1. VacA, the vacuolating cytotoxin of Helicobacter pylori, binds to multimerin 1 on human platelets
- Author
-
Toshiya Hirayama, Tadashi Sato, Junko Nakagomi, Yukio Ozaki, Masato Ohta, Kaneo Satoh, Katsue Suzuki-Inoue, and Katsuhiro Takano
- Subjects
Original Basic Research ,business.industry ,Binding protein ,Platelet ,Multimerin 1 ,VacA ,Dot blot ,Multimerin1 ,Context (language use) ,Hematology ,bacterial infections and mycoses ,medicine.disease_cause ,digestive system diseases ,Microbiology ,CD62P ,ITP ,bacteria ,Medicine ,Platelet activation ,Binding site ,business ,Peptide sequence ,Exotoxin - 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.
- Published
- 2013
- Full Text
- View/download PDF