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Novel toxin receptor discovered for ulcer-causing stomach pathogen
Date:5/23/2008

nes (again, in the presence of VacA), the vacuoles returned.

This is the first example of a bacterial virulence factor that uses sphingomyelin as a receptor, Blanke said. Only sphingomyelin confers sensitivity to the toxin in these cells, whereas other common membrane lipids do not.

Sphingomyelin recently was discovered to have the ability to cluster into specialized membrane islands, or rafts, that look like raised platforms on the cell surface.

Blankes team found that VacA preferentially binds to and enters the cell by means of these sphingomyelin rafts.

Our model is that these platforms serve as the entry portals for the toxin into the cell, Blanke said. We think that sphingomyelin is important because it seems to cluster the toxin in these portals of entry. This seems to be absolutely essential for toxin activity.

Finding the mechanism by which the toxin gets into cells is of great interest to those hoping to treat H. pylori infection, Blanke said.

Identifying toxin receptors is important because they are outstanding targets for new drugs to block the action of toxins on human cells, he said.

Also, because some bacterial toxins are so adept at breeching the membrane barrier to enter human cells, this work may also point the way to new strategies for sending protein-based pharmaceuticals into the cell, he said.


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Contact: Diana Yates
diya@illinois.edu
217-333-5802
University of Illinois at Urbana-Champaign
Source:Eurekalert  

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