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Alliance"],"published-print":{"date-parts":[[2020,1]]},"abstract":"<jats:p><jats:italic>Toxoplasma gondii<\/jats:italic>is an obligate intracellular protozoan parasite capable of infecting warm-blooded animals by ingestion. The organism enters host cells and resides in the cytoplasm in a membrane-bound parasitophorous vacuole (PV). Inducing an interferon response enables IFN-\u03b3\u2013inducible immunity-related GTPase (IRG protein) to accumulate on the PV and to restrict parasite growth. However, little is known about the mechanisms by which IRG proteins recognize and destroy<jats:italic>T. gondii<\/jats:italic>PV. We characterized the role of IRG protein Irgb6 in the cell-autonomous response against<jats:italic>T. gondii<\/jats:italic>, which involves vacuole ubiquitination and breakdown. We show that Irgb6 is capable of binding a specific phospholipid on the PV membrane. Furthermore, the absence of Irgb6 causes reduced targeting of other effector IRG proteins to the PV. This suggests that Irgb6 has a role as a pioneer in the process by which multiple IRG proteins access the PV. Irgb6-deficient mice are highly susceptible to infection by a strain of<jats:italic>T. gondii<\/jats:italic>avirulent in wild-type mice.<\/jats:p>","DOI":"10.26508\/lsa.201900549","type":"journal-article","created":{"date-parts":[[2019,12,18]],"date-time":"2019-12-18T18:45:22Z","timestamp":1576694722000},"page":"e201900549","update-policy":"https:\/\/doi.org\/10.26508\/lsa.crossmarkpolicy","source":"Crossref","is-referenced-by-count":27,"title":["Initial phospholipid-dependent Irgb6 targeting to<i>Toxoplasma gondii<\/i>vacuoles mediates host defense"],"prefix":"10.26508","volume":"3","author":[{"given":"Youngae","family":"Lee","sequence":"first","affiliation":[{"name":"Department of Immunoparasitology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan"},{"name":"Laboratory of Immunoparasitology, WPI Immunology Frontier Research Center, Osaka University, Osaka, 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