{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,28]],"date-time":"2026-03-28T07:43:26Z","timestamp":1774683806722,"version":"3.50.1"},"reference-count":66,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2010,3,15]]},"abstract":"<jats:p>Legionnaires' disease is caused by a lethal colonization of alveolar macrophages with the Gram-negative bacterium Legionella pneumophila. LpGT (L. pneumophila glucosyltransferase; also known as Lgt1) has recently been identified as a virulence factor, shutting down protein synthesis in the human cell by specific glucosylation of EF1A (elongation factor 1A), using an unknown mode of substrate recognition and a retaining mechanism for glycosyl transfer. We have determined the crystal structure of LpGT in complex with substrates, revealing a GT-A fold with two unusual protruding domains. Through structure-guided mutagenesis of LpGT, several residues essential for binding of the UDP-glucose-donor and EF1A-acceptor substrates were identified, which also affected L. pneumophila virulence as demonstrated by microinjection studies. Together, these results suggested that a positively charged EF1A loop binds to a negatively charged conserved groove on the LpGT structure, and that two asparagine residues are essential for catalysis. Furthermore, we showed that two further L. pneumophila glycosyltransferases possessed the conserved UDP-glucose-binding sites and EF1A-binding grooves, and are, like LpGT, translocated into the macrophage through the Icm\/Dot (intracellular multiplication\/defect in organelle trafficking) system.<\/jats:p>","DOI":"10.1042\/bj20091351","type":"journal-article","created":{"date-parts":[[2009,12,23]],"date-time":"2009-12-23T16:16:28Z","timestamp":1261584988000},"page":"281-292","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":31,"title":["Molecular mechanism of elongation factor 1A inhibition by a <i>Legionella pneumophila<\/i> glycosyltransferase"],"prefix":"10.1042","volume":"426","author":[{"given":"Ramon","family":"Hurtado-Guerrero","sequence":"first","affiliation":[{"name":"Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tal","family":"Zusman","sequence":"additional","affiliation":[{"name":"Molecular Microbiology and Biotechnology, Life Sciences, Tel Aviv University, Tel Aviv, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shalini","family":"Pathak","sequence":"additional","affiliation":[{"name":"Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adel\u00a0F.\u00a0M.","family":"Ibrahim","sequence":"additional","affiliation":[{"name":"DNA Manipulation Team, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sharon","family":"Shepherd","sequence":"additional","affiliation":[{"name":"Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alan","family":"Prescott","sequence":"additional","affiliation":[{"name":"Division of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gil","family":"Segal","sequence":"additional","affiliation":[{"name":"Molecular Microbiology and Biotechnology, Life Sciences, Tel Aviv University, Tel Aviv, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daan\u00a0M.\u00a0F.","family":"van\u00a0Aalten","sequence":"additional","affiliation":[{"name":"Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2010,2,24]]},"reference":[{"key":"2021112214282714200_B1","first-page":"3","article-title":"Carbohydrate-active enzymes: an integrated database approach","volume-title":"Recent Advances in Carbohydrate Bioengineering","author":"Coutinho","year":"1999"},{"key":"2021112214282714200_B2","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1038\/375500a0","article-title":"Glucosylation of Rho proteins by Clostridium difficile toxin B","volume":"375","author":"Just","year":"1995","journal-title":"Nature"},{"key":"2021112214282714200_B3","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.bbagen.2004.03.014","article-title":"Large clostridial cytotoxins: cellular biology of Rho\/Ras-glucosylating toxins","volume":"1673","author":"Schirmer","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112214282714200_B4","article-title":"Clostridium difficile","author":"Lyerly","year":"1995"},{"key":"2021112214282714200_B5","doi-asserted-by":"crossref","first-page":"15R","DOI":"10.1093\/glycob\/cwm004","article-title":"Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function","volume":"17","author":"Jank","year":"2007","journal-title":"Glycobiology"},{"key":"2021112214282714200_B6","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1128\/IAI.71.1.181-186.2003","article-title":"Purification and characterization of a UDP-glucosyltransferase produced by Legionella pneumophila","volume":"71","author":"Belyi","year":"2003","journal-title":"Infect. Immun."},{"key":"2021112214282714200_B7","doi-asserted-by":"crossref","first-page":"16953","DOI":"10.1073\/pnas.0601562103","article-title":"Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A","volume":"103","author":"Belyi","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112214282714200_B8","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1007\/s00018-006-6391-1","article-title":"Legionella pneumophila: a human pathogen that co-evolved with fresh water protozoa","volume":"64","author":"Albert-Weissenberger","year":"2007","journal-title":"Cell. Mol. Life Sci."