{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T15:40:21Z","timestamp":1791214821083,"version":"4.1.0"},"reference-count":167,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2020,1,30]],"date-time":"2020-01-30T00:00:00Z","timestamp":1580342400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001711","name":"Schweizerischer Nationalfonds zur F\u00f6rderung der Wissenschaftlichen Forschung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001711","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006447","name":"Universit\u00e4t Z\u00fcrich","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006447","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"DOI":"10.3389\/fimmu.2020.00025","type":"journal-article","created":{"date-parts":[[2020,1,30]],"date-time":"2020-01-30T04:34:11Z","timestamp":1580358851000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":56,"title":["Phosphoinositides and the Fate of Legionella in Phagocytes"],"prefix":"10.3389","volume":"11","author":[{"given":"A. Leoni","family":"Swart","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hubert","family":"Hilbi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2020,1,30]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"286","DOI":"10.1111\/j.1758-2229.2011.00247.x","article-title":"Legionella spp. outdoors: colonization, communication and persistence","volume":"3","author":"Hilbi","year":"2011","journal-title":"Environ Microbiol Rep."},{"key":"B2","doi-asserted-by":"publisher","first-page":"274","DOI":"10.1128\/CMR.00052-09","article-title":"Molecular pathogenesis of infections caused by Legionella pneumophila","volume":"23","author":"Newton","year":"2010","journal-title":"Clin Microbiol Rev"},{"key":"B3","doi-asserted-by":"publisher","first-page":"21660","DOI":"10.3390\/ijms141121660","article-title":"Biofilms: the stronghold of Legionella pneumophila","volume":"14","author":"Abdel-Nour","year":"2013","journal-title":"Int J Mol Sci"},{"key":"B4","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1111\/j.1462-2920.2009.02025.x","article-title":"Biofilms: the environmental playground of Legionella pneumophila","volume":"12","author":"Declerck","year":"2010","journal-title":"Environ Microbiol"},{"key":"B5","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1007\/s00248-009-9514-z","article-title":"Legionella, protozoa, and biofilms: interactions within complex microbial systems","volume":"58","author":"Taylor","year":"2009","journal-title":"Microb Ecol"},{"key":"B6","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1111\/j.1462-5822.2009.01398.x","article-title":"Caenorhabditis is a metazoan host for Legionella","volume":"12","author":"Brassinga","year":"2010","journal-title":"Cell Microbiol"},{"key":"B7","doi-asserted-by":"publisher","first-page":"4105","DOI":"10.1128\/AEM.03021-09","article-title":"Caenorhabditis elegans as an alternative model host for Legionella pneumophila, and protective effects of Bifidobacterium infantis","volume":"76","author":"Komura","year":"2010","journal-title":"Appl Environ Microbiol"},{"key":"B8","doi-asserted-by":"publisher","first-page":"563","DOI":"10.1111\/j.1462-2920.2007.01238.x","article-title":"Environmental predators as models for bacterial pathogenesis","volume":"9","author":"Hilbi","year":"2007","journal-title":"Environ Microbiol"},{"key":"B9","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1016\/j.ijmm.2016.05.012","article-title":"Legionella-protozoa-nematode interactions in aquatic biofilms and influence of Mip on Caenorhabditis elegans colonization","volume":"306","author":"Rasch","year":"2016","journal-title":"Int J Med Microbiol"},{"key":"B10","doi-asserted-by":"publisher","first-page":"286","DOI":"10.1016\/0966-842X(96)10041-X","article-title":"The molecular ecology of Legionellae","volume":"4","author":"Fields","year":"1996","journal-title":"Trends Microbiol"},{"key":"B11","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1111\/cmi.12235","article-title":"The natural alternative: protozoa as cellular models for Legionella infection","volume":"16","author":"Hoffmann","year":"2014","journal-title":"Cell Microbiol"},{"key":"B12","doi-asserted-by":"publisher","first-page":"61","DOI":"10.3389\/fcimb.2018.00061","article-title":"Acanthamoeba and Dictyostelium as cellular models for Legionella infection","volume":"8","author":"Swart","year":"2018","journal-title":"Front Cell Infect Microbiol"},{"key":"B13","doi-asserted-by":"publisher","first-page":"579","DOI":"10.3201\/eid1704.100446","article-title":"Legionella longbeachae and legionellosis","volume":"17","author":"Whiley","year":"2011","journal-title":"Emerg Infect Dis"},{"key":"B14","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1056\/NEJMc1505356","article-title":"Probable person-to-person transmission of Legionnaires' disease","volume":"374","author":"Correia","year":"2016","journal-title":"N Engl J Med"},{"key":"B15","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1016\/j.tim.2012.03.005","article-title":"Exploitation of evolutionarily conserved amoeba and mammalian processes by Legionella","volume":"20","author":"Al-Quadan","year":"2012","journal-title":"Trends Microbiol"},{"key":"B16","doi-asserted-by":"publisher","first-page":"208","DOI":"10.3389\/fmicb.2011.00208","article-title":"Comparative and functional genomics of Legionella identified eukaryotic like proteins as key players in host-pathogen interactions","volume":"2","author":"Gomez-Valero","year":"2011","journal-title":"Front Microbiol"},{"key":"B17","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1038\/nrmicro1967","article-title":"The Legionella pneumophila replication vacuole: making a cosy niche inside host cells","volume":"7","author":"Isberg","year":"2009","journal-title":"Nat Rev Microbiol"},{"key":"B18","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1146\/annurev-cellbio-100913-013439","article-title":"Bacterial pathogen manipulation of host membrane trafficking","volume":"30","author":"Asrat","year":"2014","journal-title":"Annu Rev Cell Dev