ArticleThe Biochemical journal2004
Targeting of Helicobacter pylori vacuolating toxin to lipid raft membrane domains analysed by atomic force microscopy.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 49 citations in OpenAlex.
- Review
- Vacuolating Cytotoxin A (VacA) and Extracellular Vesicles inIranian journal of pathology · 2025Review
- There Are No Insurmountable Barriers: Passage of theMembranes · 2023Review
- Cell lipid biology in infections: an overview.Frontiers in cellular and infection microbiology · 2023Review
- Cryo-EM Analysis Reveals Structural Basis of Helicobacter pylori VacA Toxin Oligomerization.Journal of molecular biology · 2019Article
- Determinants of Raft Partitioning of the Helicobacter pylori Pore-Forming Toxin VacA.Infection and immunity · 2018Article
- Review
- 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
- Review
- Review
- Pore-forming Activity of the Escherichia coli Type III Secretion System Protein EspD.The Journal of biological chemistry · 2015Article
- Structural analysis of the oligomeric states of Helicobacter pylori VacA toxin.Journal of molecular biology · 2013Article
- Remodeling the host environment: modulation of the gastric epithelium by the Helicobacter pylori vacuolating toxin (VacA).Frontiers in cellular and infection microbiology · 2012Review
- The N-terminal amphipathic region of the Escherichia coli type III secretion system protein EspD is required for membrane insertion and function.Molecular microbiology · 2011Article
- Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA.Cellular microbiology · 2010Article
- Molecular imaging of membrane proteins and microfilaments using atomic force microscopy.Experimental & molecular medicine · 2010Review
- Reconstitution of Helicobacter pylori VacA toxin from purified components.Biochemistry · 2010Article
- Probing the lipid membrane dipole potential by atomic force microscopy.Biophysical journal · 2008Article
- Sphingomyelin functions as a novel receptor for Helicobacter pylori VacA.PLoS pathogens · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Helicobacter pylori vacuolating toxin VacA causes several effects on mammalian cells in vitro, including intracellular vacuolation, formation of pores in the plasma membrane and apoptosis. When added to cells, VacA becomes associated with detergent-resistant membranes, indicating that it binds preferentially to lipid rafts. In the present study, we have used atomic force microscopy to examine directly the association of VacA with lipid domains in supported lipid bilayers. VacA did not bind to lipid bilayers at pH 7.6. In contrast, at pH 4.0, VacA associated with the bilayers in the form of 26-nm oligomeric complexes. VacA bound to bilayers produced from either brain lipids or SM (sphingomyelin) plus cholesterol, each of which lacked detectable lipid domains. Bilayers composed of DOPC (dioleoylphosphatidylcholine), SM and cholesterol contained clearly visible raft-like domains, and VacA preferentially associated with these rafts. VacA bound poorly to raft-like domains in DOPC/SM bilayers, indicating that cholesterol is required for efficient association of VacA with lipid domains. When PS (phosphatidylserine), an anionic phospholipid that does not partition significantly into rafts, was added to the mixture of DOPC, SM and cholesterol, VacA was excluded from the rafts, indicating that it binds more avidly to PS than to the raft components. A typical plasma membrane exhibits pronounced lipid asymmetry, with SM enriched in the outer leaflet and PS in the inner leaflet. Therefore it is probable that the association of VacA with rafts in DOPC/SM/cholesterol bilayers represents a useful model for understanding the interactions of VacA with membranes in vivo.
Indexed as
Identifiers
What OpenQuestion holds
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.