},{"key":"2021112214282714200_B9","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1099\/jmm.0.47556-0","article-title":"Legionnaires' disease in immunocompromised patients: a case report of Legionella longbeachae pneumonia and review of the literature","volume":"57","author":"Kumpers","year":"2008","journal-title":"J. Med. Microbiol."},{"key":"2021112214282714200_B10","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.tim.2007.06.006","article-title":"Effector proteins translocated by Legionella pneumophila: strength in numbers","volume":"15","author":"Ninio","year":"2007","journal-title":"Trends Microbiol."},{"key":"2021112214282714200_B11","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1111\/j.1462-5822.2008.01145.x","article-title":"Host cell processes that influence the intracellular survival of Legionella pneumophila","volume":"10","author":"Shin","year":"2008","journal-title":"Cell. Microbiol."},{"key":"2021112214282714200_B12","doi-asserted-by":"crossref","first-page":"20167","DOI":"10.1074\/jbc.M109.008441","article-title":"Region of elongation factor 1A1 involved in substrate recognition by Legionella pneumophila glucosyltransferase Lgt1: identification of Lgt1 as a retaining glucosyltransferase","volume":"284","author":"Belyi","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021112214282714200_B13","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"2021112214282714200_B14","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/nmeth876","article-title":"High-throughput RNAi screening by time-lapse imaging of live human cells","volume":"3","author":"Neumann","year":"2006","journal-title":"Nat. Methods"},{"key":"2021112214282714200_B15","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1083\/jcb.96.2.424","article-title":"A microtubule-associated protein antigen unique to mitotic spindle microtubules in PtK1 cells","volume":"96","author":"Izant","year":"1983","journal-title":"J. Cell. Biol."},{"key":"2021112214282714200_B16","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1242\/jcs.102.1.103","article-title":"Stable and slow-turning-over microtubules characterize the processes of motile epithelial cells treated with scatter factor","volume":"102","author":"Prescott","year":"1992","journal-title":"J. Cell Sci."},{"key":"2021112214282714200_B17","doi-asserted-by":"crossref","first-page":"1617","DOI":"10.1016\/j.str.2006.09.005","article-title":"Lysine methylation as a routine rescue strategy for protein crystallization","volume":"14","author":"Walter","year":"2006","journal-title":"Structure"},{"key":"2021112214282714200_B18","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"2021112214282714200_B19","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 Suite: Programs for Protein Crystallography","volume":"50","author":"Collaborative Computational Project","year":"1994","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021112214282714200_B20","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.ocl.2004.04.001","article-title":"Imaging of early stages of osteonecrosis of the knee","volume":"35","author":"Pape","year":"2004","journal-title":"Orthop. Clin. North Am."},{"key":"2021112214282714200_B21","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1038\/8263","article-title":"Automated protein model building combined with iterative structure refinement","volume":"6","author":"Perrakis","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"2021112214282714200_B22","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021112214282714200_B23","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021112214282714200_B24","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1107\/S0907444904011679","article-title":"PRODRG: a tool for high-throughput crystallography of protein-ligand complexes","volume":"60","author":"Schuttelkopf","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021112214282714200_B25","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1006\/jmbi.1993.1351","article-title":"Main-chain bond lengths and bond angles in protein structures","volume":"231","author":"Laskowski","year":"1993","journal-title":"J. Mol. Biol."},{"key":"2021112214282714200_B26","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/381272a0","article-title":"Errors in protein structures","volume":"381","author":"Hooft","year":"1996","journal-title":"Nature"},{"key":"2021112214282714200_B27","doi-asserted-by":"crossref","first-page":"5361","DOI":"10.1128\/iai.61.12.5361-5373.1993","article-title":"Identification of Legionella pneumophila genes required for growth within and killing of human macrophages","volume":"61","author":"Sadosky","year":"1993","journal-title":"Infect. Immun."},{"key":"2021112214282714200_B28","doi-asserted-by":"crossref","first-page":"3714","DOI":"10.1128\/IAI.71.7.3714-3723.2003","article-title":"Functional similarities between the icm\/dot pathogenesis systems of Coxiella burnetii and Legionella pneumophila","volume":"71","author":"Zusman","year":"2003","journal-title":"Infect. Immun."},{"key":"2021112214282714200_B29","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1111\/j.1365-2958.2007.05604.x","article-title":"The response regulator PmrA is a major regulator of the icm\/dot type\u00a0IV secretion system in Legionella pneumophila and Coxiella burnetii","volume":"63","author":"Zusman","year":"2007","journal-title":"Mol. Microbiol."