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Toxoplasma gondii rhoptry neck protein 4 (TgRON4) is a component of the moving junction, a key structure for host cell invasion. We previously showed that host cellular β-tubulin is a binding partner of TgRON4 in the invasion process. Here, to identify other binding partners of TgRON4 in the host cell, we examined the binding of TgRON4 to components of the host cell surface. TgRON4 binds to various mammalian cells, but this binding disappeared in glycosaminoglycan- and heparan sulfate-deficient CHO cells and after heparitinase treatment of mammalian cells. The C-terminal half of TgRON4 showed relatively strong binding to cells and heparin agarose. A glycoarray assay indicated that TgRON4 binds to heparin and modified heparin derivatives. Immunoprecipitation of T. gondii-infected CHO cell lysates showed that TgRON4 interacts with glypican 1 during Toxoplasma invasion. This interaction suggests a role for heparan sulfate in parasite invasion. Copyright © 2017 Elsevier B.V. All rights reserved.


Hitoshi Takemae, Kyousuke Kobayashi, Tatsuki Sugi, Yongmei Han, Haiyan Gong, Akiko Ishiwa, Frances C Recuenco, Fumi Murakoshi, Ryo Takano, Yuho Murata, Kisaburo Nagamune, Taisuke Horimoto, Hiroomi Akashi, Kentaro Kato. Toxoplasma gondii RON4 binds to heparan sulfate on the host cell surface. Parasitology international. 2017 Nov 18;67(2):123-130

PMID: 29081389

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