Biol"},{"key":"B19","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1016\/j.tim.2016.02.003","article-title":"Subversion of retrograde trafficking by translocated pathogen effectors","volume":"24","author":"Personnic","year":"2016","journal-title":"Trends Microbiol"},{"key":"B20","doi-asserted-by":"publisher","first-page":"482","DOI":"10.3389\/fcimb.2017.00482","article-title":"Formation of the Legionella replicative compartment at the crossroads of retrograde trafficking","volume":"7","author":"B\u00e4rlocher","year":"2017","journal-title":"Front Cell Infect Microbiol"},{"key":"B21","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/j.ijmm.2017.08.004","article-title":"Formation of the Legionella-containing vacuole: phosphoinositide conversion, GTPase modulation and ER dynamics","volume":"308","author":"Steiner","year":"2018","journal-title":"Int J Med Microbiol"},{"key":"B22","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1126\/science.1067025","article-title":"A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes","volume":"295","author":"Nagai","year":"2002","journal-title":"Science"},{"key":"B23","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1007\/82_2013_340","article-title":"Modulation of small GTPases by Legionella","volume":"376","author":"Goody","year":"2013","journal-title":"Curr Top Microbiol Immunol"},{"key":"B24","doi-asserted-by":"publisher","first-page":"1034","DOI":"10.1111\/cmi.12256","article-title":"Functional analysis of novel Rab GTPases identified in the proteome of purified Legionella-containing vacuoles from macrophages","volume":"16","author":"Hoffmann","year":"2014","journal-title":"Cell Microbiol"},{"key":"B25","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1146\/annurev-micro-102215-095557","article-title":"Autophagy evasion and endoplasmic reticulum subversion: the Yin and Yang of Legionella intracellular infection","volume":"70","author":"Sherwood","year":"2016","journal-title":"Annu Rev Microbiol"},{"key":"B26","doi-asserted-by":"publisher","first-page":"e1003598","DOI":"10.1371\/journal.ppat.1003598","article-title":"Activation of Ran GTPase by a Legionella effector promotes microtubule polymerization, pathogen vacuole motility and infection","volume":"9","author":"Rothmeier","year":"2013","journal-title":"PLoS Pathog"},{"key":"B27","doi-asserted-by":"publisher","first-page":"622","DOI":"10.1074\/mcp.M116.063453","article-title":"Comparative proteomics of purified pathogen vacuoles correlates intracellular replication of Legionella pneumophila with the small GTPase Ras-related protein 1 (Rap1)","volume":"16","author":"Schm\u00f6lders","year":"2017","journal-title":"Mol Cell Proteomics"},{"key":"B28","doi-asserted-by":"publisher","first-page":"1817","DOI":"10.15252\/embr.201743903","article-title":"ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila","volume":"18","author":"Steiner","year":"2017","journal-title":"EMBO Rep"},{"key":"B29","doi-asserted-by":"publisher","first-page":"302","DOI":"10.1016\/j.chom.2017.07.020","article-title":"Legionella pneumophila modulates mitochondrial dynamics to trigger metabolic repurposing of infected macrophages","volume":"22","author":"Escoll","year":"2017","journal-title":"Cell Host Microbe."},{"key":"B30","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1038\/ng.3481","article-title":"Genomic analysis of 38 Legionella species identifies large and diverse effector repertoires","volume":"48","author":"Burstein","year":"2016","journal-title":"Nat Genet"},{"key":"B31","doi-asserted-by":"publisher","first-page":"2265","DOI":"10.1073\/pnas.1808016116","article-title":"More than 18,000 effectors in the Legionella genus genome provide multiple, independent combinations for replication in human cells","volume":"116","author":"Gomez-Valero","year":"2019","journal-title":"Proc Natl Acad Sci USA"},{"key":"B32","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1146\/annurev-cellbio-100109-104034","article-title":"Modulation of host cell function by Legionella pneumophila type IV effectors","volume":"26","author":"Hubber","year":"2010","journal-title":"Annu Rev Cell Dev Biol"},{"key":"B33","doi-asserted-by":"publisher","first-page":"1187","DOI":"10.1111\/j.1600-0854.2012.01344.x","article-title":"Secretive bacterial pathogens and the secretory pathway","volume":"13","author":"Hilbi","year":"2012","journal-title":"Traffic"},{"key":"B34","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/j.chom.2013.08.010","article-title":"A Rab-centric perspective of bacterial pathogen-occupied vacuoles","volume":"14","author":"Sherwood","year":"2013","journal-title":"Cell Host Microbe"},{"key":"B35","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1007\/82_2013_341","article-title":"Phosphoinositide lipids and the Legionella pathogen vacuole","volume":"376","author":"Haneburger","year":"2013","journal-title":"Curr Top Microbiol Immunol"},{"key":"B36","doi-asserted-by":"publisher","first-page":"935","DOI":"10.1111\/cmi.12450","article-title":"Formation of a pathogen vacuole according to Legionella pneumophila: how to kill one bird with many stones","volume":"17","author":"Finsel","year":"2015","journal-title":"Cell Microbiol"},{"key":"B37","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1038\/nrmicro.2017.67","article-title":"Legionella and Coxiella effectors: strength in diversity and activity","volume":"15","author":"Qiu","year":"2017","journal-title":"Nat Rev Microbiol"},{"key":"B38","doi-asserted-by":"publisher","first-page":"971","DOI":"10.1038\/ncb1463","article-title":"The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor","volume":"8","author":"Murata","year":"2006","journal-title":"Nat Cell Biol"},{"key":"B39","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1016\/j.devcel.2006.05.013","article-title":"Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila","volume":"11","author":"Machner","year":"2006","journal-title":"Dev Cell"},{"key":"B40","doi-asserted-by":"publisher","first-page":"598","DOI":"10.1038\/embor.2010.97","article-title":"High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA","volume":"11","author":"Schoebel","year":"2010","journal-title":"EMBO Rep"},{"key":"B41","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1016\/j.chom.2011.08.002","article-title":"Covalent coercion by Legionella pneumophila","volume":"10","author":"Itzen","year":"2011","journal-title":"Cell Host Microbe"},{"key":"B42","doi-asserted-by":"publisher","first-page":"977","DOI":"10.1111\/cmi.12258","article-title":"Icm\/Dot-dependent inhibition of phagocyte migration by Legionella is antagonized by a translocated Ran GTPase activator","volume":"16","author":"Simon","year":"2014","journal-title":"Cell Microbiol"},{"key":"B43","doi-asserted-by":"publisher","first-page":"1543","DOI":"10.1038\/s41467-017-01512-5","article-title":"Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5","volume":"8","author":"B\u00e4rlocher","year":"2017","journal-title":"Nat Commun."