},{"key":"2021112214282714200_B30","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1128\/IAI.67.5.2117-2124.1999","article-title":"Legionella pneumophila utilizes the same genes to multiply within Acanthamoeba castellanii and human macrophages","volume":"67","author":"Segal","year":"1999","journal-title":"Infect. Immun."},{"key":"2021112214282714200_B31","doi-asserted-by":"crossref","first-page":"1985","DOI":"10.1128\/JB.01493-07","article-title":"The response regulator CpxR directly regulates expression of several Legionella pneumophila icm\/dot components as well as new translocated substrates","volume":"190","author":"Altman","year":"2008","journal-title":"J. Bacteriol."},{"key":"2021112214282714200_B32","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.tibs.2004.11.005","article-title":"Substrate-induced conformational changes in glycosyltransferases","volume":"30","author":"Qasba","year":"2005","journal-title":"Trends Biochem. Sci."},{"key":"2021112214282714200_B33","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/S0968-0004(00)89105-7","article-title":"Dali: a network tool for protein structure comparison","volume":"20","author":"Holm","year":"1995","journal-title":"Trends Biochem. Sci."},{"key":"2021112214282714200_B34","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/j.jmb.2005.06.071","article-title":"Structural basis for the function of Clostridium difficile toxin B","volume":"351","author":"Reinert","year":"2005","journal-title":"J. Mol. Biol."},{"key":"2021112214282714200_B35","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1016\/j.jmb.2007.12.065","article-title":"Conformational changes and reaction of clostridial glycosylating toxins","volume":"377","author":"Ziegler","year":"2008","journal-title":"J. Mol. Biol."},{"key":"2021112214282714200_B36","doi-asserted-by":"crossref","first-page":"3026","DOI":"10.1128\/JB.01798-07","article-title":"Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila","volume":"190","author":"Belyi","year":"2008","journal-title":"J. Bacteriol."},{"key":"2021112214282714200_B37","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1016\/S1097-2765(00)00122-2","article-title":"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha","volume":"6","author":"Andersen","year":"2000","journal-title":"Mol. Cell"},{"key":"2021112214282714200_B38","doi-asserted-by":"crossref","first-page":"13228","DOI":"10.1074\/jbc.275.18.13228","article-title":"Involvement of a conserved tryptophan residue in the UDP-glucose binding of large clostridial cytotoxin glycosyltransferases","volume":"275","author":"Busch","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021112214282714200_B39","doi-asserted-by":"crossref","first-page":"35222","DOI":"10.1074\/jbc.M703138200","article-title":"Clostridium difficile glucosyltransferase toxin B: essential amino acids for substrate binding","volume":"282","author":"Jank","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2021112214282714200_B40","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1006\/jmbi.2001.4757","article-title":"Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the \u03b2-1,4-galactosyltransferase-I","volume":"310","author":"Ramakrishnan","year":"2001","journal-title":"J. Mol. Biol."},{"key":"2021112214282714200_B41","doi-asserted-by":"crossref","first-page":"6380","DOI":"10.1021\/bi990270y","article-title":"Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms","volume":"38","author":"Charnock","year":"1999","journal-title":"Biochemistry"},{"key":"2021112214282714200_B42","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1038\/84168","article-title":"Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs","volume":"8","author":"Persson","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"2021112214282714200_B43","doi-asserted-by":"crossref","first-page":"19566","DOI":"10.1074\/jbc.273.31.19566","article-title":"A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins","volume":"273","author":"Busch","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021112214282714200_B44","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1093\/glycob\/9.8.815","article-title":"Role of a conserved acidic cluster in bovine \u03b2-1,4 galactosyltransferase-1 probed by mutagenesis of a bacterially expressed recombinant enzyme","volume":"9","author":"Zhang","year":"1999","journal-title":"Glycobiology"},{"key":"2021112214282714200_B45","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1146\/annurev.biochem.76.061005.092322","article-title":"Glycosyltransferases: structures, functions, and mechanisms","volume":"77","author":"Lairson","year":"2008","journal-title":"Annu. Rev. Biochem."},{"key":"2021112214282714200_B46","doi-asserted-by":"crossref","first-page":"28339","DOI":"10.1074\/jbc.M400451200","article-title":"Intermediate trapping on a mutant retaining \u03b1-galactosyltransferase identifies an unexpected aspartate residue","volume":"279","author":"Lairson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021112214282714200_B47","doi-asserted-by":"crossref","first-page":"13512","DOI":"10.1021\/bi035430r","article-title":"Roles of individual enzyme\u2013substrate interactions by \u03b1-1,3-galactosyltransferase in catalysis and specificity","volume":"42","author":"Zhang","year":"2003","journal-title":"Biochemistry"},{"key":"2021112214282714200_B48","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1016\/j.jmb.2007.04.012","article-title":"Conformational changes induced by binding UDP-2F-galactose to \u03b1-1,3 galactosyltransferase: implications for catalysis","volume":"369","author":"Jamaluddin","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2021112214282714200_B49","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1093\/emboj\/20.4.638","article-title":"Bovine \u03b1-1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases","volume":"20","author":"Gastinel","year":"2001","journal-title":"EMBO J."