This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Hayes C.S., Aoki S.K., Low D.A.: Bacterial contact-dependent delivery systems. Annu. Rev. Genet., 2010; 44: 71-90HayesC.S.AokiS.K.LowD.A.Bacterial contact-dependent delivery systems201044719010.1146/annurev.genet.42.110807.09144921047256Search in Google Scholar
So E.C., Mattheis C., Tate E.W., Frankel G., Schroeder G.N.: Creating a customized intracellular niche: Subversion of host cell signaling by Legionella type IV secretion system effectors. Can. J. Microbiol., 2015; 61: 617-635SoE.C.MattheisC.TateE.W.FrankelG.SchroederG.N.Creating a customized intracellular niche: Subversion of host cell signaling by Legionella type IV secretion system effectors20156161763510.1139/cjm-2015-016626059316Search in Google Scholar
Brzostek K., Karwicka E.: Mechanizmy sekrecji bakterii Gramujemnych – system sekrecji II typu, sekrecja w biogenezie pilusów, autotransport. Post. Mikrobiol., 2006; 45: 135-151BrzostekK.KarwickaE.Mechanizmy sekrecji bakterii Gramujemnych – system sekrecji II typu, sekrecja w biogenezie pilusów, autotransport200645135151Search in Google Scholar
Cianciotto N.P.: Type II secretion and Legionella virulence. Curr. Top. Microbiol. Immunol., 2013; 376: 81-102CianciottoN.P.Type II secretion and Legionella virulence20133768110210.1007/82_2013_33923900831Search in Google Scholar
Cianciotto N.P.: Type II secretion: A protein secretion system for all seasons. Trends. Microbiol., 2005; 13: 581-588CianciottoN.P.Type II secretion: A protein secretion system for all seasons20051358158810.1016/j.tim.2005.09.00516216510Search in Google Scholar
White R.C., Cianciotto N.P.: Assessing the impact, genomics and evolution of type II secretion across a large, medically important genus: The Legionella type II secretion paradigm. Microb. Genom., 2019; 5: e000273WhiteR.C.CianciottoN.P.Assessing the impact, genomics and evolution of type II secretion across a large, medically important genus: The Legionella type II secretion paradigm20195e00027310.1099/mgen.0.000273661734131166887Search in Google Scholar
Cianciotto N.P., White R.C.: Expanding role of type II secretion in bacterial pathogenesis and beyond. Infect. Immun., 2017; 85: e00014-17CianciottoN.P.WhiteR.C.Expanding role of type II secretion in bacterial pathogenesis and beyond201785e000141710.1128/IAI.00014-17540084328264910Search in Google Scholar
Korotkov K.V., Sandkvist M.: Architecture, function, and substrates of the type II secretion system. EcoSal. Plus., 2019; 8: 10.1128/ ecosalplus.ESP-0034-2018KorotkovK.V.SandkvistM.Architecture, function, and substrates of the type II secretion system20198101128/ecosalplus.ESP-0034-2018Open DOISearch in Google Scholar
Abdel-Nour M., Duncan C., Low D.E., Guyard C.: Biofilms: The stronghold of Legionella pneumophila. Int. J. Mol. Sci., 2013; 14: 21660-21675Abdel-NourM.DuncanC.LowD.E.GuyardC.Biofilms: The stronghold of Legionella pneumophila201314216602167510.3390/ijms141121660385602724185913Search in Google Scholar
Boamah D.K., Zhou G., Ensminger A.W., O’Connor T.J.: From many hosts, one accidental pathogen: The diverse protozoan hosts of Legionella. Front. Cell. Infect. Microbiol., 2017; 7: 477BoamahD.K.ZhouG.EnsmingerA.W.O’ConnorT.J.From many hosts, one accidental pathogen: The diverse protozoan hosts of Legionella2017747710.3389/fcimb.2017.00477571489129250488Search in Google Scholar
Liu X., Boyer M.A., Holmgren A.M., Shin S.: Legionella-infected macrophages engage the alveolar epithelium to metabolically reprogram myeloid cells and promote antibacterial inflammation. Cell Host Microbe, 2020; 28: 683-698.e6LiuX.BoyerM.A.HolmgrenA.M.ShinS.Legionella-infected macrophages engage the alveolar epithelium to metabolically reprogram myeloid cells and promote antibacterial inflammation202028683698e610.1016/j.chom.2020.07.01932841604Search in Google Scholar
Chaudhry R., Sreenath K., Agrawal S.K., Valavane A.: Legionella and Legionnaires’ disease: Time to explore in India. Indian. J. Med. Microbiol., 2018; 36: 324-333ChaudhryR.SreenathK.AgrawalS.K.ValavaneA.Legionella and Legionnaires’ disease: Time to explore in India20183632433310.4103/ijmm.IJMM_18_29830429383Search in Google Scholar
Ditommaso S., Giacomuzzi M., Arauco Rivera S.R., Raso R., Ferrero P., Zotti C.M.: Virulence of Legionella pneumophila strains isolated from hospital water system and healthcare-associated Legionnaires’ disease in Northern Italy between 2004 and 2009. BMC Infect. Dis., 2014; 14: 483DitommasoS.GiacomuzziM.AraucoRivera S.R.RasoR.FerreroP.ZottiC.M.Virulence of Legionella pneumophila strains isolated from hospital water system and healthcare-associated Legionnaires’ disease in Northern Italy between 2004 and 200920141448310.1186/1471-2334-14-483416820425190206Search in Google Scholar
Gomez-Valero L., Rusniok C., Carson D., Mondino S., Pérez-Cobas A.E., Rolando M., Pasricha S., Reuter S., Demirtas J., Crumbach J. i wsp.: More than 18,000 effectors in the Legionella genus genome provide multiple, independent combinations for replication in human cells. Proc. Natl. Acad. Sci. USA, 2019; 116: 2265-2273Gomez-ValeroL.RusniokC.CarsonD.MondinoS.Pérez-CobasA.E.RolandoM.PasrichaS.ReuterS.DemirtasJ.CrumbachJ.i wspMore than 18,000 effectors in the Legionella genus genome provide multiple, independent combinations for replication in human cells20191162265227310.1073/pnas.1808016116636978330659146Search in Google Scholar
Correia A.M., Ferreira J.S., Borges V., Nunes A., Gomes B., Capucho R., Gonçalves J., Antunes D.M., Almeida S., Mendes A. i wsp.: Probable person-to-person transmission of Legionnaires’ disease. N. Engl. J. Med., 2016; 374: 497-498CorreiaA.M.FerreiraJ.S.BorgesV.NunesA.GomesB.CapuchoR.GonçalvesJ.AntunesD.M.AlmeidaS.MendesA.i wspProbable person-to-person transmission of Legionnaires’ disease201637449749810.1056/NEJMc150535626840151Search in Google Scholar