},{"key":"B44","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1016\/j.chom.2013.06.001","article-title":"The Legionella effector RidL inhibits retrograde trafficking to promote intracellular replication","volume":"14","author":"Finsel","year":"2013","journal-title":"Cell Host Microbe"},{"key":"B45","doi-asserted-by":"publisher","first-page":"E11151","DOI":"10.1073\/pnas.1715361115","article-title":"Molecular mechanism for the subversion of the retromer coat by the Legionella effector RidL","volume":"114","author":"Romano-Moreno","year":"2017","journal-title":"Proc Natl Acad Sci USA"},{"key":"B46","doi-asserted-by":"publisher","first-page":"E1446","DOI":"10.1073\/pnas.1717383115","article-title":"Mechanism of inhibition of retromer transport by the bacterial effector RidL","volume":"115","author":"Yao","year":"2018","journal-title":"Proc Natl Acad Sci USA"},{"key":"B47","doi-asserted-by":"publisher","first-page":"e1000822","DOI":"10.1371\/journal.ppat.1000822","article-title":"Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector","volume":"6","author":"Xu","year":"2010","journal-title":"PLoS Pathog"},{"key":"B48","doi-asserted-by":"publisher","first-page":"1072","DOI":"10.1126\/science.1227026","article-title":"The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation","volume":"338","author":"Choy","year":"2012","journal-title":"Science"},{"key":"B49","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1016\/j.devcel.2015.08.010","article-title":"The Legionella anti-autophagy effector RavZ targets the autophagosome via PI3P- and curvature-sensing motifs","volume":"34","author":"Horenkamp","year":"2015","journal-title":"Dev Cell"},{"key":"B50","doi-asserted-by":"publisher","first-page":"e23905","DOI":"10.7554\/eLife.23905","article-title":"Elucidation of the anti-autophagy mechanism of the Legionella effector RavZ using semisynthetic LC3 proteins","volume":"6","author":"Yang","year":"2017","journal-title":"Elife"},{"key":"B51","doi-asserted-by":"publisher","first-page":"e46","DOI":"10.1371\/journal.ppat.0020046","article-title":"Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole","volume":"2","author":"Weber","year":"2006","journal-title":"PLoS Pathog"},{"key":"B52","doi-asserted-by":"publisher","first-page":"1341","DOI":"10.1111\/j.1365-2958.2009.06608.x","article-title":"Pathogen trafficking pathways and host phosphoinositide metabolism","volume":"71","author":"Weber","year":"2009","journal-title":"Mol Microbiol"},{"key":"B53","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.1152\/physrev.00028.2012","article-title":"Phosphoinositides: tiny lipids with giant impact on cell regulation","volume":"93","author":"Balla","year":"2013","journal-title":"Physiol Rev"},{"key":"B54","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1038\/nature05185","article-title":"Phosphoinositides in cell regulation and membrane dynamics","volume":"443","author":"Di Paolo","year":"2006","journal-title":"Nature"},{"key":"B55","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1038\/nrm2334","article-title":"Inositol derivatives: evolution and functions","volume":"9","author":"Michell","year":"2008","journal-title":"Nat Rev Mol Cell Biol"},{"key":"B56","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1016\/S0898-6568(01)00158-9","article-title":"Phosphoinositides: key players in cell signalling, in time and space","volume":"13","author":"Payrastre","year":"2001","journal-title":"Cell Signal"},{"key":"B57","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1038\/ncb0604-487","article-title":"PI-loting membrane traffic","volume":"6","author":"De Matteis","year":"2004","journal-title":"Nat Cell Biol"},{"key":"B58","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1016\/j.plipres.2009.06.001","article-title":"Mammalian phosphoinositide kinases and phosphatases","volume":"48","author":"Sasaki","year":"2009","journal-title":"Prog Lipid Res"},{"key":"B59","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1038\/nrm2328","article-title":"Membrane recognition by phospholipid-binding domains","volume":"9","author":"Lemmon","year":"2008","journal-title":"Nat Rev Mol Cell Biol"},{"key":"B60","doi-asserted-by":"publisher","first-page":"597","DOI":"10.1038\/nature04397","article-title":"Organelle identity and the signposts for membrane traffic","volume":"438","author":"Behnia","year":"2005","journal-title":"Nature"},{"key":"B61","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1146\/annurev-cellbio-111315-125349","article-title":"Phosphoinositides in control of membrane dynamics","volume":"32","author":"Schink","year":"2016","journal-title":"Annu Rev Cell Dev Biol"},{"key":"B62","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1152\/physrev.00036.2009","article-title":"Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides","volume":"90","author":"Saarikangas","year":"2010","journal-title":"Physiol Rev"},{"key":"B63","doi-asserted-by":"publisher","first-page":"4636","DOI":"10.1073\/pnas.1423456112","article-title":"Phosphatidylinositol 4-phosphate and phosphatidylinositol 3-phosphate regulate phagolysosome biogenesis","volume":"112","author":"Jeschke","year":"2015","journal-title":"Proc Natl Acad Sci