Helicobacter pylori vacuolating cytotoxin binding to a putative cell surface receptor, heparan sulfate, studied by surface plasmon resonance
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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 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.
متن کاملBinding of Sindbis virus to cell surface heparan sulfate.
Alphaviruses are arthropod-borne viruses with wide species ranges and diverse tissue tropisms. The cell surface receptors which allow infection of so many different species and cell types are still incompletely characterized. We show here that the widely expressed glycosaminoglycan heparan sulfate can participate in the binding of Sindbis virus to cells. Enzymatic removal of heparan sulfate or ...
متن کاملCharacterization of endostatin binding to heparin and heparan sulfate by surface plasmon resonance and molecular modeling: role of divalent cations.
Endostatin (20 kDa) is a C-terminal proteolytic fragment of collagen XVIII that is localized in vascular basement membrane zones in various organs. It binds zinc, heparin/heparan sulfate, laminin, and sulfatides and inhibits angiogenesis and tumor growth. Here we determined the kinetics and affinity of the interaction of endostatin with heparin/heparan sulfate and investigated the effects of di...
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ژورنال
عنوان ژورنال: FEMS Immunology & Medical Microbiology
سال: 2001
ISSN: 0928-8244,1574-695X
DOI: 10.1111/j.1574-695x.2001.tb01557.x