Amino-Terminal Hydrophobic Region of Helicobacter pylori Vacuolating Cytotoxin (VacA) Mediates Transmembrane Protein Dimerization
نویسندگان
چکیده
منابع مشابه
Amino-terminal hydrophobic region of Helicobacter pylori vacuolating cytotoxin (VacA) mediates transmembrane protein dimerization.
Helicobacter pylori VacA is a secreted protein toxin that forms channels in lipid bilayers and induces multiple structural and functional alterations in eukaryotic cells. A unique hydrophobic segment at the amino terminus of VacA contains three tandem repeats of a GxxxG motif that is characteristic of transmembrane dimerization sequences. To examine functional properties of this region, we expr...
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 کاملVacuolating 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 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 کاملPotent 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: Infection and Immunity
سال: 2001
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.69.2.1181-1184.2001