Published in:
Open Access
01-12-2013 | Original basic research
VacA, the vacuolating cytotoxin of Helicobacter pylori, binds to multimerin 1 on human platelets
Authors:
Kaneo Satoh, Toshiya Hirayama, Katsuhiro Takano, Katsue Suzuki-Inoue, Tadashi Sato, Masato Ohta, Junko Nakagomi, Yukio Ozaki
Published in:
Thrombosis Journal
|
Issue 1/2013
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Abstract
Platelets were activated under the infection with H. pylori in human and mice. We investigated the role of VacA, an exotoxin released by H. pylori in this context. Acid-activated VacA, but not heated VacA, induced platelet CD62P expression. However, VacA reacted with none of the alleged VacA receptors present on platelet membranes. We therefore analyzed VacA associated proteins obtained through VacA affinity chromatography, using MALDI-TOF-MS. Multimerin1 was detected in two consecutive experiments, as the binding protein for VacA. Plasmon resonance confirmed their binding, and dot blot analysis revealed that the peptide sequence AA 321-340 of multimerin 1 is the binding site for VacA. In conclusion, we propose a new interaction between multimerin1 and VacA , which may give another insight into H. pylori-induced platelet activations under H. pylori infection.