VacA, the vacuolating cytotoxin of Helicobacter pylori, binds to multimerin 1 on human platelets.
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.
Kaneo
K
Satoh
Toshiya
T
Hirayama
Katsuhiro
K
Takano
Katsue
K
Suzuki-Inoue
Tadashi
T
Sato
Masato
M
Ohta
Junko
J
Nakagomi
Department of Clinical and Laboratory Medicine, Faculty of Medicine, University of Yamanashi, 1110 Shimokato, 409-3898 Chuo, Yamanashi, Japan. yozaki@yamanashi.ac.jp.
Yukio
Y
Ozaki