},{"key":"2021112214282714200_B50","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/345229a0","article-title":"Molecular genetic basis of the histo-blood group ABO system","volume":"345","author":"Yamamoto","year":"1990","journal-title":"Nature"},{"key":"2021112214282714200_B51","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1038\/nsb832","article-title":"The structural basis for specificity in human ABO(H) blood group biosynthesis","volume":"9","author":"Patenaude","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"2021112214282714200_B52","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1074\/jbc.M410245200","article-title":"Structural basis for the inactivity of human blood group O2 glycosyltransferase","volume":"280","author":"Lee","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021112214282714200_B53","doi-asserted-by":"crossref","first-page":"15307","DOI":"10.1073\/pnas.0405657101","article-title":"The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide \u03b1-N-acetylgalactosaminyltransferase-T1","volume":"101","author":"Fritz","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112214282714200_B54","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.jmb.2006.03.061","article-title":"Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide \u03b1-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)","volume":"359","author":"Kubota","year":"2006","journal-title":"J. Mol. Biol."},{"key":"2021112214282714200_B55","doi-asserted-by":"crossref","first-page":"8613","DOI":"10.1074\/jbc.M513590200","article-title":"Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide \u03b1-N-acetylgalactosaminyltransferase-2","volume":"281","author":"Fritz","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021112214282714200_B56","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1038\/nsmb950","article-title":"Structural dissection and high-throughput screening of mannosylglycerate synthase","volume":"12","author":"Flint","year":"2005","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2021112214282714200_B57","doi-asserted-by":"crossref","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. U.S.A."},{"key":"2021112214282714200_B58","doi-asserted-by":"crossref","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":"2021112214282714200_B59","doi-asserted-by":"crossref","first-page":"3948","DOI":"10.1099\/mic.0.2007\/012039-0","article-title":"The role of protein secretion systems in the virulence of the intracellular pathogen Legionella pneumophila","volume":"153","author":"De\u00a0Buck","year":"2007","journal-title":"Microbiology"},{"key":"2021112214282714200_B60","doi-asserted-by":"crossref","first-page":"7716","DOI":"10.1128\/JB.187.22.7716-7726.2005","article-title":"Evidence for acquisition of Legionella type\u00a0IV secretion substrates via interdomain horizontal gene transfer","volume":"187","author":"de\u00a0Felipe","year":"2005","journal-title":"J. Bacteriol."},{"key":"2021112214282714200_B61","doi-asserted-by":"crossref","first-page":"e188","DOI":"10.1371\/journal.ppat.0030188","article-title":"The Legionella pneumophila IcmSW complex interacts with multiple Dot\/Icm effectors to facilitate type\u00a0IV translocation","volume":"3","author":"Cambronne","year":"2007","journal-title":"PLoS Pathog."},{"key":"2021112214282714200_B62","doi-asserted-by":"crossref","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. U.S.A."},{"key":"2021112214282714200_B63","doi-asserted-by":"crossref","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":"2021112214282714200_B64","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1111\/j.1462-5822.2007.00899.x","article-title":"Host cell-dependent secretion and translocation of the LepA and LepB effectors of Legionella pneumophila","volume":"9","author":"Chen","year":"2007","journal-title":"Cell Microbiol."},{"key":"2021112214282714200_B65","doi-asserted-by":"crossref","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":"2021112214282714200_B66","doi-asserted-by":"crossref","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"}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/426\/3\/281\/661427\/bj4260281.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/426\/3\/281\/661427\/bj4260281.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T17:56:57Z","timestamp":1637603817000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/426\/3\/281\/45089\/Molecular-mechanism-of-elongation-factor-1A"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,2,24]]},"references-count":66,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2010,3,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20091351","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,2,24]]}}}