USA"},{"key":"B64","doi-asserted-by":"publisher","first-page":"4039","DOI":"10.1242\/jcs.072124","article-title":"Phosphoinositides differentially regulate bacterial uptake and Nramp1-induced resistance to Legionella infection in Dictyostelium","volume":"123","author":"Peracino","year":"2010","journal-title":"J Cell Sci"},{"key":"B65","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1007\/978-1-4939-1261-2_9","article-title":"Live cell imaging of phosphoinositide dynamics during Legionella infection","volume":"1197","author":"Weber","year":"2014","journal-title":"Methods Mol Biol"},{"key":"B66","doi-asserted-by":"publisher","first-page":"5157","DOI":"10.1128\/IAI.69.8.5157-5161.2001","article-title":"Phagocytosis of wild-type Legionella pneumophila occurs through a wortmannin-insensitive pathway","volume":"69","author":"Khelef","year":"2001","journal-title":"Infect Immun"},{"key":"B67","doi-asserted-by":"publisher","first-page":"1460","DOI":"10.1248\/bpb.b11-00011","article-title":"Phagocytic entry of Legionella pneumophila into macrophages through phosphatidylinositol 3,4,5-trisphosphate-independent pathway","volume":"35","author":"Harada","year":"2012","journal-title":"Biol Pharm Bull"},{"key":"B68","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1046\/j.1365-2958.2001.02645.x","article-title":"Icm\/Dot-dependent upregulation of phagocytosis by Legionella pneumophila","volume":"42","author":"Hilbi","year":"2001","journal-title":"Mol Microbiol"},{"key":"B69","doi-asserted-by":"publisher","first-page":"1081","DOI":"10.1084\/jem.194.8.1081","article-title":"Legionella pneumophila is internalized by a macropinocytotic uptake pathway controlled by the Dot\/Icm system and the mouse lgn1 locus","volume":"194","author":"Watarai","year":"2001","journal-title":"J Exp Med"},{"key":"B70","doi-asserted-by":"publisher","first-page":"e1007551","DOI":"10.1371\/journal.ppat.1007551","article-title":"PIKfyve\/Fab1 is required for efficient V-ATPase and hydrolase delivery to phagosomes, phagosomal killing, and restriction of Legionella infection","volume":"15","author":"Buckley","year":"2019","journal-title":"PLoS Pathog"},{"key":"B71","doi-asserted-by":"publisher","first-page":"e00839","DOI":"10.1128\/mBio.00839-13","article-title":"Live-cell imaging of phosphoinositide dynamics and membrane architecture during Legionella infection","volume":"5","author":"Weber","year":"2014","journal-title":"MBio"},{"key":"B72","doi-asserted-by":"publisher","first-page":"e02420","DOI":"10.1128\/mBio.02420-18","article-title":"Legionella-containing vacuoles capture PtdIns(4)P-rich vesicles derived from the Golgi apparatus","volume":"9","author":"Weber","year":"2018","journal-title":"MBio"},{"key":"B73","doi-asserted-by":"publisher","first-page":"91","DOI":"10.3389\/fmicb.2011.00091","article-title":"Anchors for effectors: subversion of phosphoinositide lipids by Legionella","volume":"2","author":"Hilbi","year":"2011","journal-title":"Front Microbiol"},{"key":"B74","doi-asserted-by":"publisher","first-page":"397","DOI":"10.1016\/j.str.2013.12.018","article-title":"Structural basis for PI(4)P-specific membrane recruitment of the Legionella pneumophila effector DrrA\/SidM","volume":"22","author":"Del Campo","year":"2014","journal-title":"Structure"},{"key":"B75","doi-asserted-by":"publisher","first-page":"4021","DOI":"10.1128\/IAI.01685-14","article-title":"The Legionella longbeachae Icm\/Dot substrate SidC selectively binds phosphatidylinositol 4-phosphate with nanomolar affinity and promotes pathogen vacuole-endoplasmic reticulum interactions","volume":"82","author":"Dolinsky","year":"2014","journal-title":"Infect Immun"},{"key":"B76","doi-asserted-by":"publisher","first-page":"1259","DOI":"10.1042\/BCJ20170015","article-title":"Characterization of the activation of small GTPases by their GEFs on membranes using artificial membrane tethering","volume":"474","author":"Peurois","year":"2017","journal-title":"Biochem J"},{"key":"B77","doi-asserted-by":"publisher","first-page":"e1003012","DOI":"10.1371\/journal.ppat.1003012","article-title":"The capping domain in RalF regulates effector functions","volume":"8","author":"Alix","year":"2012","journal-title":"PLoS Pathog"},{"key":"B78","doi-asserted-by":"publisher","first-page":"e1003747","DOI":"10.1371\/journal.ppat.1003747","article-title":"A novel membrane sensor controls the localization and ArfGEF activity of bacterial RalF","volume":"9","author":"Folly-Klan","year":"2013","journal-title":"PLoS Pathog"},{"key":"B79","doi-asserted-by":"publisher","first-page":"E5208","DOI":"10.1073\/pnas.1511389112","article-title":"MavN is a Legionella pneumophila vacuole-associated protein required for efficient iron acquisition during intracellular growth","volume":"112","author":"Isaac","year":"2015","journal-title":"Proc Natl Acad Sci USA"},{"key":"B80","doi-asserted-by":"publisher","first-page":"17775","DOI":"10.1073\/pnas.1902806116","article-title":"The iron-regulated vacuolar Legionella pneumophila MavN protein is a transition-metal transporter","volume":"116","author":"Christenson","year":"2019","journal-title":"Proc Natl Acad Sci USA"},{"key":"B81","doi-asserted-by":"publisher","first-page":"34686","DOI":"10.1074\/jbc.M110.170746","article-title":"Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins","volume":"285","author":"Ivanov","year":"2010","journal-title":"J Biol Chem"},{"key":"B82","doi-asserted-by":"publisher","first-page":"1713","DOI":"10.1084\/jem.20100771","article-title":"Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila","volume":"207","author":"Price","year":"2010","journal-title":"J Exp Med"},{"key":"B83","doi-asserted-by":"publisher","first-page":"3989","DOI":"10.1128\/IAI.00785-15","article-title":"Legionella pneumophila effector LpdA is a palmitoylated phospholipase D virulence factor","volume":"83","author":"Schroeder","year":"2015","journal-title":"Infect Immun"},{"key":"B84","doi-asserted-by":"publisher","first-page":"4846","DOI":"10.1074\/jbc.M807505200","article-title":"Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila","volume":"284","author":"Brombacher","year":"2009","journal-title":"J