{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T08:13:27Z","timestamp":1790669607745,"version":"4.1.0"},"reference-count":63,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2014,10,1]],"date-time":"2014-10-01T00:00:00Z","timestamp":1412121600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2014,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:named-content content-type=\"genus-species\">Legionella<\/jats:named-content>\n            spp. cause the severe pneumonia Legionnaires' disease. The environmental bacteria replicate intracellularly in free-living amoebae and human alveolar macrophages within a distinct, endoplasmic reticulum (ER)-derived compartment termed the\n            <jats:named-content content-type=\"genus-species\">Legionella<\/jats:named-content>\n            -containing vacuole (LCV). LCV formation requires the bacterial Icm\/Dot type IV secretion system (T4SS) that translocates into host cells a plethora of different \u201ceffector\u201d proteins, some of which anchor to the pathogen vacuole by binding to phosphoinositide (PI) lipids. Here, we identified by unbiased pulldown assays in\n            <jats:named-content content-type=\"genus-species\">Legionella longbeachae<\/jats:named-content>\n            lysates a 111-kDa SidC homologue as the major phosphatidylinositol 4-phosphate [PtdIns(4)\n            <jats:italic>P<\/jats:italic>\n            ]-binding protein. The PI-binding domain was mapped to a 20-kDa P4C [\n            <jats:underline>P<\/jats:underline>\n            tdIns(\n            <jats:underline>4<\/jats:underline>\n            )\n            <jats:italic>P<\/jats:italic>\n            binding of Sid\n            <jats:underline>C<\/jats:underline>\n            ] fragment. Isothermal titration calorimetry revealed that SidC of\n            <jats:named-content content-type=\"genus-species\">L. longbeachae<\/jats:named-content>\n            (SidC\n            <jats:sub>Llo<\/jats:sub>\n            ) binds PtdIns(4)\n            <jats:italic>P<\/jats:italic>\n            with a\n            <jats:italic>\n              K\n              <jats:sub>d<\/jats:sub>\n            <\/jats:italic>\n            (dissociation constant) of 71 nM, which is 3 to 4 times lower than that of the SidC orthologue of\n            <jats:named-content content-type=\"genus-species\">Legionella pneumophila<\/jats:named-content>\n            (SidC\n            <jats:sub>Lpn<\/jats:sub>\n            ). Upon infection of RAW 264.7 macrophages with\n            <jats:named-content content-type=\"genus-species\">L. longbeachae<\/jats:named-content>\n            , endogenous SidC\n            <jats:sub>Llo<\/jats:sub>\n            or ectopically produced SidC\n            <jats:sub>Lpn<\/jats:sub>\n            localized in an Icm\/Dot-dependent manner to the PtdIns(4)\n            <jats:italic>P<\/jats:italic>\n            -positive LCVs. An\n            <jats:named-content content-type=\"genus-species\">L. longbeachae<\/jats:named-content>\n            \u0394\n            <jats:italic>sidC<\/jats:italic>\n            deletion mutant was impaired for calnexin recruitment to LCVs in\n            <jats:named-content content-type=\"genus-species\">Dictyostelium discoideum<\/jats:named-content>\n            amoebae and outcompeted by wild-type bacteria in\n            <jats:named-content content-type=\"genus-species\">Acanthamoeba castellanii<\/jats:named-content>\n            . Calnexin recruitment was restored by SidC\n            <jats:sub>Llo<\/jats:sub>\n            or its orthologues SidC\n            <jats:sub>Lpn<\/jats:sub>\n            and SdcA\n            <jats:sub>Lpn<\/jats:sub>\n            . Conversely, calnexin recruitment was restored by SidC\n            <jats:sub>Llo<\/jats:sub>\n            in\n            <jats:named-content content-type=\"genus-species\">L. pneumophila<\/jats:named-content>\n            lacking\n            <jats:italic>sidC<\/jats:italic>\n            and\n            <jats:italic>sdcA<\/jats:italic>\n            . Together, biochemical, genetic, and cell biological data indicate that SidC\n            <jats:sub>Llo<\/jats:sub>\n            is an\n            <jats:named-content content-type=\"genus-species\">L. longbeachae<\/jats:named-content>\n            effector that binds through a P4C domain with high affinity to PtdIns(4)\n            <jats:italic>P<\/jats:italic>\n            on LCVs, promotes ER recruitment to the LCV, and thus plays a role in pathogen-host interactions.\n          <\/jats:p>","DOI":"10.1128\/iai.01685-14","type":"journal-article","created":{"date-parts":[[2014,7,15]],"date-time":"2014-07-15T05:03:41Z","timestamp":1405400621000},"page":"4021-4033","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":61,"title":["The Legionella longbeachae Icm\/Dot Substrate SidC Selectively Binds Phosphatidylinositol 4-Phosphate with Nanomolar Affinity and Promotes Pathogen Vacuole-Endoplasmic Reticulum Interactions"],"prefix":"10.1128","volume":"82","author":[{"given":"Stephanie","family":"Dolinsky","sequence":"first","affiliation":[{"name":"Max von Pettenkofer Institute, Department of Medicine, Ludwig-Maximilians University Munich, Munich, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ina","family":"Haneburger","sequence":"additional","affiliation":[{"name":"Max von Pettenkofer Institute, Department of Medicine, Ludwig-Maximilians University Munich, Munich, Germany"},{"name":"Institute of Medical Microbiology, Department of Medicine, University of Z\u00fcrich, Z\u00fcrich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adam","family":"Cichy","sequence":"additional","affiliation":[{"name":"Center for Integrated Protein Science Munich, Department of Chemistry, Technical University Munich, Garching, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mandy","family":"Hannemann","sequence":"additional","affiliation":[{"name":"Center for Integrated Protein Science Munich, Department of Chemistry, Technical University Munich, Garching, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aymelt","family":"Itzen","sequence":"additional","affiliation":[{"name":"Center for Integrated Protein Science Munich, Department of Chemistry, Technical University Munich, Garching, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hubert","family":"Hilbi","sequence":"additional","affiliation":[{"name":"Max von Pettenkofer Institute, Department of Medicine, Ludwig-Maximilians University Munich, Munich, Germany"},{"name":"Institute of Medical Microbiology, Department of Medicine, University of Z\u00fcrich, Z\u00fcrich, 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