VacA, the vacuolating cytotoxin of Helicobacter pylori, binds to multimerin 1 on human platelets.
VacA, the vacuolating cytotoxin of Helicobacter pylori, binds to multimerin 1 on human platelets.
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VACA是幽门螺杆菌的螺旋杆菌的液泡细胞毒素，与人血小板上的多粒蛋白1结合。
DOI：
10.1186/1477-9560-11-23
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发表时间：
2013-11-12
影响因子：
3.1
通讯作者：
Ozaki Y
中科院分区：
文献类型：
--
作者：
Satoh K;Hirayama T;Takano K;Suzuki-Inoue K;Sato T;Ohta M;Nakagomi J;Ozaki Y
感染H. pylori在人类和小鼠中的作用。我们研究了H. pylori在此背景下酸活化的VacA，但不加热VacA，诱导血小板CD 62 P的表达。然而，VacA与血小板膜上存在的所谓VacA受体无反应。因此，我们分析了通过VacA亲和层析获得的VacA相关蛋白，使用MALDI-TOF-MS。Multimerin 1在两个连续的实验中被检测到，作为VacA的结合蛋白。等离子体共振证实了它们的结合，斑点印迹分析显示多聚体蛋白1的肽序列AA 321-340是VacA的结合位点。总之，我们提出了一个新的多聚体蛋白1和VacA之间的相互作用，这可能会给另一个洞察H。幽门螺杆菌诱导的血小板活化。幽门感染
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.