Biol Chem"},{"key":"B85","doi-asserted-by":"publisher","first-page":"2862","DOI":"10.1074\/jbc.RA118.005952","article-title":"The Legionella effector LtpM is a new type of phosphoinositide-activated glucosyltransferase","volume":"294","author":"Levanova","year":"2019","journal-title":"J Biol Chem"},{"key":"B86","doi-asserted-by":"publisher","first-page":"1469","DOI":"10.1038\/emboj.2013.82","article-title":"Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain","volume":"32","author":"Campanacci","year":"2013","journal-title":"EMBO J"},{"key":"B87","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1038\/nature10335","article-title":"Modulation of Rab GTPase function by a protein phosphocholine transferase","volume":"477","author":"Mukherjee","year":"2011","journal-title":"Nature"},{"key":"B88","doi-asserted-by":"publisher","first-page":"21212","DOI":"10.1073\/pnas.1114023109","article-title":"Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination","volume":"108","author":"Tan","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"B89","doi-asserted-by":"publisher","first-page":"1651","DOI":"10.1126\/science.1158160","article-title":"Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors","volume":"320","author":"Pan","year":"2008","journal-title":"Science"},{"key":"B90","doi-asserted-by":"publisher","first-page":"5621","DOI":"10.1073\/pnas.1121161109","article-title":"Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor","volume":"109","author":"Oesterlin","year":"2012","journal-title":"Proc Natl Acad Sci USA"},{"key":"B91","doi-asserted-by":"publisher","first-page":"4375","DOI":"10.1021\/acs.biochem.6b00524","article-title":"Unraveling the phosphocholination mechanism of the Legionella pneumophila enzyme AnkX","volume":"55","author":"Gavriljuk","year":"2016","journal-title":"Biochemistry"},{"key":"B92","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1038\/nature06336","article-title":"Legionella pneumophila proteins that regulate Rab1 membrane cycling","volume":"450","author":"Ingmundson","year":"2007","journal-title":"Nature"},{"key":"B93","doi-asserted-by":"publisher","first-page":"e01035","DOI":"10.1128\/mBio.01035-13","article-title":"AMPylation is critical for Rab1 localization to vacuoles containing Legionella pneumophila","volume":"5","author":"Hardiman","year":"2014","journal-title":"MBio"},{"key":"B94","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1038\/embor.2012.211","article-title":"Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB","volume":"14","author":"Gazdag","year":"2013","journal-title":"EMBO Rep"},{"key":"B95","doi-asserted-by":"publisher","first-page":"e00153","DOI":"10.1128\/IAI.00153-19","article-title":"Study of Legionella effector domains revealed novel and prevalent phosphatidylinositol 3-phosphate binding domains","volume":"87","author":"Nachmias","year":"2019","journal-title":"Infect Immun"},{"key":"B96","doi-asserted-by":"publisher","first-page":"16236","DOI":"10.1038\/nmicrobiol.2016.236","article-title":"Modulation of membrane phosphoinositide dynamics by the phosphatidylinositide 4-kinase activity of the Legionella LepB effector","volume":"2","author":"Dong","year":"2016","journal-title":"Nat Microbiol"},{"key":"B97","doi-asserted-by":"publisher","first-page":"1358","DOI":"10.1126\/science.1094226","article-title":"Legionella effectors that promote nonlytic release from protozoa","volume":"303","author":"Chen","year":"2004","journal-title":"Science"},{"key":"B98","doi-asserted-by":"publisher","first-page":"24000","DOI":"10.1074\/jbc.M113.470625","article-title":"The Legionella pneumophila GTPase activating protein LepB accelerates Rab1 deactivation by a non-canonical hydrolytic mechanism","volume":"288","author":"Mishra","year":"2013","journal-title":"J Biol Chem"},{"key":"B99","doi-asserted-by":"publisher","first-page":"e1002988","DOI":"10.1371\/journal.ppat.1002988","article-title":"Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesis","volume":"8","author":"Viner","year":"2012","journal-title":"PLoS Pathog"},{"key":"B100","doi-asserted-by":"publisher","first-page":"e17638","DOI":"10.1371\/journal.pone.0017638","article-title":"Comprehensive identification of protein substrates of the Dot\/Icm type IV transporter of Legionella pneumophila","volume":"6","author":"Zhu","year":"2011","journal-title":"PLoS ONE"},{"key":"B101","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1016\/j.chom.2018.07.003","article-title":"A phosphatidylinositol 3-kinase effector alters phagosomal maturation to promote intracellular growth of Francisella","volume":"24","author":"Ledvina","year":"2018","journal-title":"Cell Host Microbe"},{"key":"B102","doi-asserted-by":"publisher","first-page":"e1004222","DOI":"10.1371\/journal.ppat.1004222","article-title":"The machinery at endoplasmic reticulum-plasma membrane contact sites contributes to spatial regulation of multiple Legionella effector proteins","volume":"10","author":"Hubber","year":"2014","journal-title":"PLoS Pathog"},{"key":"B103","doi-asserted-by":"publisher","first-page":"1389","DOI":"10.1128\/JB.06306-11","article-title":"Legionella pneumophila LidA affects nucleotide binding and activity of the host GTPase Rab1","volume":"194","author":"Neunuebel","year":"2012","journal-title":"J Bacteriol"},{"key":"B104","doi-asserted-by":"publisher","first-page":"e1002528","DOI":"10.1371\/journal.ppat.1002528","article-title":"Structural insights into a unique Legionella pneumophila effector LidA recognizing both GDP and GTP bound Rab1 in their active state","volume":"8","author":"Cheng","year":"2012","journal-title":"PLoS Pathog"},{"key":"B105","doi-asserted-by":"publisher","first-page":"17945","DOI":"10.1073\/pnas.1113133108","article-title":"Protein LidA from Legionella is a Rab GTPase supereffector","volume":"108","author":"Schoebel","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"B106","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1046\/j.1365-2958.2003.03400.x","article-title":"The Legionella pneumophila LidA protein: a