De Giglio O., Fasano F., Diella G., Lopuzzo M., Napoli C., Apollonio F., Brigida S., Calia C., Campanale C., Marzella A. i wsp.: Legionella and legionellosis in touristic-recreational facilities: Influence of climate factors and geostatistical analysis in Southern Italy (2001–2017). Environ. Res., 2019; 178: 108721De GiglioO.FasanoF.DiellaG.LopuzzoM.NapoliC.ApollonioF.BrigidaS.CaliaC.CampanaleC.MarzellaA.i wspLegionella and legionellosis in touristic-recreational facilities: Influence of climate factors and geostatistical analysis in Southern Italy (2001–2017)201917810872110.1016/j.envres.2019.10872131541805Search in Google Scholar
Surveillance Atlas of Infectious Diseases. http://atlas.ecdc.europa.eu/public/index.aspx (01.11.2020)http://atlas.ecdc.europa.eu/public/index.aspx01.11.2020Search in Google Scholar
Lin S.Y., Chen Y.H., Lu P.L., Tsai Y.M., Chen T.C.: An underestimated co-infection: Swine influenza and pneumonia due to Legionella pneumophila. Am. J. Med. Sci., 2016; 352: 314-316LinS.Y.ChenY.H.LuP.L.TsaiY.M.ChenT.C.An underestimated co-infection: Swine influenza and pneumonia due to Legionella pneumophila201635231431610.1016/j.amjms.2016.04.01027650238Search in Google Scholar
Faulkner G., Garduño R.A.: Ultrastructural analysis of differentiation in Legionella pneumophila. J. Bacteriol., 2002; 184: 70257041FaulknerG.GarduñoR.A.Ultrastructural analysis of differentiation in Legionella pneumophila20021847025704110.1128/JB.184.24.7025-7041.200213545512446652Search in Google Scholar
Fuche F., Vianney A., Andrea C., Doublet P., Gilbert C.: Functional type 1 secretion system involved in Legionella pneumophila virulence. J. Bacteriol., 2015; 197: 563-571FucheF.VianneyA.AndreaC.DoubletP.GilbertC.Functional type 1 secretion system involved in Legionella pneumophila virulence201519756357110.1128/JB.02164-14428597025422301Search in Google Scholar
Qin T., Zhou H., Ren H., Liu W.: Distribution of secretion systems in the genus Legionella and its correlation with pathogenicity. Front. Microbiol., 2017; 8: 388QinT.ZhouH.RenH.LiuW.Distribution of secretion systems in the genus Legionella and its correlation with pathogenicity2017838810.3389/fmicb.2017.00388534848728352254Search in Google Scholar
Nakano N., Kubori T., Kinoshita M., Imada K., Nagai H.: Crystal structure of Legionella DotD: Insights into the relationship between type IVB and type II/III secretion systems. PLoS Pathog., 2010; 6: e1001129NakanoN.KuboriT.KinoshitaM.ImadaK.NagaiH.Crystal structure of Legionella DotD: Insights into the relationship between type IVB and type II/III secretion systems20106e100112910.1371/journal.ppat.1001129295136720949065Search in Google Scholar
White R.C., Truchan H.K., Zheng H., Tyson J.Y., Cianciotto N.P.: Type II secretion promotes bacterial growth within the Legionella-containing vacuole in infected amoebae. Infect. Immun., 2019; 87: e00374-19WhiteR.C.TruchanH.K.ZhengH.TysonJ.Y.CianciottoN.P.Type II secretion promotes bacterial growth within the Legionella-containing vacuole in infected amoebae201987e003741910.1128/IAI.00374-19680334831405960Search in Google Scholar
De Buck E., Maes L., Meyen E., Van Mellaert L., Geukens N., Anné J., Lammertyn E.: Legionella pneumophila Philadelphia-1 tatB and tatC affect intracellular replication and biofilm formation. Biochem. Biophys. Res. Commun. 2005; 331: 1413-1420De BuckE.MaesL.MeyenE.VanMellaert L.GeukensN.AnnéJ.LammertynE.Legionella pneumophila Philadelphia-1 tatB and tatC affect intracellular replication and biofilm formation20053311413142010.1016/j.bbrc.2005.04.06015883032Search in Google Scholar
Personnic N., Striednig B., Hilbi H.: Quorum sensing controls persistence, resuscitation, and virulence of Legionella subpopulations in biofilms. ISME J., 2021; 15: 196-210PersonnicN.StriednigB.HilbiH.Quorum sensing controls persistence, resuscitation, and virulence of Legionella subpopulations in biofilms20211519621010.1038/s41396-020-00774-0785269532951019Search in Google Scholar
Abby S.S., Cury J., Guglielmini J., Néron B., Touchon M., Rocha E.P.: Identification of protein secretion systems in bacterial genomes. Sci. Rep., 2016; 6: 23080AbbyS.S.CuryJ.GuglielminiJ.NéronB.TouchonM.RochaE.P.Identification of protein secretion systems in bacterial genomes201662308010.1038/srep23080479323026979785Search in Google Scholar
Costa T.R., Felisberto-Rodrigues C., Meir A., Prevost M.S., Redzej A., Trokter M., Waksman G.: Secretion systems in Gramnegative bacteria: Structural and mechanistic insights. Nat. Rev. Microbiol., 2015; 13: 343-359CostaT.R.Felisberto-RodriguesC.MeirA.PrevostM.S.RedzejA.TrokterM.WaksmanG.Secretion systems in Gramnegative bacteria: Structural and mechanistic insights20151334335910.1038/nrmicro345625978706Search in Google Scholar
Lu C., Korotkov K.V., Hol W.G.: Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL. J. Struct. Biol., 2014; 187: 223-235LuC.KorotkovK.V.HolW.G.Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL201418722323510.1016/j.jsb.2014.07.006415074725092625Search in Google Scholar
Ghosal D., Kim K.W., Zheng H., Kaplan M., Truchan H.K., Lopez A.E., McIntire I.E., Vogel J.P., Cianciotto N.P., Jensen G.J.: In vivo structure of the Legionella type II secretion system by electron cryotomography. Nat. Microbiol., 2019; 4: 2101-2108GhosalD.KimK.W.ZhengH.KaplanM.TruchanH.K.LopezA.E.McIntireI.E.VogelJ.P.CianciottoN.P.JensenG.J.In vivo structure of the Legionella type II secretion system by electron cryotomography201942101210810.1038/s41564-019-0603-6687991031754273Search in Google Scholar
