Review
- Structure-guided identification of a potential inhibitor targeting the VacA toxin of Helicobacter pylori.PloS one · 2026Article
- 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
- 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
- Helicobacter pyloriBioengineered · 2022Article
- Functional Properties of Oligomeric and Monomeric Forms of Helicobacter pylori VacA Toxin.Infection and immunity · 2021Article
- Review
- Functional Properties of Helicobacter pylori VacA Toxin m1 and m2 Variants.Infection and immunity · 2020Article
- Multiple Pleomorphic Tetramers of Thermostable Direct Hemolysin from Grimontia hollisae in Exerting Hemolysis and Membrane Binding.Scientific reports · 2019Article
- 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
- Determinants of Raft Partitioning of the Helicobacter pylori Pore-Forming Toxin VacA.Infection and immunity · 2018Article
- Review
- While the revolution will not be crystallized, biochemistry reigns supreme.Protein science : a publication of the Protein Society · 2017Review
- 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
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Helicobacter pylori is a Gram-negative bacterium that colonizes the human stomach and contributes to peptic ulceration and gastric adenocarcinoma. H. pylori secretes a pore-forming exotoxin known as vacuolating toxin (VacA). VacA contains two distinct domains, designated p33 and p55, and assembles into large "snowflake"-shaped oligomers. Thus far, no structural data are available for the p33 domain, which is essential for membrane channel formation. Using single-particle electron microscopy and the random conical tilt approach, we have determined the three-dimensional structures of six VacA oligomeric conformations at ~15-Å resolution. The p55 domain, composed primarily of β-helical structures, localizes to the peripheral arms, while the p33 domain consists of two globular densities that localize within the center of the complexes. By fitting the VacA p55 crystal structure into the electron microscopy densities, we have mapped inter-VacA interactions that support oligomerization. In addition, we have examined VacA variants/mutants that differ from wild-type (WT) VacA in toxin activity and/or oligomeric structural features. Oligomers formed by VacA∆6-27, a mutant that fails to form membrane channels, lack an organized p33 central core. Mixed oligomers containing both WT and VacA∆6-27 subunits also lack an organized core. Oligomers formed by a VacA s2m1 chimera (which lacks cell-vacuolating activity) and VacAΔ301-328 (which retains vacuolating activity) each contain p33 central cores similar to those of WT oligomers. By providing the most detailed view of the VacA structure to date, these data offer new insights into the toxin's channel-forming component and the intermolecular interactions that underlie oligomeric assembly.
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Registered trials
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