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Furthermore, we also show that mGBP2 recognizes phosphatidic acid (PA) produced by the\n                    <jats:italic toggle=\"yes\">Legionella<\/jats:italic>\n                    effector Lpg2552 and fails to target the vacuole harboring Lpg2552-depleted\n                    <jats:italic toggle=\"yes\">L. pneumophila<\/jats:italic>\n                    . Consistently, this strain successfully grows in cells expressing mGBP2. We additionally identified lysine 585 (K585) of mGBP2 is required for the binding to PA and K585-mutated mGBP2 fails to recognize LCV. Interestingly, this lysine residue is only conserved in GBP1 among human GBPs and the conserved lysine residue is important for PA recognition and subsequent LCV distribution. Importantly,\n                    <jats:italic toggle=\"yes\">L. pneumophila<\/jats:italic>\n                    lacking Lpg2552 exhibits high resistance against IFN stimulation in THP-1-derived human macrophage.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2420096122","type":"journal-article","created":{"date-parts":[[2025,8,8]],"date-time":"2025-08-08T15:28:51Z","timestamp":1754666931000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Phosphatidic acid production on the vacuole harboring\n                    <i>Legionella pneumophila<\/i>\n                    is a signal for recognition of interferon-induced GTPases"],"prefix":"10.1073","volume":"122","author":[{"given":"Hiromu","family":"Oide","sequence":"first","affiliation":[{"name":"Department of Biomedical Sciences, School of Life Sciences, Tokyo University of Pharmacy and Life Sciences","place":["Hachioji, Tokyo, 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