Essential Domain of Receptor Tyrosine Phosphatase β (RPTPβ) for Interaction with Helicobacter pylori Vacuolating Cytotoxin
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چکیده
منابع مشابه
Vacuolating Cytotoxin of Helicobacter pylori
Vacuolating cytotoxin (VacA) is one of the most important virulence factors of H. pylori (Hp), which isthe only toxic protein that is secreted from Hp cell into the culture supernatant. The effects of VacA oneukaryotic systems is the subject of many previous and on going research studies. Intracellular targetsfor this toxin include: late endosomal and lysosomal compartments, m...
متن کاملHelicobacter pylori vacuolating cytotoxin, VacA.
Helicobacter pylori is the leading bacterial cause of food-borne illness worldwide and plays a major role in the development of chronic gastritis, peptic ulcer, and gastric cancer. Strains isolated from patients contain the cagA gene (cytotoxin-associated gene A) and produce the vacuolating cytotoxin, VacA. Recent molecular and cellular studies of VacA action have begun to unravel its structure...
متن کاملPleiotropic actions of Helicobacter pylori vacuolating cytotoxin, VacA.
Helicobacter pylori produces a vacuolating cytotoxin, VacA, and most virulent H. pylori strains secrete VacA. VacA binds to two types of receptor-like protein tyrosine phosphatase (RPTP), RPTPalpha and RPTPbeta, on the surface of host cells. VacA bound to RPTPbeta, relocates and concentrates in lipid rafts in the plasma membrane. VacA causes vacuolization, membrane anion-selective channel and p...
متن کاملOligomeric and subunit structure of the Helicobacter pylori vacuolating cytotoxin
Disease-associated strains of Helicobacter pylori produce a potent toxin that is believed to play a key role in peptic ulcer disease in man. In vitro the toxin causes severe vacuolar degeneration in target cells and has thus been termed VacA (for vacuolating cytotoxin A). Cytotoxic activity is associated with a > 600-kD protein consisting of several copies of a 95-kD polypeptide that undergoes ...
متن کاملBinding of the Helicobacter pylori vacuolating cytotoxin to target cells.
The vacuolating cytotoxin of Helicobacter pylori, VacA, enters the cytoplasm of target cells and causes vacuolar degeneration by interfering with late stages of endocytosis. By using indirect immunofluorescence and flow cytometry, we have demonstrated that VacA binds to specific high-affinity cell surface receptors and that this interaction is necessary for cell intoxication.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m406473200