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Published in: Thrombosis Journal 1/2013

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.
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Metadata
Title
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
Publication date
01-12-2013
Publisher
BioMed Central
Published in
Thrombosis Journal / Issue 1/2013
Electronic ISSN: 1477-9560
DOI
https://doi.org/10.1186/1477-9560-11-23

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