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Toxins 2010, 2(1), 69-92; doi:10.3390/toxins2010069

The Versatility of the Helicobacter pylori Vacuolating Cytotoxin VacA in Signal Transduction and Molecular Crosstalk

Ardmore House, School of Biomolecular and Biomedical Sciences, Belfield Campus, University College Dublin, Dublin-4, Ireland
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Author to whom correspondence should be addressed.
Received: 3 December 2009 / Revised: 31 December 2009 / Accepted: 14 January 2010 / Published: 15 January 2010
(This article belongs to the Special Issue Bacterial Protein Toxins)
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Abstract

By modulating important properties of eukaryotic cells, many bacterial protein toxins highjack host signalling pathways to create a suitable niche for the pathogen to colonize and persist. Helicobacter pylori VacA is paradigm of pore-forming toxins which contributes to the pathogenesis of peptic ulceration. Several cellular receptors have been described for VacA, which exert different effects on epithelial and immune cells. The crystal structure of VacA p55 subunit might be important for elucidating details of receptor interaction and pore formation. Here we discuss the multiple signalling activities of this important toxin and the molecular crosstalk between VacA and other virulence factors.
Keywords: Helicobacter pylori; signalling; type IV secretion; CagA; pathogenicity island; vacuolating cytotoxin; VacA; lipid rafts Helicobacter pylori; signalling; type IV secretion; CagA; pathogenicity island; vacuolating cytotoxin; VacA; lipid rafts
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Backert, S.; Tegtmeyer, N. The Versatility of the Helicobacter pylori Vacuolating Cytotoxin VacA in Signal Transduction and Molecular Crosstalk. Toxins 2010, 2, 69-92.

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