Helicobacter pylori vacuolating cytotoxin binds to the 140-kDa protein in human gastric cancer cell lines, AZ-521 and AGS

To investigatie a potential mechanism of how Helicobacter pylori establishes infection, we purified a lot of vacuolating toxin (VacA) from supernatant of H. pylori ATCC49503 (tox+ strain 60190). We used an antibody which was prepared by immunizing rabbits with a synthetic peptide consisting of 16 am...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-09, Vol.238 (2), p.629-632
Main Authors: Yahiro, K, Niidome, T, Hatakeyama, T, Aoyagi, H, Kurazono, H, Padilla, P I, Wada, A, Hirayama, T
Format: Article
Language:English
Subjects:
Animals
Bacterial Proteins - metabolism
Bacterial Toxins - metabolism
Haplorhini
Helicobacter pylori - metabolism
HL-60 Cells
Humans
Membrane Proteins - metabolism
Protein Binding
Rabbits
Stomach Neoplasms - metabolism
Tumor Cells, Cultured
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Summary:To investigatie a potential mechanism of how Helicobacter pylori establishes infection, we purified a lot of vacuolating toxin (VacA) from supernatant of H. pylori ATCC49503 (tox+ strain 60190). We used an antibody which was prepared by immunizing rabbits with a synthetic peptide consisting of 16 amino acids reflecting a portion (Glu69-Arg83) of amino acid sequence of Vac A. VacA caused vacuoles in human gastric cancer cell lines AZ-521 AGS, and monkey kidney cell line COS-7, but not human promyeloblastic cell line HL-60. By immunoprecipitation analysis using anti VacA antibody, a biotinylated cell surface protein of 140kDa (p140) was precipitated only when the lysates of VacA-susceptible cells were incubated with VacA but not with inactivated VacA, indicating the association of p140 with VacA.
ISSN:0006-291X
DOI:10.1006/bbrc.1997.7345