ArticleCellular microbiology2010
Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA.
Article in Cellular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed, 46 citations in OpenAlex.
- Bacterial Toxin Exploits Host Membrane Phospholipid as a Receptor for Binding, Entry, and Cytopathogenicity.Molecular microbiology · 2026Article
- 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
- Restoration of mitochondrial structure and function withinAdvances in microbiology · 2023Article
- Cell lipid biology in infections: an overview.Frontiers in cellular and infection microbiology · 2023Review
- The CPNE Family and Their Role in Cancers.Frontiers in genetics · 2021Review
- Functional Properties of Helicobacter pylori VacA Toxin m1 and m2 Variants.Infection and immunity · 2020Article
- A Comprehensive Review on the Manipulation of the Sphingolipid Pathway by Pathogenic Bacteria.Frontiers in cell and developmental biology · 2019Review
- Article
- Helicobacter pylori Infection Modulates Host Cell Metabolism through VacA-Dependent Inhibition of mTORC1.Cell host & microbe · 2018Article
- Determinants of Raft Partitioning of the Helicobacter pylori Pore-Forming Toxin VacA.Infection and immunity · 2018Article
- Helicobacter pylori targets mitochondrial import and components of mitochondrial DNA replication machinery through an alternative VacA-dependent and a VacA-independent mechanisms.Scientific reports · 2017Article
- Review
- Pleiotropic cytotoxicity of VacA toxin in host cells and its impact on immunotherapy.BioImpacts : BI · 2017Review
- Helicobacter pylori VacA, acting through receptor protein tyrosine phosphatase α, is crucial for CagA phosphorylation in human duodenum carcinoma cell line AZ-521.Disease models & mechanisms · 2016Article
- Review
- Review
- Review
- Role of connexin 43 in Helicobacter pylori VacA-induced cell death.Infection and immunity · 2014Article
- Co-development of diagnostic vectors to support targeted therapies and theranostics: essential tools in personalized cancer therapy.Frontiers in oncology · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Plasma membrane sphingomyelin (SM) binds the Helicobacter pylori vacuolating toxin (VacA) to the surface of epithelial cells. To evaluate the importance of SM for VacA cellular entry, we characterized toxin uptake and trafficking within cells enriched with synthetic variants of SM, whose intracellular trafficking properties are strictly dependent on the acyl chain lengths of their sphingolipid backbones. While toxin binding to the surface of cells was independent of acyl chain length, cells enriched with 12- or 18-carbon acyl chain variants of SM (e.g. C12-SM or C18-SM) were more sensitive to VacA, as indicated by toxin-induced cellular vacuolation, than those enriched with shorter 2- or 6-carbon variants (e.g. C2-SM or C6-SM). In C18-SM-enriched cells, VacA was taken into cells by a previously described Cdc42-dependent pinocytic mechanism, localized initially to GPI-enriched vesicles, and ultimately trafficked to Rab7/Lamp1 compartments. In contrast, within C2-SM-enriched cells, VacA was taken up at a slower rate by a Cdc42-independent mechanism and trafficked to Rab11 compartments. VacA-associated predominantly with detergent-resistant membranes (DRMs) in cells enriched with C18-SM, but predominantly with non-DRMs in C2-SM-enriched cells. These results suggest that SM is required for targeting VacA to membrane rafts important for subsequent Cdc42-dependent pinocytic cellular entry.
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