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 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.
Yahiro
K
K
Faculty of Engineering, Nagasaki University, Nagasaki, 852, Japan.
Niidome
T
T
Hatakeyama
T
T
Aoyagi
H
H
Kurazono
H
H
Padilla
P I
PI
Wada
A
A
Hirayama
T
T
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001427:Bacterial Toxins / Q000378:metabolism*; D018922:HL-60 Cells; D000882:Haplorhini; D016480:Helicobacter pylori / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D013274:Stomach Neoplasms / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D001426:Bacterial Proteins; D001427:Bacterial Toxins; D008565:Membrane Proteins; C074689:VacA protein, Helicobacter pylori