Abstract
For a virulence factor secreted by a pathogen, identification of the active conformation is complicated by the fact that the protein is often translocated into the host cell cytosol. Using a variety of techniques, the vacuolating cytotoxin VacA, which is produced by Helicobacter pylori, has been shown to exist as monomers as well as large oligomeric structures. The amino- and carboxy-terminal regions of VacA are connected by a protease-sensitive loop. However, until recently, it remained unclear whether the independent fragments of the toxin were active in the host cell cytosol, or whether the toxin acted as a complex.
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