Thomassin J.L., Santos Moreno J., Guilvout I., Tran Van Nhieu G., Francetic O.: The trans-envelope architecture and function of the type 2 secretion system: New insights raising new questions. Mol. Microbiol., 2017; 105: 211-226ThomassinJ.L.SantosMoreno J.GuilvoutI.TranVan Nhieu G.FranceticO.The trans-envelope architecture and function of the type 2 secretion system: New insights raising new questions201710521122610.1111/mmi.1370428486768Search in Google Scholar
Filloux A., Voulhoux R.: Multiple structures disclose the secretins’ secrets. J. Bacteriol. 2018; 200: e00702-17FillouxA.VoulhouxR.Multiple structures disclose the secretins’ secrets2018200e007021710.1128/JB.00702-17580968929263097Search in Google Scholar
Naskar S., Hohl M., Tassinari M., Low H.H.: The structure and mechanism of the bacterial type II secretion system. Mol. Microbiol., 2021; 115: 412-424NaskarS.HohlM.TassinariM.LowH.H.The structure and mechanism of the bacterial type II secretion system202111541242410.1111/mmi.1466433283907Search in Google Scholar
Nivaskumar M., Francetic O.: Type II secretion system: A magic beanstalk or a protein escalator. Biochim. Biophys. Acta, 2014; 1843: 1568-1577NivaskumarM.FranceticO.Type II secretion system: A magic beanstalk or a protein escalator201418431568157710.1016/j.bbamcr.2013.12.020Search in Google Scholar
Gray M.D., Bagdasarian M., Hol W.G., Sandkvist M.: In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae. Mol. Microbiol., 2011; 79: 786-798GrayM.D.BagdasarianM.HolW.G.SandkvistM.In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae20117978679810.1111/j.1365-2958.2010.07487.xSearch in Google Scholar
López-Castilla A., Thomassin J.L., Bardiaux B., Zheng W., Nivaskumar M., Yu X., Nilges M., Egelman E.H., Izadi-Pruneyre N., Francetic O.: Structure of the calcium-dependent type 2 secretion pseudopilus. Nat. Microbiol., 2017; 2: 1686-1695López-CastillaA.ThomassinJ.L.BardiauxB.ZhengW.NivaskumarM.YuX.NilgesM.EgelmanE.H.Izadi-PruneyreN.FranceticO.Structure of the calcium-dependent type 2 secretion pseudopilus201721686169510.1038/s41564-017-0041-2Search in Google Scholar
Nunn D.: Bacterial type II protein export and pilus biogenesis: More than just homologies? Trends Cell Biol., 1999; 9: 402-408NunnD.Bacterial type II protein export and pilus biogenesis: More than just homologies?1999940240810.1016/S0962-8924(99)01634-7Search in Google Scholar
Guilvout I., Chami M., Engel A., Pugsley A.P., Bayan N.: Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. EMBO J., 2006; 25: 5241-5249GuilvoutI.ChamiM.EngelA.PugsleyA.P.BayanN.Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin2006255241524910.1038/sj.emboj.7601402163660817082772Search in Google Scholar
Viarre V., Cascales E., Ball G., Michel G.P., Filloux A., Voulhoux R.: HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor. J. Biol. Chem., 2009; 284: 33815-33823ViarreV.CascalesE.BallG.MichelG.P.FillouxA.VoulhouxR.HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor2009284338153382310.1074/jbc.M109.065938279715119815547Search in Google Scholar
Carter T., Buensuceso R.N., Tammam S., Lamers R.P., Harvey H., Howell P.L., Burrows L.L.: The type IVa pilus machinery is recruited to sites of future cell division. mBio, 2017; 8: e02103-16CarterT.BuensucesoR.N.TammamS.LamersR.P.HarveyH.HowellP.L.BurrowsL.L.The type IVa pilus machinery is recruited to sites of future cell division20178e021031610.1128/mBio.02103-16528550428143978Search in Google Scholar
Yahashiri A., Jorgenson M.A., Weiss D.S.: The SPOR domain, a widely conserved peptidoglycan binding domain that targets proteins to the site of cell division. J. Bacteriol., 2017; 199: e00118-17YahashiriA.JorgensonM.A.WeissD.S.The SPOR domain, a widely conserved peptidoglycan binding domain that targets proteins to the site of cell division2017199e001181710.1128/JB.00118-17549474128396350Search in Google Scholar
Truchan H.K., Christman H.D., White R.C., Rutledge N.S., Cianciotto N.P.: Type II secretion substrates of Legionella pneumophila translocate out of the pathogen-occupied vacuole via a semipermeable membrane. mBio, 2017; 8: e00870-17TruchanH.K.ChristmanH.D.WhiteR.C.RutledgeN.S.CianciottoN.P.Type II secretion substrates of Legionella pneumophila translocate out of the pathogen-occupied vacuole via a semipermeable membrane20178e008701710.1128/mBio.00870-17547889728634242Search in Google Scholar
Freudl R.: Signal peptides for recombinant protein secretion in bacterial expression systems. Microb. Cell Fact., 2018; 17: 52FreudlR.Signal peptides for recombinant protein secretion in bacterial expression systems2018175210.1186/s12934-018-0901-3587501429598818Search in Google Scholar
Cianciotto N.P.: Many substrates and functions of type II secretion: Lessons learned from Legionella pneumophila. Future Microbiol., 2009; 4: 797-805CianciottoN.P.Many substrates and functions of type II secretion: Lessons learned from Legionella pneumophila2009479780510.2217/fmb.09.53275469319722835Search in Google Scholar
Rusch S.L., Kendall D.A.: Interactions that drive Sec-dependent bacterial protein transport. Biochemistry, 2007; 46: 9665-9673RuschS.L.KendallD.A.Interactions that drive Sec-dependent bacterial protein transport2007469665967310.1021/bi7010064267560717676771Search in Google Scholar
Denks K., Vogt A., Sacchelaru I., Petriman N.A., Kudva R., Koch H.G.: The Sec translocon mediated protein transport in prokaryotes and eukaryotes. Mol. Membr. Biol., 2014; 31: 58-84DenksK.VogtA.SacchelaruI.PetrimanN.A.KudvaR.KochH.G.The Sec translocon mediated protein transport in prokaryotes and eukaryotes201431588410.3109/09687688.2014.90745524762201Search in Google Scholar
Elvekrog M.M., Walter P.: Dynamics of co-translational protein targeting. Curr. Opin. Chem. Biol., 2015; 29: 79-86ElvekrogM.M.WalterP.Dynamics of co-translational protein targeting201529798610.1016/j.cbpa.2015.09.016468444026517565Search in Google Scholar
