{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T06:12:22Z","timestamp":1792735942093,"version":"4.5.0"},"reference-count":76,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2015,9,1]],"date-time":"2015-09-01T00:00:00Z","timestamp":1441065600000},"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":[[2015,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Intracellular growth of\n            <jats:named-content content-type=\"genus-species\">Legionella pneumophila<\/jats:named-content>\n            occurs in a replication vacuole constructed by host proteins that regulate vesicular traffic from the host endoplasmic reticulum (ER). This process is promoted by a combination of approximately 300 Icm\/Dot translocated substrates (IDTS). One of these proteins, Ceg9, was previously identified in a screen for\n            <jats:named-content content-type=\"genus-species\">L. pneumophila<\/jats:named-content>\n            IDTS that manipulate secretory traffic when overexpressed in yeast. Using ectopic expression of Ceg9 in mammalian cells, we demonstrate that Ceg9 interacts with isoforms of host reticulon 4 (Rtn4), a protein that regulates ER tubule formation. Binding occurs under conditions that prevent association with other known reticulon binding proteins, arguing that Ceg9 binding is stable. A tripartite complex was demonstrated among Rtn4, Ceg9, and atlastin 1, a previously characterized reticulon interacting partner. The binding of Ceg9 to Rtn4 was not due to bridging by atlastin 1 but resulted from the two interacting partners binding independently to reticulon. When Ceg9 is ectopically expressed in mammalian cells, it shows a localization pattern that is indistinguishable from that of Rtn4, perhaps due to interactions between and similar structural features of the two proteins. Consistent with Rtn4 playing a role in the formation of the\n            <jats:named-content content-type=\"genus-species\">Legionella<\/jats:named-content>\n            -containing vacuole, it was recruited to almost 50% of the vacuoles within 20 min postinfection. Our studies suggest that\n            <jats:named-content content-type=\"genus-species\">L. pneumophila<\/jats:named-content>\n            proteins interact with ER tubules at an early stage of replication vacuole formation.\n          <\/jats:p>","DOI":"10.1128\/iai.00507-15","type":"journal-article","created":{"date-parts":[[2015,6,23]],"date-time":"2015-06-23T01:31:23Z","timestamp":1435023083000},"page":"3479-3489","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":40,"title":["Endoplasmic Reticulum Tubule Protein Reticulon 4 Associates with the Legionella pneumophila Vacuole and with Translocated Substrate Ceg9"],"prefix":"10.1128","volume":"83","author":[{"given":"Eva","family":"Haenssler","sequence":"first","affiliation":[{"name":"Howard Hughes Medical Institute, Tufts University School of Medicine, Boston, Massachusetts, USA"},{"name":"Department of Molecular Biology and Microbiology, Tufts University School of 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