All subtypes of the cytotoxin VacA adsorb to the surface of Helicobacter pylori post-secretion

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All subtypes of the cytotoxin VacA adsorb to the surface of Helicobacter pylori post-secretion.

The major secreted virulence factor of Helicobacter pylori, the vacuolating cytotoxin VacA, is known to insert into eukaryotic membranes and has been observed in association with the surface of H. pylori cells that are actively producing it. Here, it is demonstrated that VacA is capable of interacting with the surface of H. pylori and Escherichia coli after secretion. It is shown that this inte...

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Helicobacter 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...

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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...

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Pleiotropic 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...

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Potent neutralization of vacuolating cytotoxin (VacA) of Helicobacter pylori by immunoglobulins against the soluble recombinant VacA.

BACKGROUND The recombinant vacuolating cytotoxin (rVacA) of Helicobacter pylori that retains native conformational epitopes was evaluated as a vaccine antigen for anti-H. pylori treatment. METHODS s1m1 vacA gene fraction encoding the mature VacA protein was expressed as a soluble protein in E. coli at low temperature. The efficacy of anti-rVacA antibody against VacA or H. pylori was assessed ...

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ژورنال

عنوان ژورنال: Journal of Medical Microbiology

سال: 2005

ISSN: 0022-2615,1473-5644

DOI: 10.1099/jmm.0.45946-0