Bechtluft P., Nouwen N., Tans S.J., Driessen A.J.: SecB – a chaperone dedicated to protein translocation. Mol. Biosyst., 2010; 6: 620-627BechtluftP.NouwenN.TansS.J.DriessenA.J.SecB – a chaperone dedicated to protein translocation2010662062710.1039/B915435C20237639Search in Google Scholar
Lycklama A., Nijeholt J.A., Driessen A.J.: The bacterial Sec-translocase: Structure and mechanism. Philos. Trans. R. Soc. B. Lond. B Biol. Sci., 2012; 367: 1016-1028LycklamaA.NijeholtJ.A.DriessenA.J.The bacterial Sec-translocase: Structure and mechanism20123671016102810.1098/rstb.2011.0201329743222411975Search in Google Scholar
Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S., Tanaka T., Perederina A., Vassylyev D.G., Kohno T., Maturana A.D., Ito K., Nureki O.: Structure and function of a membrane component SecDF that enhances protein export. Nature, 2011; 474: 235-238TsukazakiT.MoriH.EchizenY.IshitaniR.FukaiS.TanakaT.PerederinaA.VassylyevD.G.KohnoT.MaturanaA.D.ItoK.NurekiO.Structure and function of a membrane component SecDF that enhances protein export201147423523810.1038/nature09980369791521562494Search in Google Scholar
Dalbey R.E., Wang P., van Dijl J.M.: Membrane proteases in the bacterial protein secretion and quality control pathway. Microbiol. Mol. Biol. Rev., 2012; 76: 311-330DalbeyR.E.WangP.van DijlJ.M.Membrane proteases in the bacterial protein secretion and quality control pathway20127631133010.1128/MMBR.05019-11337224822688815Search in Google Scholar
Palmer T., Berks B.C.: The twin-arginine translocation (Tat) protein export pathway. Nat. Rev. Microbiol., 2012; 10: 483-496PalmerT.BerksB.C.The twin-arginine translocation (Tat) protein export pathway20121048349610.1038/nrmicro281422683878Search in Google Scholar
Oertel D., Schmitz S., Freudl R.: A TatABC-type Tat translocase is required for unimpaired aerobic growth of Corynebacterium glutamicum ATCC13032. PLoS One, 2015; 10: e0123413OertelD.SchmitzS.FreudlR.A TatABC-type Tat translocase is required for unimpaired aerobic growth of Corynebacterium glutamicum ATCC13032201510e012341310.1371/journal.pone.0123413438355925837592Search in Google Scholar
Sargent F., Stanley N.R., Berks B.C., Palmer T.: Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein. J. Biol. Chem., 1999; 274: 36073-36082SargentF.StanleyN.R.BerksB.C.PalmerT.Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein1999274360733608210.1074/jbc.274.51.36073Search in Google Scholar
Simone D., Bay D.C., Leach T., Turner R.J.: Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental niche. PLoS One, 2013; 8: e78742SimoneD.BayD.C.LeachT.TurnerR.J.Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental niche20138e7874210.1371/journal.pone.0078742Search in Google Scholar
Blaudeck N., Kreutzenbeck P., Müller M., Sprenger G.A., Freudl R.: Isolation and characterization of bifunctional Escherichia coli TatA mutant proteins that allow efficient Tat-dependent protein translocation in the absence of TatB. J. Biol. Chem., 2005; 280: 3426-3432BlaudeckN.KreutzenbeckP.MüllerM.SprengerG.A.FreudlR.Isolation and characterization of bifunctional Escherichia coli TatA mutant proteins that allow efficient Tat-dependent protein translocation in the absence of TatB20052803426343210.1074/jbc.M411210200Search in Google Scholar
Jongbloed J.D., van der Ploeg R., van Dijl J.M.: Bifunctional TatA subunits in minimal Tat protein translocases. Trends Microbiol., 2006; 14: 2-4JongbloedJ.D.van derPloeg R.van DijlJ.M.Bifunctional TatA subunits in minimal Tat protein translocases2006142410.1016/j.tim.2005.11.001Search in Google Scholar
Alami M., Lüke I., Deitermann S., Eisner G., Koch H.G., Brunner J., Müller M.: Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell, 2003; 12: 937-946AlamiM.LükeI.DeitermannS.EisnerG.KochH.G.BrunnerJ.MüllerM.Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli20031293794610.1016/S1097-2765(03)00398-8Search in Google Scholar
Lausberg F., Fleckenstein S., Kreutzenbeck P., Fröbel J., Rose P., Müller M., Freudl R.: Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli. PLoS One, 2012; 7: e39867LausbergF.FleckensteinS.KreutzenbeckP.FröbelJ.RoseP.MüllerM.FreudlR.Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli20127e3986710.1371/journal.pone.0039867338369422761916Search in Google Scholar
Brüser T., Sanders C.: An alternative model of the twin arginine translocation system. Microbiol. Res., 2003; 158: 7-17BrüserT.SandersC.An alternative model of the twin arginine translocation system200315871710.1078/0944-5013-0017612608575Search in Google Scholar
Gohlke U., Pullan L., McDevitt C.A., Porcelli I., de Leeuw E., Palmer T., Saibil H.R., Berks B.C.: The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc. Natl. Acad. Sci. USA, 2005; 102: 10482-10486GohlkeU.PullanL.McDevittC.A.PorcelliI.de LeeuwE.PalmerT.SaibilH.R.BerksB.C.The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter2005102104821048610.1073/pnas.0503558102118078116027357Search in Google Scholar
Mori H., Cline K.: A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase. J. Cell Biol., 2002; 157: 205-210MoriH.ClineK.A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase200215720521010.1083/jcb.200202048219925211956224Search in Google Scholar
Lüke I., Hanford J.I., Palmer T., Sargent F.: Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB. Arch. Microbiol., 2009; 191: 919-925LükeI.HanfordJ.I.PalmerT.SargentF.Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB200919191992510.1007/s00203-009-0516-519809807Search in Google Scholar
Hospenthal M.K., Costa T.R., Waksman G.A.: A comprehensive guide to pilus biogenesis in Gram-negative bacteria. Nat. Rev. Microbiol., 2017; 15: 365-379HospenthalM.K.CostaT.R.WaksmanG.A.A comprehensive guide to pilus biogenesis in Gram-negative bacteria20171536537910.1038/nrmicro.2017.4028496159Search in Google Scholar
