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• W2040386489 abstract "and survive at low pH or might trigger inflammation in the infected stomach. VacA, a toxin expressed by most clinical isolates of H. pylori, meets both criteria. Coincubation of recombinant VacA protein with gastric cell lines induces vacuole formation in the cytoplasm (4), and VacA-expressing strains appear to colonize the stomach more efficiently (5). However, isogenic vacA mutants can colonize and trigger gastritis in both gnotobiotic piglets and Mongolian gerbils (6, 7). Thus, while VacA is clearly a type of virulence factor, it does not appear to be absolutely required for H. pylori virulence. VacA is expressed as a 140-kDa precursor that is processed to a functional 94-kDa toxin. Following export and exposure to acid, this toxin assembles spontaneously into oligomers. Three domains are required for its activity: a 33‐amino acid N-terminal signal sequence, which is cleaved from the mature protein but is required to direct the toxin to the periplasm; an Nterminal 37-kDa region, which contains the vacuolating activity; and a Cterminal 58-kDa region, which is required for binding of the protein to" @default.
• W2040386489 created "2016-06-24" @default.
• W2040386489 creator A5042603101 @default.
• W2040386489 date "2001-09-15" @default.
• W2040386489 modified "2023-09-22" @default.
• W2040386489 title "VacA pores as portable portals for urea" @default.
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• W2040386489 doi "https://doi.org/10.1172/jci14004" @default.
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