Abstract
VacA, the major exotoxin produced by Helicobacter pylori, is composed of identical 87-kDa monomers that assemble into flower-shaped oligomers. The monomers can be proteolytically cleaved into two moieties of 37 and 58 kDa, or P37 and P58. The most studied property of VacA is the alteration of intracellular vesicular trafficking in eukaryotic cells leading to the formation of large vacuoles containing markers of late endosomes and lysosomes. However, VacA also causes a reduction in trans-epithelial electrical resistance in polarized monolayers and forms ion channels in lipid bilayers. The ability to induce vacuoles is localized mostly but not entirely in P37, while P58 is involved in cell targeting. Here, we review the structural aspects of VacA biology.
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