Peabody C.R., Chung Y.J., Yen M.R., Vidal-Ingigliardi D., Pugsley A.P., Saier M.H.: Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Microbiology, 2003; 149: 3051-3072PeabodyC.R.ChungY.J.YenM.R.Vidal-IngigliardiD.PugsleyA.P.SaierM.H.Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella20031493051307210.1099/mic.0.26364-014600218Search in Google Scholar
Francetić O., Pugsley A.P.: Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca. J. Bacteriol., 2005; 187: 7045-7055FrancetićO.PugsleyA.P.Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca20051877045705510.1128/JB.187.20.7045-7055.2005125160016199575Search in Google Scholar
Johnson T.L., Abendroth J., Hol W.G., Sandkvist M.: Type II secretion: From structure to function. FEMS Microbiol. Lett., 2006; 255: 175-186JohnsonT.L.AbendrothJ.HolW.G.SandkvistM.Type II secretion: From structure to function200625517518610.1111/j.1574-6968.2006.00102.x16448494Search in Google Scholar
Liles M.R., Viswanathan V.K., Cianciotto N.P.: Identification and temperature regulation of Legionella pneumophila genes involved in type IV pilus biogenesis and type II protein secretion. Infect. Immun., 1998; 66: 1776-1782LilesM.R.ViswanathanV.K.CianciottoN.P.Identification and temperature regulation of Legionella pneumophila genes involved in type IV pilus biogenesis and type II protein secretion1998661776178210.1128/IAI.66.4.1776-1782.19981081209529113Search in Google Scholar
Liles M.R., Edelstein P.H., Cianciotto N.P.: The prepilin peptidase is required for protein secretion by and the virulence of the intracellular pathogen Legionella pneumophila. Mol. Microbiol., 1999; 31: 959-970LilesM.R.EdelsteinP.H.CianciottoN.P.The prepilin peptidase is required for protein secretion by and the virulence of the intracellular pathogen Legionella pneumophila19993195997010.1046/j.1365-2958.1999.01239.x10048038Search in Google Scholar
Hales L.M., Shuman H.A.: Legionella pneumophila contains a type II general secretion pathway required for growth in amoebae as well as for secretion of the Msp protease. Infect. Immun. 1999; 67: 3662-3666HalesL.M.ShumanH.A.Legionella pneumophila contains a type II general secretion pathway required for growth in amoebae as well as for secretion of the Msp protease1999673662366610.1128/IAI.67.7.3662-3666.199911656110377156Search in Google Scholar
Rossier O., Cianciotto N.P.: Type II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila. Infect. Immun., 2001; 69: 20922098RossierO.CianciottoN.P.Type II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila2001692092209810.1128/IAI.69.4.2092-2098.20019813411254562Search in Google Scholar
Rossier O., Starkenburg S.R., Cianciotto N.P.: Legionella pneumophila type II protein secretion promotes virulence in the A/J mouse model of Legionnaires’ disease pneumonia. Infect. Immun., 2004; 72: 310-321RossierO.StarkenburgS.R.CianciottoN.P.Legionella pneumophila type II protein secretion promotes virulence in the A/J mouse model of Legionnaires’ disease pneumonia20047231032110.1128/IAI.72.1.310-321.200434401214688110Search in Google Scholar
Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F. i wsp.: Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity. Nat. Genet., 2004; 36: 1165-1173CazaletC.RusniokC.BruggemannH.ZidaneN.MagnierA.MaL.TichitM.JarraudS.BouchierC.VandeneschF.i wspEvidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity2004361165117310.1038/ng144715467720Search in Google Scholar
Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M. i wsp.: The genomic sequence of the accidental pathogen Legionella pneumophila. Science, 2004; 305: 1966-1968ChienM.MorozovaI.ShiS.ShengH.ChenJ.GomezS.M.AsamaniG.HillK.NuaraJ.FederM.i wspThe genomic sequence of the accidental pathogen Legionella pneumophila20043051966196810.1126/science.109977615448271Search in Google Scholar
Glöckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Hacker J., Heuner K.: Identification and characterization of a new conjugation/type IVA secretion system (trb/tra) of Legionella pneumophila Corby localized on two mobile genomic islands. Int. J. Med. Microbiol., 2008; 298: 411-428GlöcknerG.Albert-WeissenbergerC.WeinmannE.JacobiS.SchunderE.SteinertM.HackerJ.HeunerK.Identification and characterization of a new conjugation/type IVA secretion system (trb/tra) of Legionella pneumophila Corby localized on two mobile genomic islands200829841142810.1016/j.ijmm.2007.07.01217888731Search in Google Scholar
DebRoy S., Dao J., Söderberg M., Rossier O., Cianciotto N.P.: Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung. Proc. Natl. Acad. Sci. USA, 2006; 103: 19146-19151DebRoyS.DaoJ.SöderbergM.RossierO.CianciottoN.P.Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung2006103191461915110.1073/pnas.0608279103174819017148602Search in Google Scholar
White R.C., Gunderson F.F., Tyson J.Y., Richardson K.H., Portlock T.J., Garnett J.A., Cianciotto N.P.: Type II secretiondependent aminopeptidase LapA and acyltransferase PlaC are redundant for nutrient acquisition during Legionella pneumophila intracellular infection of amoebas. mBio, 2018; 9: e00528-18WhiteR.C.GundersonF.F.TysonJ.Y.RichardsonK.H.PortlockT.J.GarnettJ.A.CianciottoN.P.Type II secretiondependent aminopeptidase LapA and acyltransferase PlaC are redundant for nutrient acquisition during Legionella pneumophila intracellular infection of amoebas20189e005281810.1128/mBio.00528-18590440729666285Search in Google Scholar
Pearce M.M., Cianciotto N.P.: Legionella pneumophila secretes an endoglucanase that belongs to the family-5 of glycosyl hydrolases and is dependent upon type II secretion. FEMS Microbiol. Lett., 2009; 300: 256-264PearceM.M.CianciottoN.P.Legionella pneumophila secretes an endoglucanase that belongs to the family-5 of glycosyl hydrolases and is dependent upon type II secretion200930025626410.1111/j.1574-6968.2009.01801.x276643219817866Search in Google Scholar