translocated substrate of the Dot\/Icm system associated with maintenance of bacterial integrity","volume":"48","author":"Conover","year":"2003","journal-title":"Mol Microbiol"},{"key":"B107","doi-asserted-by":"publisher","first-page":"4370","DOI":"10.1128\/IAI.73.7.4370-4380.2005","article-title":"LidA, a translocated substrate of the Legionella pneumophila type IV secretion system, interferes with the early secretory pathway","volume":"73","author":"Derre","year":"2005","journal-title":"Infect Immun"},{"key":"B108","doi-asserted-by":"publisher","first-page":"34175","DOI":"10.1074\/jbc.M114.592568","article-title":"A type IV translocated Legionella cysteine phytase counteracts intracellular growth restriction by phytate","volume":"289","author":"Weber","year":"2014","journal-title":"J Biol Chem"},{"key":"B109","doi-asserted-by":"publisher","first-page":"4261","DOI":"10.1128\/IAI.01054-13","article-title":"LtpD is a novel Legionella pneumophila effector that binds phosphatidylinositol 3-phosphate and inositol monophosphatase IMPA1","volume":"81","author":"Harding","year":"2013","journal-title":"Infect Immun"},{"key":"B110","doi-asserted-by":"publisher","first-page":"230","DOI":"10.1111\/j.1462-5822.2008.01249.x","article-title":"Large-scale identification of Legionella pneumophila Dot\/Icm substrates that modulate host cell vesicle trafficking pathways","volume":"11","author":"Heidtman","year":"2009","journal-title":"Cell Microbiol"},{"key":"B111","doi-asserted-by":"publisher","first-page":"11080","DOI":"10.1074\/jbc.M112.426049","article-title":"The Legionella pneumophila Dot\/Icm-secreted effector PlcC\/CegC1 together with PlcA and PlcB promotes virulence and belongs to a novel zinc metallophospholipase C family present in bacteria and fungi","volume":"288","author":"Aurass","year":"2013","journal-title":"J Biol Chem"},{"key":"B112","doi-asserted-by":"publisher","first-page":"1392","DOI":"10.1074\/jbc.M410820200","article-title":"The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site","volume":"280","author":"Amor","year":"2005","journal-title":"J Biol Chem"},{"key":"B113","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1073\/pnas.0406239101","article-title":"A C-terminal translocation signal required for Dot\/Icm-dependent delivery of the Legionella RalF protein to host cells","volume":"102","author":"Nagai","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"B114","doi-asserted-by":"publisher","first-page":"6405","DOI":"10.1074\/jbc.RA118.007086","article-title":"The Legionella effector RavD binds phosphatidylinositol-3-phosphate and helps suppress endolysosomal maturation of the Legionella-containing vacuole","volume":"294","author":"Pike","year":"2019","journal-title":"J Biol Chem"},{"key":"B115","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1073\/pnas.0304916101","article-title":"Multiple substrates of the Legionella pneumophila Dot\/Icm system identified by interbacterial protein transfer","volume":"101","author":"Luo","year":"2004","journal-title":"Proc Natl Acad Sci USA"},{"key":"B116","doi-asserted-by":"publisher","first-page":"2416","DOI":"10.1111\/j.1462-5822.2008.01219.x","article-title":"The Legionella pneumophila phosphatidylinositol 4-phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole","volume":"10","author":"Ragaz","year":"2008","journal-title":"Cell Microbiol"},{"key":"B117","doi-asserted-by":"publisher","first-page":"488","DOI":"10.1111\/tra.12158","article-title":"Legionella pneumophila subversion of host vesicular transport by SidC effector proteins","volume":"15","author":"Horenkamp","year":"2014","journal-title":"Traffic"},{"key":"B118","doi-asserted-by":"publisher","first-page":"10538","DOI":"10.1073\/pnas.1402605111","article-title":"The Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling","volume":"111","author":"Hsu","year":"2014","journal-title":"Proc Natl Acad Sci USA"},{"key":"B119","doi-asserted-by":"publisher","first-page":"e36154","DOI":"10.7554\/eLife.36154","article-title":"Insights into the ubiquitin transfer cascade catalyzed by the Legionella effector SidC","volume":"7","author":"Wasilko","year":"2018","journal-title":"Elife"},{"key":"B120","doi-asserted-by":"publisher","first-page":"852","DOI":"10.1111\/j.1462-5822.2012.01761.x","article-title":"Domain organization of Legionella effector SetA","volume":"14","author":"Jank","year":"2012","journal-title":"Cell Microbiol"},{"key":"B121","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1016\/j.jsb.2014.02.003","article-title":"The structure of the N-terminal domain of the Legionella protein SidC","volume":"186","author":"Gazdag","year":"2014","journal-title":"J Struct Biol"},{"key":"B122","doi-asserted-by":"publisher","first-page":"5121","DOI":"10.1073\/pnas.0611030104","article-title":"Legionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein family","volume":"104","author":"Banga","year":"2007","journal-title":"Proc Natl Acad Sci USA"},{"key":"B123","doi-asserted-by":"publisher","first-page":"13567","DOI":"10.1073\/pnas.1207903109","article-title":"Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase","volume":"109","author":"Hsu","year":"2012","journal-title":"Proc Natl Acad Sci USA"},{"key":"B124","doi-asserted-by":"publisher","first-page":"974","DOI":"10.1126\/science.1149121","article-title":"A bifunctional bacterial protein links GDI displacement to Rab1 activation","volume":"318","author":"Machner","year":"2007","journal-title":"Science"},{"key":"B125","doi-asserted-by":"publisher","first-page":"1060","DOI":"10.1016\/j.molcel.2009.11.014","article-title":"RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity","volume":"36","author":"Schoebel","year":"2009","journal-title":"Mol Cell"},{"key":"B126","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1038\/emboj.2009.347","article-title":"Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM\/DrrA","volume":"29","author":"Suh","year":"2010","journal-title":"EMBO J"},{"key":"B127","doi-asserted-by":"publisher","first-page":"4699","DOI":"10.1073\/pnas.0914231107","article-title":"Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM\/DrrA","volume":"107","author":"Zhu","year":"2010","journal-title":"Proc