Toxin floats on lipid rafts

Toxin floats on lipid rafts
Credit: iStock

Helicobacter pylori, the leading cause of peptic ulcer disease and stomach cancer. One factor important to H. pylori infection is the pore-forming toxin VacA. It is thought to gain entry into host cells by binding to specialized membrane domains called lipid rafts.

Using Giant Plasma Membrane Vesicles (GPMVs), Anne Kenworthy, Ph.D., and colleagues studied how VacA binds to cell membranes.

They found that wild-type VacA toxin predominantly associated with the raft phase of GPMVs. Mutant VacA proteins that did not form oligomers or membrane channels still associated with , and a partial domain of the VacA protein was also capable of binding to lipid rafts.

The study, reported in Infection and Immunity, provides a direct measure of VacA's association with lipid rafts and defines features of the protein that mediate its affinity for raft domains. The findings are important for understanding the toxin's function in H. pylori infection.


Explore further

Helicobacter creates immune system blind spot

More information: Krishnan Raghunathan et al. Determinants of Raft Partitioning of the Helicobacter pylori Pore-Forming Toxin VacA, Infection and Immunity (2018). DOI: 10.1128/IAI.00872-17
Journal information: Infection and Immunity

Citation: Toxin floats on lipid rafts (2018, April 24) retrieved 16 June 2019 from https://medicalxpress.com/news/2018-04-toxin-lipid-rafts.html
This document is subject to copyright. Apart from any fair dealing for the purpose of private study or research, no part may be reproduced without the written permission. The content is provided for information purposes only.
3 shares

Feedback to editors

User comments

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more