Herrmann V., Eidner A., Rydzewski K., Blädel I., Jules M., Buchrieser C., Eisenreich W., Heuneret K.: GamA is a eukaryoticlike glucoamylase responsible for glycogen- and starch-degrading activity of Legionella pneumophila. Int. J. Med. Microbiol., 2011; 301: 133-139HerrmannV.EidnerA.RydzewskiK.BlädelI.JulesM.BuchrieserC.EisenreichW.HeuneretK.GamA is a eukaryoticlike glucoamylase responsible for glycogen- and starch-degrading activity of Legionella pneumophila201130113313910.1016/j.ijmm.2010.08.01620965781Search in Google Scholar
Rossier O., Dao J., Cianciotto N.P.: The type II secretion system of Legionella pneumophila elaborates two aminopeptidases as well as a metalloprotease that contributes to differential infection among protozoan hosts. Appl. Environ. Microbiol., 2008; 74: 753-761RossierO.DaoJ.CianciottoN.P.The type II secretion system of Legionella pneumophila elaborates two aminopeptidases as well as a metalloprotease that contributes to differential infection among protozoan hosts20087475376110.1128/AEM.01944-07222773118083880Search in Google Scholar
Abdel-Nour M., Duncan C., Prashar A., Rao C., Ginevra C., Jarraud S., Low D.E., Ensminger A.W., Terebiznik M.R., Guyard C.: The Legionella pneumophila collagen-like protein mediates sedimentation, autoaggregation, and pathogen-phagocyte interactions. Appl. Environ. Microbiol., 2014; 80: 1441-1454Abdel-NourM.DuncanC.PrasharA.RaoC.GinevraC.JarraudS.LowD.E.EnsmingerA.W.TerebiznikM.R.GuyardC.The Legionella pneumophila collagen-like protein mediates sedimentation, autoaggregation, and pathogen-phagocyte interactions2014801441145410.1128/AEM.03254-13391107024334670Search in Google Scholar
Aragon V., Rossier O., Cianciotto N.P.: Legionella pneumophila genes that encode lipase and phospholipase C activities. Microbiology, 2002; 148: 2223-2231AragonV.RossierO.CianciottoN.P.Legionella pneumophila genes that encode lipase and phospholipase C activities20021482223223110.1099/00221287-148-7-222312101309Search in Google Scholar
Söderberg M.A., Cianciotto N.P.: A Legionella pneumophila pep-tidyl-prolyl cis-trans isomerase present in culture supernatants is necessary for optimal growth at low temperatures. Appl. Environ. Microbiol., 2008; 74: 1634-1638SöderbergM.A.CianciottoN.P.A Legionella pneumophila pep-tidyl-prolyl cis-trans isomerase present in culture supernatants is necessary for optimal growth at low temperatures2008741634163810.1128/AEM.02512-07225860918165359Search in Google Scholar
Aragon V., Kurtz S., Cianciotto N.P.: Legionella pneumophila major acid phosphatase and its role in intracellular infection. Infect. Immun., 2001; 69: 177-185AragonV.KurtzS.CianciottoN.P.Legionella pneumophila major acid phosphatase and its role in intracellular infection20016917718510.1128/IAI.69.1.177-185.20019787011119504Search in Google Scholar
Tyson J.Y., Vargas P., Cianciotto N.P.: The novel Legionella pneumophila type II secretion substrate NttC contriubtes to infection of amoebae Hartmannella vermiformis and Willaertia magna. Microbiology, 2014; 160: 2732-2744TysonJ.Y.VargasP.CianciottoN.P.The novel Legionella pneumophila type II secretion substrate NttC contriubtes to infection of amoebae Hartmannella vermiformis and Willaertia magna20141602732274410.1099/mic.0.082750-0425291125253612Search in Google Scholar
Flieger A., Gong S., Faigle M., Stevanovic S., Cianciotto N.P., Neumeister B.: Novel lysophospholipase A secreted by Legionella pneumophila. J. Bacteriol., 2001; 183: 2121-2124FliegerA.GongS.FaigleM.StevanovicS.CianciottoN.P.NeumeisterB.Novel lysophospholipase A secreted by Legionella pneumophila20011832121212410.1128/JB.183.6.2121-2124.20019511111222614Search in Google Scholar
Flieger A., Neumeister B., Cianciotto N.P.: Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine. Infect. Immun., 2002; 70: 6094-6106FliegerA.NeumeisterB.CianciottoN.P.Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine2002706094610610.1128/IAI.70.11.6094-6106.200213042212379686Search in Google Scholar
Banerji S., Bewersdorff M., Hermes B., Cianciotto N.P., Flieger A.: Characterization of the major secreted zinc metalloproteasedependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila. Infect. Immun., 2005; 73: 2899-2909BanerjiS.BewersdorffM.HermesB.CianciottoN.P.FliegerA.Characterization of the major secreted zinc metalloproteasedependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila2005732899290910.1128/IAI.73.5.2899-2909.2005108737015845496Search in Google Scholar
McCoy-Simandle K., Stewart C.R., Dao J., DebRoy S., Rossier O., Bryce P.J., Cianciotto N.P.: Legionella pneumophila type II secretion dampens the cytokine response of infected macrophages and epithelia. Infect. Immun., 2011; 79: 1984-1997McCoy-SimandleK.StewartC.R.DaoJ.DebRoyS.RossierO.BryceP.J.CianciottoN.P.Legionella pneumophila type II secretion dampens the cytokine response of infected macrophages and epithelia2011791984199710.1128/IAI.01077-10308815621383054Search in Google Scholar
Rossier O., Dao J., Cianciotto N.P.: A type II secreted RNase of Legionella pneumophila facilitates optimal intracellular infection of Hartmannella vermiformis. Microbiology, 2009; 155: 882-890RossierO.DaoJ.CianciottoN.P.A type II secreted RNase of Legionella pneumophila facilitates optimal intracellular infection of Hartmannella vermiformis200915588289010.1099/mic.0.023218-0266239119246759Search in Google Scholar
Hiller M., Lang C., Michel W., Flieger A.: Secreted phospholipases of the lung pathogen Legionella pneumophila. Int. J. Med. Microbiol., 2018; 308: 168-175HillerM.LangC.MichelW.FliegerA.Secreted phospholipases of the lung pathogen Legionella pneumophila201830816817510.1016/j.ijmm.2017.10.00229108710Search in Google Scholar