Natl Acad Sci USA"},{"key":"B128","doi-asserted-by":"publisher","first-page":"946","DOI":"10.1126\/science.1192276","article-title":"The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b","volume":"329","author":"Muller","year":"2010","journal-title":"Science"},{"key":"B129","doi-asserted-by":"publisher","first-page":"24518","DOI":"10.1074\/jbc.M113.474239","article-title":"Identification and structural characterization of a Legionella phosphoinositide phosphatase","volume":"288","author":"Toulabi","year":"2013","journal-title":"J Biol Chem"},{"key":"B130","doi-asserted-by":"publisher","first-page":"4866","DOI":"10.1073\/pnas.0501315102","article-title":"Pathogen effector protein screening in yeast identifies Legionella factors that interfere with membrane trafficking","volume":"102","author":"Shohdy","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"B131","doi-asserted-by":"publisher","first-page":"3597","DOI":"10.1128\/IAI.02060-05","article-title":"Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells","volume":"74","author":"VanRheenen","year":"2006","journal-title":"Infect Immun"},{"key":"B132","doi-asserted-by":"publisher","first-page":"1783","DOI":"10.1111\/cmi.12157","article-title":"Induction of caspase 3 activation by multiple Legionella pneumophila Dot\/Icm substrates","volume":"15","author":"Zhu","year":"2013","journal-title":"Cell Microbiol"},{"key":"B133","doi-asserted-by":"publisher","first-page":"4560","DOI":"10.1073\/pnas.1316376111","article-title":"VipD is a Rab5-activated phospholipase A1 that protects Legionella pneumophila from endosomal fusion","volume":"111","author":"Gaspar","year":"2014","journal-title":"Proc Natl Acad Sci USA"},{"key":"B134","doi-asserted-by":"publisher","first-page":"e1003082","DOI":"10.1371\/journal.ppat.1003082","article-title":"VipD of Legionella pneumophila targets activated Rab5 and Rab22 to interfere with endosomal trafficking in macrophages","volume":"8","author":"Ku","year":"2012","journal-title":"PLoS Pathog"},{"key":"B135","doi-asserted-by":"publisher","first-page":"E3514","DOI":"10.1073\/pnas.1405391111","article-title":"Structural basis for the recruitment and activation of the Legionella phospholipase VipD by the host GTPase Rab5","volume":"111","author":"Lucas","year":"2014","journal-title":"Proc Natl Acad Sci USA"},{"key":"B136","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1007\/978-1-62703-161-5_23","article-title":"Interactions of Legionella effector proteins with host phosphoinositide lipids","volume":"954","author":"Weber","year":"2013","journal-title":"Methods Mol Biol"},{"key":"B137","doi-asserted-by":"publisher","first-page":"e1004965","DOI":"10.1371\/journal.ppat.1004965","article-title":"Structure of the Legionella virulence factor, SidC reveals a unique PI(4)P-specific binding domain essential for its targeting to the bacterial phagosome","volume":"11","author":"Luo","year":"2015","journal-title":"PLoS Pathog"},{"key":"B138","doi-asserted-by":"publisher","DOI":"10.1002\/0471143030.cb0334s46","article-title":"Isolation of Legionella-containing vacuoles by immuno-magnetic separation","author":"Urwyler","year":"2010","journal-title":"Curr Protoc Cell Biol."},{"key":"B139","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1007\/978-1-62703-161-5_18","article-title":"Pathogen vacuole purification from Legionella-infected amoeba and macrophages","volume":"954","author":"Hoffmann","year":"2013","journal-title":"Methods Mol Biol"},{"key":"B140","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1111\/j.1600-0854.2008.00851.x","article-title":"Proteome analysis of Legionella vacuoles purified by magnetic immunoseparation reveals secretory and endosomal GTPases","volume":"10","author":"Urwyler","year":"2009","journal-title":"Traffic"},{"key":"B141","doi-asserted-by":"publisher","first-page":"e1005408","DOI":"10.1371\/journal.ppat.1005408","article-title":"IFNs modify the proteome of Legionella-containing vacuoles and restrict infection via IRG1-derived itaconic acid","volume":"12","author":"Naujoks","year":"2016","journal-title":"PLoS Pathog"},{"key":"B142","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1007\/978-1-62703-302-2_24","article-title":"Immunomagnetic purification of fluorescent Legionella-containing vacuoles","volume":"983","author":"Finsel","year":"2013","journal-title":"Methods Mol Biol"},{"key":"B143","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1083\/jcb.201312072","article-title":"A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi","volume":"205","author":"Hammond","year":"2014","journal-title":"J Cell Biol"},{"key":"B144","doi-asserted-by":"publisher","first-page":"4328","DOI":"10.1242\/jcs.180364","article-title":"In vivo tracking of phosphoinositides in Drosophila photoreceptors","volume":"128","author":"Hardie","year":"2015","journal-title":"J Cell Sci"},{"key":"B145","doi-asserted-by":"publisher","first-page":"2749","DOI":"10.1016\/j.febslet.2011.08.006","article-title":"Identification and modelling of a PPM protein phosphatase fold in the Legionella pneumophila deAMPylase SidD","volume":"585","author":"Rigden","year":"2011","journal-title":"FEBS Lett"},{"key":"B146","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1038\/nature10307","article-title":"Legionella pneumophila SidD is a deAMPylase that modifies Rab1","volume":"475","author":"Tan","year":"2011","journal-title":"Nature"},{"key":"B147","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1126\/science.1207193","article-title":"De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila","volume":"333","author":"Neunuebel","year":"2011","journal-title":"Science"},{"key":"B148","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1111\/j.1600-0854.2010.01050.x","article-title":"Legionella pneumophila promotes functional interactions between plasma membrane syntaxins and Sec22b","volume":"11","author":"Arasaki","year":"2010","journal-title":"Traffic"},{"key":"B149","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1016\/j.chom.2011.11.009","article-title":"The