Toxoplasma gondii RON4 binds to heparan sulfate on the host cell surface

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

doi:10.1016/j.parint.2017.10.008

Toxoplasma gondii RON4 binds to heparan sulfate on the host cell surface

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

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	123-130
Number of pages	8
Journal	Parasitology International
Volume	67
Issue number	2
DOIs	https://doi.org/10.1016/j.parint.2017.10.008
Publication status	Published - 2018 Apr

Keywords

Flow cytometry
Glycoarray
Heparan sulfate
Toxoplasma

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.parint.2017.10.008

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title = "Toxoplasma gondii RON4 binds to heparan sulfate on the host cell surface",

abstract = "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.",

keywords = "Flow cytometry, Glycoarray, Heparan sulfate, Toxoplasma",

author = "Hitoshi Takemae and Kyousuke Kobayashi and Tatsuki Sugi and Yongmei Han and Haiyan Gong and Akiko Ishiwa and Recuenco, {Frances C.} and Fumi Murakoshi and Ryo Takano and Yuho Murata and Kisaburo Nagamune and Taisuke Horimoto and Hiroomi Akashi and Kentaro Kato",

note = "Funding Information: This study was supported by grant-in-Aids for Young Scientists, Exploratory Research, Scientific Research on Innovative Areas (3308) from the Ministry of Education, Culture, Science, Sports, and Technology (MEXT) of Japan, Bio-oriented Technology Research Advancement Institution (BRAIN), and the Program to Disseminate Tenure Tracking System from the Japan Science and Technology Agency (JST). Publisher Copyright: {\textcopyright} 2017 Elsevier B.V.",

year = "2018",

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doi = "10.1016/j.parint.2017.10.008",

language = "English",

volume = "67",

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T1 - Toxoplasma gondii RON4 binds to heparan sulfate on the host cell surface

AU - Takemae, Hitoshi

AU - Kobayashi, Kyousuke

AU - Sugi, Tatsuki

AU - Han, Yongmei

AU - Gong, Haiyan

AU - Ishiwa, Akiko

AU - Recuenco, Frances C.

AU - Murakoshi, Fumi

AU - Takano, Ryo

AU - Murata, Yuho

AU - Nagamune, Kisaburo

AU - Horimoto, Taisuke

AU - Akashi, Hiroomi

AU - Kato, Kentaro

N1 - Funding Information: This study was supported by grant-in-Aids for Young Scientists, Exploratory Research, Scientific Research on Innovative Areas (3308) from the Ministry of Education, Culture, Science, Sports, and Technology (MEXT) of Japan, Bio-oriented Technology Research Advancement Institution (BRAIN), and the Program to Disseminate Tenure Tracking System from the Japan Science and Technology Agency (JST). Publisher Copyright: © 2017 Elsevier B.V.

PY - 2018/4

Y1 - 2018/4

N2 - 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.

AB - 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.

KW - Flow cytometry

KW - Glycoarray

KW - Heparan sulfate

KW - Toxoplasma

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JO - Parasitology International

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ER -

Toxoplasma gondii RON4 binds to heparan sulfate on the host cell surface

Abstract

Keywords

UN SDGs

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