Flieger A., Frischknecht F., Häcker G., Hornef M.W., Pradel G.: Pathways of host cell exit by intracellular pathogens. Microb. Cell, 2018; 5: 525-544FliegerA.FrischknechtF.HäckerG.HornefM.W.PradelG.Pathways of host cell exit by intracellular pathogens2018552554410.15698/mic2018.12.659628202130533418Search in Google Scholar
Hoffmann C., Harrison C.F., Hilbi H.: The natural alternative: Protozoa as cellular models for Legionella infection. Cell. Microbiol., 2014; 16: 15-26HoffmannC.HarrisonC.F.HilbiH.The natural alternative: Protozoa as cellular models for Legionella infection201416152610.1111/cmi.1223524168696Search in Google Scholar
Lang C., Rastew E., Hermes B., Siegbrecht E., Ahrends R., Banerji S., Flieger A.: Zinc metalloproteinase ProA directly activates Legionella pneumophila PlaC glycerophospholipid:cholesterol acyltransferase. J. Biol. Chem., 2012; 287: 23464-23478LangC.RastewE.HermesB.SiegbrechtE.AhrendsR.BanerjiS.FliegerA.Zinc metalloproteinase ProA directly activates Legionella pneumophila PlaC glycerophospholipid:cholesterol acyltransferase2012287234642347810.1074/jbc.M112.346387339062322582391Search in Google Scholar
Banerji S., Aurass P., Flieger A.: The manifold phospholipases A of Legionella pneumophila – identification, export, regulation, and their link to bacterial virulence. Int. J. Med. Microbiol., 2008; 298: 169-181BanerjiS.AurassP.FliegerA.The manifold phospholipases A of Legionella pneumophila – identification, export, regulation, and their link to bacterial virulence200829816918110.1016/j.ijmm.2007.11.00418178130Search in Google Scholar
Best A., Jones S., Abu Kwaik Y.: Mammalian solute carrier (SLC)-like transporters of Legionella pneumophila. Sci. Rep., 2018; 8: 8352BestA.JonesS.AbuKwaik Y.Mammalian solute carrier (SLC)-like transporters of Legionella pneumophila20188835210.1038/s41598-018-26782-x597423429844490Search in Google Scholar
Price C.T., Richards A.M., Von Dwingelo J.E., Samara H.A, Abu Kwaik Y.: Amoeba host-Legionella synchronization of amino acid auxotrophy and its role in bacterial adaptation and pathogenic evolution. Environ. Microbiol., 2014; 16: 350-358PriceC.T.RichardsA.M.VonDwingelo J.E.SamaraH.AAbuKwaik Y.Amoeba host-Legionella synchronization of amino acid auxotrophy and its role in bacterial adaptation and pathogenic evolution20141635035810.1111/1462-2920.12290394689124112119Search in Google Scholar
Rehman S., Grigoryeva L.S., Richardson K.H., Corsini P., White R.C., Shaw R., Portlock T.J., Dorgan B., Zanjani Z.S., Fornili A., Cianciotto N.P., Garnett J.A.: Structure and functional analysis of the Legionella pneumophila chitinase ChiA reveals a novel mechanism of metal-dependent mucin degradation. PLoS Pathog., 2020; 16: e1008342RehmanS.GrigoryevaL.S.RichardsonK.H.CorsiniP.WhiteR.C.ShawR.PortlockT.J.DorganB.ZanjaniZ.S.ForniliA.CianciottoN.P.GarnettJ.A.Structure and functional analysis of the Legionella pneumophila chitinase ChiA reveals a novel mechanism of metal-dependent mucin degradation202016e100834210.1371/journal.ppat.1008342722457432365117Search in Google Scholar
Portlock T.J., Tyson J.Y., Dantu S.C., Rehman S., White R.C., McIntire I.E., Sewell L., Richardson K., Shaw R., Pandini A., Cianciotto N.P., Garnett J.A.: Structure, dynamics and cellular insight into novel substrates of the Legionella pneumophila type II secretion system. Front. Mol. Biosci., 2020; 7: 112PortlockT.J.TysonJ.Y.DantuS.C.RehmanS.WhiteR.C.McIntireI.E.SewellL.RichardsonK.ShawR.PandiniA.CianciottoN.P.GarnettJ.A.Structure, dynamics and cellular insight into novel substrates of the Legionella pneumophila type II secretion system2020711210.3389/fmolb.2020.00112732595732656228Search in Google Scholar
de Felipe K.S., Glover R.T., Charpentier X., Anderson O.R., Reyes R., Pericone C.D, Shuman H.A.: Legionella eukaryotic-like type IV substrates interfere with organelle trafficking. PLoS Pathog., 2008; 4: e1000117de FelipeK.S.GloverR.T.CharpentierX.AndersonO.R.ReyesR.PericoneC.DShumanH.A.Legionella eukaryotic-like type IV substrates interfere with organelle trafficking20084e100011710.1371/journal.ppat.1000117247551118670632Search in Google Scholar
de Felipe K.S., Pampou S., Jovanovic O.S., Pericone C.D., Ye S.F., Kalachikov S., Shuman H.A.: Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer. J. Bacteriol., 2005; 187: 7716-7726de FelipeK.S.PampouS.JovanovicO.S.PericoneC.D.YeS.F.KalachikovS.ShumanH.A.Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer20051877716772610.1128/JB.187.22.7716-7726.2005128029916267296Search in Google Scholar
Gomez-Valero L., Rusniok C., Cazalet C., Buchrieser C.: Comparative and functional genomics of Legionella identified eukaryotic like proteins as key players in host-pathogen interactions. Front. Microbiol., 2011; 2: 208Gomez-ValeroL.RusniokC.CazaletC.BuchrieserC.Comparative and functional genomics of Legionella identified eukaryotic like proteins as key players in host-pathogen interactions2011220810.3389/fmicb.2011.00208320337422059087Search in Google Scholar
Lurie-Weinberger M.N., Gomez-Valero L., Merault N., Glöckner G., Buchrieser C., Gophna U.: The origins of eukaryotic-like proteins in Legionella pneumophila. Int. J. Med. Microbiol., 2010; 300: 470-481Lurie-WeinbergerM.N.Gomez-ValeroL.MeraultN.GlöcknerG.BuchrieserC.GophnaU.The origins of eukaryotic-like proteins in Legionella pneumophila201030047048110.1016/j.ijmm.2010.04.01620537944Search in Google Scholar
Schroeder G.N., Petty N.K., Mousnier A., Harding C.R., Vogrin A.J., Wee B., Fry N.K., Harrison T.G., Newton H.J., Thomson N.R. i wsp.: Legionella pneumophila strain 130b possesses a unique combination of type IV secretion systems and novel Dot/Icm secretion system effector proteins. J. Bacteriol., 2010; 192: 6001-6016SchroederG.N.PettyN.K.MousnierA.HardingC.R.VogrinA.J.WeeB.FryN.K.HarrisonT.G.NewtonH.J.ThomsonN.R.i wspLegionella pneumophila strain 130b possesses a unique combination of type IV secretion systems and novel Dot/Icm secretion system effector proteins20101926001601610.1128/JB.00778-10297644320833813Search in Google Scholar