Legionella pneumophila effector DrrA is sufficient to stimulate SNARE-dependent membrane fusion","volume":"11","author":"Arasaki","year":"2012","journal-title":"Cell Host Microbe"},{"key":"B150","doi-asserted-by":"publisher","first-page":"3048","DOI":"10.1128\/IAI.72.5.3048-3053.2004","article-title":"Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system","volume":"72","author":"Derre","year":"2004","journal-title":"Infect Immun"},{"key":"B151","doi-asserted-by":"publisher","first-page":"1201","DOI":"10.1084\/jem.20031706","article-title":"Legionella subvert the functions of rab1 and sec22b to create a replicative organelle","volume":"199","author":"Kagan","year":"2004","journal-title":"J Exp Med"},{"key":"B152","doi-asserted-by":"publisher","first-page":"2226","DOI":"10.1128\/IAI.00157-13","article-title":"Targeting of the small GTPase Rab6A by the Legionella pneumophila effector LidA","volume":"81","author":"Chen","year":"2013","journal-title":"Infect Immun"},{"key":"B153","doi-asserted-by":"publisher","first-page":"5832","DOI":"10.1074\/jbc.M115.700930","article-title":"The Rab-binding profiles of bacterial virulence factors during infection","volume":"291","author":"So","year":"2016","journal-title":"J Biol Chem"},{"key":"B154","doi-asserted-by":"publisher","first-page":"397","DOI":"10.3389\/fcimb.2017.00397","article-title":"Legionella effector AnkX disrupts host cell endocytic recycling in a phosphocholination-dependent manner","volume":"7","author":"Allgood","year":"2017","journal-title":"Front Cell Infect Microbiol"},{"key":"B155","doi-asserted-by":"publisher","first-page":"1774","DOI":"10.1038\/emboj.2012.16","article-title":"Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins","volume":"31","author":"Goody","year":"2012","journal-title":"EMBO J"},{"key":"B156","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1111\/j.1462-5822.2008.01266.x","article-title":"The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE","volume":"11","author":"Weber","year":"2009","journal-title":"Cell Microbiol"},{"key":"B157","doi-asserted-by":"publisher","first-page":"1683","DOI":"10.1128\/IAI.74.3.1683-1691.2006","article-title":"Identification of Legionella pneumophila-specific genes by genomic subtractive hybridization with Legionella micdadei and identification of lpnE, a gene required for efficient host cell entry","volume":"74","author":"Newton","year":"2006","journal-title":"Infect Immun"},{"key":"B158","doi-asserted-by":"publisher","first-page":"5575","DOI":"10.1128\/IAI.00443-07","article-title":"Sel1 repeat protein LpnE is a Legionella pneumophila virulence determinant that influences vacuolar trafficking","volume":"75","author":"Newton","year":"2007","journal-title":"Infect Immun"},{"key":"B159","doi-asserted-by":"publisher","first-page":"e1000117","DOI":"10.1371\/journal.ppat.1000117","article-title":"Legionella eukaryotic-like type IV substrates interfere with organelle trafficking","volume":"4","author":"de Felipe","year":"2008","journal-title":"PLoS Pathog"},{"key":"B160","doi-asserted-by":"publisher","first-page":"532","DOI":"10.1038\/s41467-017-00700-7","article-title":"A systematic exploration of the interactions between bacterial effector proteins and host cell membranes","volume":"8","author":"Weigele","year":"2017","journal-title":"Nat Commun"},{"key":"B161","doi-asserted-by":"publisher","first-page":"710","DOI":"10.1111\/febs.14710","article-title":"The structure of Legionella effector protein LpnE provides insights into its interaction with Oculocerebrorenal syndrome of Lowe (OCRL) protein","volume":"286","author":"Voth","year":"2019","journal-title":"FEBS J"},{"key":"B162","doi-asserted-by":"publisher","first-page":"618","DOI":"10.1111\/j.1600-0854.2007.00546.x","article-title":"Regulation of phagocytosis in Dictyostelium by the inositol 5-phosphatase OCRL homolog Dd5P4","volume":"8","author":"Loovers","year":"2007","journal-title":"Traffic"},{"key":"B163","doi-asserted-by":"publisher","first-page":"4853","DOI":"10.1073\/pnas.92.11.4853","article-title":"The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase","volume":"92","author":"Zhang","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"B164","doi-asserted-by":"publisher","first-page":"e00158","DOI":"10.1128\/AEM.00158-18","article-title":"Quantitative imaging flow cytometry of Legionella-infected Dictyostelium amoebae reveals the impact of retrograde trafficking on pathogen vacuole composition","volume":"84","author":"Welin","year":"2018","journal-title":"Appl Environ Microbiol"},{"key":"B165","doi-asserted-by":"publisher","first-page":"280","DOI":"10.1038\/12993","article-title":"ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex","volume":"1","author":"Godi","year":"1999","journal-title":"Nat Cell Biol"},{"key":"B166","doi-asserted-by":"publisher","first-page":"3750","DOI":"10.1038\/sj.emboj.7601274","article-title":"Membrane targeting and activation of the Lowe syndrome protein OCRL1 by rab GTPases","volume":"25","author":"Hyvola","year":"2006","journal-title":"EMBO J"},{"key":"B167","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/j.ymgme.2006.04.005","article-title":"The effect of missense mutations in the RhoGAP-homology domain on ocrl1 function","volume":"89","author":"Lichter-Konecki","year":"2006","journal-title":"Mol Genet Metab"}],"container-title":["Frontiers in Immunology"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/article\/10.3389\/fimmu.2020.00025\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,1,30]],"date-time":"2020-01-30T04:34:15Z","timestamp":1580358855000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/article\/10.3389\/fimmu.2020.00025\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,1,30]]},"references-count":167,"alternative-id":["10.3389\/fimmu.2020.00025"],"URL":"https:\/\/doi.org\/10.3389\/fimmu.2020.00025","relation":{},"ISSN":["1664-3224"],"issn-type":[{"value":"1664-3224","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,1,30]]},"article-number":"25"}}