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Another approach would be to use probiotics. Probiotics prevent infection with pathogenic bacteria both through activation of the host's immune system and through direct competition of the probiotic bacteria with the pathogen. There is good evidence that H. pylori is killed by lactobacilli both in vitro and to a limited extent in vivo (24, 25, 76, 93, 373, 426, 540). It is unlikely that such an approach will lead to complete eradication of H. pylori bacteria in the stomach, but, as indicated above, complete eradication is not needed to prevent disease: either reduction of the amount of bacteria or altering of the immune response might result in a significant decrease in inflammation, thus reducing the induction of peptic ulcers and cancer.
The VacA protein influences cellular processes via different routes, thus assisting in chronic colonization of the gastric mucosa by H. pylori. (1) Surface-bound VacA may be directly delivered to the cell membrane. Secreted VacA may either (2) bind to a cell membrane receptor and initiate a proinflammatory response, (3) be taken up directly by the cell and be trafficked to the mitochondria and induce apoptosis, (4) be taken up by pinocytosis and induce vacuolization, (5) form a membrane channel, resulting in leakage of nutrients to the extracellular space, or (6) pass through the tight junctions and inhibit T-cell activation and proliferation. (Modified with permission from Nature Reviews Microbiology [101], copyright Macmillan Magazines Ltd.)
Secreted VacA can be further processed into a 33-kDa N-terminal fragment and a 55-kDa C-terminal fragment through proteolytic cleavage. The N-terminal protein performs an essential function in the formation of anion channels, while the C-terminal protein mediates cell binding (293, 314, 483, 633). In spite of the proteolytic cleavage, these fragments remain noncovalently associated with each other (621). Purified VacA spontaneously forms oligomeric aggregates (>900 kDa) and upon exposure to acidic pH disassembles into the active monomers that form pores in the cell membrane (104, 380, 436). This autoaggregation and subsequent acid activation have been claimed to be crucial for the toxic activity (434, 629) but are likely to be an in vitro artifact (286, 363, 498). 2ff7e9595c
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