Hughes E.D., Swanson M.S.: How Legionella defend their turf. eLife, 2019; 8: e48695HughesE.D.SwansonM.S.How Legionella defend their turf20198e4869510.7554/eLife.48695659875831251173Search in Google Scholar
Duncan C., Prashar A., So J., Tang P., Low D.E., Terebiznik M., Guyard C.: Lcl of Legionella pneumophila is an immunogenic GAG binding adhesion that promotes interactions with lung epithelial cells and plays a crucial role in biofilm formation. Infect. Immun., 2011; 79: 2168-2181DuncanC.PrasharA.SoJ.TangP.LowD.E.TerebiznikM.GuyardC.Lcl of Legionella pneumophila is an immunogenic GAG binding adhesion that promotes interactions with lung epithelial cells and plays a crucial role in biofilm formation2011792168218110.1128/IAI.01304-10312584021422183Search in Google Scholar
Lucas C.E., Brown E., Fields B.S.: Type IV pili and type II secretion play a limited role in Legionella pneumophila biofilm colonization and retention. Microbiology, 2006; 152: 3569-3573LucasC.E.BrownE.FieldsB.S.Type IV pili and type II secretion play a limited role in Legionella pneumophila biofilm colonization and retention20061523569357310.1099/mic.0.2006/000497-017159209Search in Google Scholar
Stewart C.R., Rossier O., Cianciotto N.P.: Surface translocation by Legionella pneumophila: A form of sliding motility that is dependent upon type II protein secretion. J. Bacteriol., 2009; 191: 1537-1546StewartC.R.RossierO.CianciottoN.P.Surface translocation by Legionella pneumophila: A form of sliding motility that is dependent upon type II protein secretion20091911537154610.1128/JB.01531-08264819319114479Search in Google Scholar
Söderberg M.A., Rossier O., Cianciotto N.P.: The Type II protein secretion system of Legionella pneumophila promotes growth at low temperatures. J Bacteriol., 2004; 186: 3712-3720SöderbergM.A.RossierO.CianciottoN.P.The Type II protein secretion system of Legionella pneumophila promotes growth at low temperatures20041863712372010.1128/JB.186.12.3712-3720.200441995615175284Search in Google Scholar
Söderberg M.A., Dao J., Starkenburg S. R., Cianciotto N. P.: Importance of type II secretion for survival of Legionella pneumophila in tap water and in amoebae at low temperatures. Appl. Environ. Microbiol., 2008; 74: 5583-5588SöderbergM.A.DaoJ.StarkenburgS. R.CianciottoN. P.Importance of type II secretion for survival of Legionella pneumophila in tap water and in amoebae at low temperatures2008745583558810.1128/AEM.00067-08254664018621869Search in Google Scholar
Tyson J.Y., Pearce M.M., Vargas P., Bagchi S., Mulhern B.J., Cianciotto N.P.: Multiple Legionella pneumophila type II secretion substrates, including a novel protein, contribute to differential infection of amoebae Acanthamoeba castellanii, Hartmannella vermiformis, and Naegleria lovaniensis. Infect. Immun., 2013; 81: 1399-1410TysonJ.Y.PearceM.M.VargasP.BagchiS.MulhernB.J.CianciottoN.P.Multiple Legionella pneumophila type II secretion substrates, including a novel protein, contribute to differential infection of amoebae Acanthamoeba castellanii, Hartmannella vermiformis, and Naegleria lovaniensis2013811399141010.1128/IAI.00045-13364800323429532Search in Google Scholar
Polesky A.H., Ross J.T., Falkow S., Tompkins L.S.: Identification of Legionella pneumophila genes important for infection of amoebas by signature-tagged mutagenesis. Infect. Immun., 2001; 69: 977-987PoleskyA.H.RossJ.T.FalkowS.TompkinsL.S.Identification of Legionella pneumophila genes important for infection of amoebas by signature-tagged mutagenesis20016997798710.1128/IAI.69.2.977-987.20019797711159993Search in Google Scholar
White R.C., Cianciotto N.P.: Type II secretion is necessary for optimal association of the Legionella-containing vacuole with macrophage Rab1B but enhances intracellular replication mainly by Rab1B-independent mechanisms. Infect. Immun., 2016; 84: 33133327WhiteR.C.CianciottoN.P.Type II secretion is necessary for optimal association of the Legionella-containing vacuole with macrophage Rab1B but enhances intracellular replication mainly by Rab1B-independent mechanisms2016843313332710.1128/IAI.00750-16511671027600508Search in Google Scholar
Mallama C.A., McCoy-Simandle K., Cianciotto N.P.: The type II secretion system of Legionella pneumophila dampens the MyD88 and Toll-like receptor 2 signaling pathway in infected human macrophages. Infect. Immun., 2017; 85: e00897-16MallamaC.A.McCoy-SimandleK.CianciottoN.P.The type II secretion system of Legionella pneumophila dampens the MyD88 and Toll-like receptor 2 signaling pathway in infected human macrophages201785e008971610.1128/IAI.00897-16536429828138020Search in Google Scholar
Grabiec A., Meng G., Fichte S., Bessler W., Wagner H., Kirschning C.J.: Human but not murine Toll-like receptor 2 discriminates between tri-palmitoylated and tri-lauroylated peptides. J. Biol. Chem., 2004; 279: 48004-48012GrabiecA.MengG.FichteS.BesslerW.WagnerH.KirschningC.J.Human but not murine Toll-like receptor 2 discriminates between tri-palmitoylated and tri-lauroylated peptides2004279480044801210.1074/jbc.M40531120015342637Search in Google Scholar
Lang C., Hiller M., Flieger A.: Disulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity. Sci. Rep., 2017; 7: 16313LangC.HillerM.FliegerA.Disulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity201771631310.1038/s41598-017-12796-4570117429176577Search in Google Scholar
Jan A.T.: Outer membrane vesicles (OMVs) of gram-negative bacteria: A perspective update. Front. Microbiol., 2017; 8: 1053JanA.T.Outer membrane vesicles (OMVs) of gram-negative bacteria: A perspective update20178105310.3389/fmicb.2017.01053546529228649237Search in Google Scholar