Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA.

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 previ

SUBMITTER: Gupta VR 

PROVIDER: S-EPMC2980835 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature