. .. Effet, 112 5.4.1. Influence de la surexpression des gènes d'intérêt sur la formation du kyste

, Publication : Erat, a newly described protein impairs encystment in the amoeba Acanthamoeba castellanii, p.116

. .. Discussion,

. .. Annexes,

R. Anwar, A. Khan, N. A. Siddiqui, and R. , Combating Acanthamoeba spp. cysts: What are the options?, Parasites and Vectors, vol.11, pp.4-6, 2018.

Y. Aqeel, R. Siddiqui, and N. A. Khan, Silencing of xylose isomerase and cellulose synthase by siRNA inhibits encystation in Acanthamoeba castellanii, Parasitol Res, vol.112, pp.1221-1227, 2013.

C. Aurrecoechea, A. Barreto, J. Brestelli, B. P. Brunk, E. Caler et al.,

X. , G. A. Grant, G. Harb, O. S. Heiges, M. Iodice et al., AmoebaDB and MicrosporidiaDB: functional genomic resources for Amoebozoa and Microsporidia species, Nucleic Acids Res, vol.39, pp.612-619, 2011.

E. Bateman, Expression plasmids and production of EGFP in stably transfected Acanthamoeba, Protein Expr Purif, vol.70, pp.95-100, 2010.

A. Chawla, M. Armstrong, and C. F. , Acanthamoeba keratitis-An increasing incidence, Contact Lens Anterior Eye, vol.37, p.120, 2014.

N. Chelkha, A. Levasseur, P. Pontarotti, D. Raoult, B. Scola et al., Colson P, 2018.

M. Clarke, A. J. Lohan, B. Liu, I. Lagkouvardos, S. Roy et al., Genome of, 2013.
URL : https://hal.archives-ouvertes.fr/hal-01988455

, Genome Biol, vol.14, p.11

R. Dudley, S. Alsam, and N. A. Khan, The role of proteases in the differentiation of Acanthamoeba castellanii, FEMS Microbiol Lett, vol.286, pp.9-15, 2008.

R. C. Edgar, MUSCLE: A multiple sequence alignment method with reduced time and space complexity, BMC Bioinformatics, vol.5, pp.1-19, 2004.

L. Favrot, J. S. Blanchard, and O. Vergnolle, Bacterial GCN5-related N-Acetyltransferases: from resistance to regulation, Biochemistry, vol.55, pp.989-1002, 2016.

E. Fouque, M. Trouilhé, V. Thomas, P. Hartemann, M. Rodier et al., , 2012.

, Cellular, biochemical, and molecular changes during encystment of free-living amoebae, Eukaryot Cell, vol.11, pp.382-387

M. Garajová, M. Mrva, N. Va?kovicová, M. Martinka, J. Melicherová et al., , 2019.

G. Greub and D. Raoult, Microorganisms resistant to free-living amoebae, Clin Microbiol Rev, vol.17, pp.413-446, 2004.

J. F. De-jonckheere, Ecology of Acanthamoeba. Rev Infect Dis, vol.13, pp.385-387, 1991.

S. Kalyaanamoorthy, B. Q. Minh, T. Wong, V. Haeseler, A. Jermiin et al., , 2017.

, ModelFinder: fast model selection for accurate phylogenetic estimates, Nat Methods, vol.14, pp.587-589

U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, vol.227, pp.680-685, 1970.

D. Leitsch, M. Köhsler, M. Marchetti-deschmann, A. Deutsch, G. Allmaier et al., Proteomic aspects of Parachlamydia acanthamoebae infection in Acanthamoeba spp, ISME J, vol.4, pp.1366-1374, 2010.

K. J. Livak and T. D. Schmittgen, Analysis of relative gene expression data using realtime quantitative PCR and the 2-??CT method, Methods, vol.25, pp.402-408, 2001.

D. Lloyd, Encystment in Acanthamoeba castellanii: A review, Exp Parasitol, vol.145, pp.20-27, 2014.

A. B. Lopez, K. Sener, E. L. Jarroll, and H. Van-keulen, , 2003.

, Mol Biochem Parasitol, vol.128, pp.51-57

J. Lorenzo-morales, J. Kliescikova, E. Martinez-carretero, D. Pablos, L. M. Profotova et al., Glycogen phosphorylase in Acanthamoeba spp.: Determining the role of the enzyme during the encystment process using RNA interference, Eukaryot Cell, vol.7, pp.509-517, 2008.

P. Magistrado-coxen, Y. Aqeel, A. Lopez, J. R. Haserick, B. R. Urbanowicz et al., , 2019.

, PLoS Negl Trop Dis, vol.13, p.7352

F. Marciano-cabral and G. Cabral, Acanthamoeba spp. as agents of disease in humans, Clin Microbiol Rev, vol.16, pp.273-307, 2003.

A. J. Martinez and G. S. Visvesvaraz, Free-living, amphizoic and opportunistic amebas, 1997.

, Brain Pathol, pp.583-598

T. Mazur, E. Hadas, and I. Iwanicka, The duration of the cyst stage and the viability and virulence of Acanthamoeba isolates, Trop Med Parasitol, vol.46, pp.102-108, 1995.

E. Moon, S. Kim, Y. Hong, D. Chung, . Il et al., , 2015.

, Autophagy Inhibitors as a Potential Antiamoebic Treatment for Acanthamoeba Keratitis, Antimicrob Agents Chemother, vol.59, pp.4020-4025

E. Moon, Y. Hong, D. Chung, Y. Goo, and H. Kong, , 2016.

E. K. Moon, D. Chung, . Il, Y. Hong, and H. H. Kong, Atg3-mediated lipidation of atg8 is involved in encystation of Acanthamoeba, Korean J Parasitol, vol.49, pp.103-108, 2011.

E. K. Moon, D. Chung, . Il, Y. C. Hong, and H. H. Kong, Autophagy protein 8 mediating autophagosome in encysting Acanthamoeba, Mol Biochem Parasitol, vol.168, pp.43-48, 2009.

E. K. Moon, Y. Hong, D. Chung, . Il, Y. K. Goo et al., , 2014.

E. K. Moon, Y. Hong, D. Chung, . Il, and H. H. Kong, Identification of Atg8 isoform in encysting Acanthamoeba, Korean J Parasitol, vol.51, pp.497-502, 2013.

E. K. Moon, Y. Hong, H. A. Lee, F. S. Quan, and H. H. Kong, DNA methylation of gene expression in Acanthamoeba castellanii encystation, Korean J Parasitol, vol.55, pp.115-120, 2017.

E. K. Moon, H. H. Kong, Y. Hong, H. A. Lee, and F. S. Quan, , 2017.

, Korean J Parasitol, vol.55, pp.109-114

A. Naguleswaran, E. V. Elias, J. Mcclintick, H. J. Edenberg, and W. J. Sullivan, , 2010.

, Toxoplasma gondii lysine acetyltransferase GCN5-A functions in the cellular response to alkaline stress and expression of cyst genes, PLoS Pathog, vol.6, p.1001232

L. Nguyen, H. A. Schmidt, V. Haeseler, A. Minh, and B. Q. , IQ-TREE: a fast and effective stochastic algorithm for estimating maximum-likelihood phylogenies, Mol Biol Evol, vol.32, pp.268-274, 2015.

S. Rodríguez-zaragoza, Ecology of free-living amoebae, Crit Rev Microbiol, vol.20, pp.225-241, 1994.

N. M. Seibel, J. Eljouni, M. M. Nalaskowski, and W. Hampe, Nuclear localization of enhanced green fluorescent protein homomultimers, Anal Biochem, vol.368, pp.95-99, 2007.

S. M. Song, B. I. Han, E. K. Moon, Y. R. Lee, H. S. Yu et al., Autophagy protein 16-mediated autophagy is required for the encystation of Acanthamoeba castellanii, Mol Biochem Parasitol, vol.183, pp.158-165, 2012.

V. Thomas, G. Mcdonnell, S. P. Denyer, and J. Y. Maillard, Free-living amoebae and their intracellular pathogenic microorganisms: Risks for water quality, FEMS Microbiol Rev, vol.34, pp.231-259, 2010.

T. Macechko, P. Steimle, P. A. Lindmark, D. G. Erlandsen, S. L. Jarroll et al., , 1992.

, Galactosamine-synthesizing enzymes are induced when Giardia encyst, Mol Biochem Parasitol, vol.56, pp.301-309

M. W. Vetting, L. P. Luiz, M. Yu, S. S. Hegde, S. Magnet et al., , 2005.

, Structure and functions of the GNAT superfamily of acetyltransferases, Arch Biochem Biophys, vol.433, pp.212-226

B. Byrne and M. S. Swanson, Expression of Legionella pneumophila virulence traits in response to growth conditions, Infect Immun, vol.66, pp.3029-3063, 1998.

A. Castellani, An amoeba growing in cultures of a yeast, Nature, vol.126, p.823, 1930.

T. Cavalier-smith, Only six kingdoms of life, Proc R Soc B Biol Sci, vol.271, pp.1251-1262, 2004.

T. Cavalier-smith, E. E. Chao, and R. Lewis, 187-gene phylogeny of protozoan phylum Amoebozoa reveals a new class (Cutosea) of deep-branching, ultrastructurally unique, enveloped marine Lobosa and clarifies amoeba evolution, Mol Phylogenet Evol, vol.99, pp.275-296, 2016.

C. Cazalet, C. Rusniok, H. Brüggemann, N. Zidane, A. Magnier et al., Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity, Nat Genet, vol.36, pp.1165-1173, 2004.

J. P. Chamberland, L. T. Antonow, D. Santos, M. Ritter, and B. , NECAP2 controls clathrin coat recruitment to early endosomes for fast endocytic recycling, J Cell Sci, vol.129, pp.2625-2637, 2016.

J. A. Chambers and J. E. Thompson, A scanning electron microscopic study of the excystment process of Acanthamoeba castellanii, Exp Cell Res, vol.73, pp.415-421, 1972.

B. Chang, F. Kura, J. Amemura-maekawa, N. Koizumi, and H. Watanabe, Identification of a Novel Adhesion Molecule Involved in the Virulence of Legionella pneumophila, Infect Immun, vol.73, pp.4272-4280, 2005.

B. Chávez-munguía, M. Omaña-molina, M. González-lázaro, A. González-robles, P. Bonilla et al., Ultrastructural study of encystation and excystation in Acanthamoeba castellanii, J Eukaryot Microbiol, vol.52, pp.153-158, 2005.

B. Chávez-munguía, L. Salazar-villatoro, A. Lagunes-guillén, M. Omaña-molina, M. Espinosa-cantellano et al., Acanthamoeba castellanii cysts: new ultrastructural findings, Parasitol Res, vol.112, pp.1125-1130, 2013.

J. Chen, K. S. Felipe, C. M. De, H. Lu, O. R. Anderson et al., Legionella effectors that promote nonlytic release from protozoa, Science (80-), vol.303, pp.1358-1361, 2004.

L. Chen, T. Orfeo, G. Gilmartin, and E. Bateman, Mechanism of cyst specific protein 21 mRNA induction during Acanthamoeba differentiation, Biochim Biophys Acta -Mol Cell Res, vol.1691, pp.23-31, 2004.

L. Chen, Z. Peng, and E. Bateman, In vivo interactions of the Acanthamoeba TBP gene promoter, Nucleic Acids Res, vol.32, pp.1251-1260, 2004.

J. Cherfils, Arf GTPases and their effectors: assembling multivalent membranebinding platforms, Curr Opin Struct Biol, vol.29, pp.67-76, 2014.

D. W. Fraser, T. R. Tsai, W. Orenstein, W. E. Parkin, H. J. Beecham et al., Legionnaires' disease: description of an epidemic of pneumonia, N Engl J Med, vol.297, pp.1189-1197, 1977.

L. Gomez-valero, C. Rusniok, M. Rolando, M. Neou, D. Dervins-ravault et al., Comparative analyses of Legionella species identifies genetic features of strains causing Legionnaires' disease, Genome Biol, vol.15, p.505, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01329875

H. Hilbi and A. Kortholt, Role of the small GTPase Rap1 in signal transduction, cell dynamics and bacterial infection, Small GTPases, vol.10, pp.336-342, 2019.

D. W. Huang, B. T. Sherman, X. Zheng, J. Yang, T. Imamichi et al., Extracting biological meaning from large gene lists with DAVID, Curr Protoc Bioinforma, vol.27, 2009.

W. Huang and D. J. Klionsky, Autophagy in yeast: a review of the molecular machinery, Cell Struct Funct, vol.27, pp.409-429, 2002.

S. Ignoul and J. Eggermont, CBS domains: structure, function, and pathology in human proteins, Am J Physiol -Cell Physiol, vol.289, pp.1369-1378, 2005.

H. Inoue, H. Nojima, and H. Okayama, High efficiency transformation of Escherichia coli with plasmids, Gene, vol.96, pp.23-28, 1990.

R. R. Isberg, T. J. O'connor, and M. Heidtman, The Legionella pneumophila replication vacuole: making a cosy niche inside host cells, Nat Rev Microbiol, vol.7, pp.13-24, 2009.

G. Isenberg, U. Aebi, and T. D. Pollard, An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions, Nature, vol.288, pp.455-459, 1980.

C. L. Jackson and S. Bouvet, Arfs at a glance, J Cell Sci, vol.127, pp.4103-4112, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01130377

R. Jaenisch and A. Bird, Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals, Nat Genet, vol.33, pp.245-54, 2003.

S. Jean and A. A. Kiger, Coordination between RAB GTPase and phosphoinositide regulation and functions, Nat Rev Mol Cell Biol, vol.13, pp.463-470, 2012.

C. Jenzer and R. Legouis, , 2017.

, Med Sci, vol.33, pp.238-245

K. C. Jeong, D. Ghosal, Y. Chang, G. J. Jensen, and J. P. Vogel, Polar delivery of Legionella type IV secretion system substrates is essential for virulence, Proc Natl Acad Sci U S A, vol.114, pp.8077-8082, 2017.

D. A. De-jesús-díaz, C. Murphy, A. Sol, M. Dorer, and R. R. Isberg, Host cell S phase restricts Legionella pneumophila intracellular replication by destabilizing the membrane-bound replication compartment, MBio, vol.8, 2017.

J. F. De-jonckheere, Isoenzyme and total protein analysis by agarose isoelectric focusing, and taxonomy of the genus Acanthamoeba, J Protozool, vol.30, pp.701-706, 1983.

J. F. De-jonckheere, Ecology of Acanthamoeba. Rev Infect Dis, vol.13, pp.385-387, 1991.

J. F. De-jonckheere, A century of research on the amoeboflagellate genus Naegleria, Acta Protozool, vol.41, pp.309-342, 2002.

H. H. Kong, T. H. Kim, and D. I. Chung, Purification and characterization of a secretory serine proteinase of Acanthamoeba healyi isolated from GAE, J Parasitol, vol.86, pp.12-19, 2000.

V. Koronakis, J. Eswaran, and C. Hughes, Structure and function of TolC: the bacterial exit duct for proteins and drugs, Annu Rev Biochem, vol.73, pp.467-489, 2004.

K. Kot, N. A. ?anocha-arendarczyk, and D. I. Kosik-bogacka, Amoebas from the genus Acanthamoeba and their pathogenic properties, Ann Parasitol, vol.64, pp.299-308, 2018.

T. Kouzarides, Chromatin modifications and their function, Cell, vol.128, pp.693-705, 2007.

C. Krinos, A. S. High, and F. G. Rodgers, Role of the 25 kDa major outer membrane protein of Legionella pneumophila in attachment to U-937 cells and its potential as a virulence factor for chick embryos, J Appl Microbiol, vol.86, pp.237-244, 1999.

K. Król-turmi?ska and A. Olender, Human infections caused by free-living amoebae, Ann Agric Environ Med, vol.24, pp.254-260, 2017.

B. Ku, K. Lee, W. S. Park, C. Yang, J. Ge et al., VipD of Legionella pneumophila targets activated Rab5 and Rab22 to interfere with endosomal trafficking in macrophages, PLoS Pathog, vol.8, p.1003082, 2012.

S. Lakhundi, N. A. Khan, and R. Siddiqui, The effect of environmental and physiological conditions on excystation of Acanthamoeba castellanii belonging to the T4 genotype, Parasitol Res, vol.113, pp.2809-2816, 2014.

C. Lang, M. Hiller, and A. Flieger, Disulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity, Sci Rep, vol.7, p.16313, 2017.

A. Lazdunski, J. Guzzo, A. Filloux, M. Bally, and M. Murgier, Secretion of extracellular proteins by Pseudomonas aeruginosa, Biochimie, vol.72, pp.147-156, 1990.

J. Lee, S. Song, E. Moon, Y. Lee, B. K. Jha et al., Cysteine protease inhibitor (AcStefin) is required for complete cyst formation of Acanthamoeba, Eukaryot Cell, vol.12, pp.567-574, 2013.

Y. R. Lee, B. K. Na, E. K. Moon, S. M. Song, S. Y. Joo et al., Essential role for an M17 leucine aminopeptidase in encystation of Acanthamoeba castellanii, PLoS One, vol.10, 2015.

D. Leitsch, M. Köhsler, M. Marchetti-deschmann, A. Deutsch, G. Allmaier et al., Major role for cysteine proteases during the early phase of Acanthamoeba castellanii encystment, Eukaryot Cell, vol.9, pp.611-619, 2010.

N. Levanova, I. Tabakova, T. Jank, and Y. Belyi, Purification and analysis of effector glucosyltransferase Lgt1 from Legionella pneumophila, Methods in molecular biology, pp.277-287, 2019.

L. Li, S. J. Wright, S. Krystofova, G. Park, and K. A. Borkovich, Heterotrimeric G protein signaling in filamentous fungi, Annu Rev Microbiol, vol.61, pp.423-452, 2007.

Z. Li, A. S. Dugan, G. Bloomfield, J. Skelton, A. Ivens et al., The amoebal MAP kinase response to Legionella pneumophila is regulated by DupA, Cell Host Microbe, vol.6, pp.253-267, 2009.

Z. Lifshitz, D. Burstein, M. Peeri, T. Zusman, K. Schwartz et al., Computational modeling and experimental validation of the Legionella and Coxiella virulence-related type-IVB secretion signal, Proc Natl Acad Sci, vol.110, pp.707-715, 2013.

W. Liu, Y. Xie, J. Ma, X. Luo, P. Nie et al., IBS: an illustrator for the presentation and visualization of biological sequences: Fig, Bioinformatics, vol.1, pp.3359-3361, 2015.

Y. Liu and Z. Q. Luo, The Legionella pneumophila effector SidJ is required for efficient recruitment of endoplasmic reticulum proteins to the bacterial phagosome, Infect Immun, vol.75, pp.592-603, 2007.

K. J. Livak and T. D. Schmittgen, Analysis of relative gene expression data using realtime quantitative PCR and the 2-??CT method, Methods, vol.25, pp.402-408, 2001.

D. Lloyd, Encystment in Acanthamoeba castellanii: A review, Exp Parasitol, vol.145, pp.20-27, 2014.

D. Lloyd, N. A. Turner, W. Khunkitti, A. C. Hann, J. R. Furr et al., Encystation in Acanthamoeba castellanii: Development of biocide resistance, vol.48, pp.11-16, 2001.

J. Lorenzo-morales, N. Coronado-Álvarez, E. Martínez-carretero, S. K. Maciver, and B. Valladares, Detection of four adenovirus serotypes within water-isolated strains of Acanthamoeba in the Canary Islands, Spain, Am J Trop Med Hyg, vol.77, pp.753-756, 2007.

J. Lorenzo-morales, N. A. Khan, and J. Walochnik, An update on Acanthamoeba keratitis: diagnosis, pathogenesis and treatment, Parasite, vol.22, p.10, 2015.

J. Lorenzo-morales, J. Kliescikova, E. Martinez-carretero, D. Pablos, L. M. Profotova et al., Glycogen phosphorylase in Acanthamoeba spp.: Determining the role of the enzyme during the encystment process using RNA interference, Eukaryot Cell, vol.7, pp.509-517, 2008.

J. Lorenzo-morales, C. M. Martín-navarro, A. López-arencibia, F. Arnalich-montiel, J. E. Piñero et al., Acanthamoeba keratitis: an emerging disease gathering importance worldwide?, Trends Parasitol, vol.29, pp.181-187, 2013.

J. Lorenzo-morales, C. M. Martín-navarro, A. López-arencibia, M. A. Santana-morales, R. N. Afonso-lehmann et al., Therapeutic potential of a combination of two gene-specific small interfering RNAs against clinical strains of Acanthamoeba, Antimicrob Agents Chemother, vol.54, pp.5151-5155, 2010.

J. Lorenzo-morales, A. Ortega-rivas, P. Foronda, N. Abreu-acosta, D. Ballart et al., RNA interference (RNAi) for the silencing of extracellular serine proteases genes in Acanthamoeba: Molecular analysis and effect on pathogenecity, Mol Biochem Parasitol, vol.144, pp.10-15, 2005.

V. P. Losick and R. R. Isberg, NF-?B translocation prevents host cell death after lowdose challenge by Legionella pneumophila, J Exp Med, vol.203, pp.2177-2189, 2006.

H. Lu and M. Clarke, Dynamic properties of Legionella-containing phagosomes in Dictyostelium amoebae, Cell Microbiol, vol.7, pp.995-1007, 2005.

D. Lye, G. S. Fout, S. R. Crout, R. Danielson, C. L. Thio et al., Survey of ground, surface, and potable waters for the presence of Legionella species by EnviroAmp(R) PCR Legionella kit, culture, and immunofluorescent staining, Water Res, vol.31, pp.287-293, 1997.

M. P. Machner and R. R. Isberg, Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila, Dev Cell, vol.11, pp.47-56, 2006.

S. K. Maciver, Asexual Amoebae Escape Muller's Ratchet through Polyploidy, Trends Parasitol, vol.32, pp.855-862, 2016.

N. Mackman, J. M. Nicaud, L. Gray, and I. B. Holland, Secretion of haemolysin by Escherichia coli, Curr Top Microbiol Immunol, vol.125, pp.159-81, 1986.

P. Magistrado-coxen, Y. Aqeel, A. Lopez, J. R. Haserick, B. R. Urbanowicz et al., The most abundant cyst wall proteins of Acanthamoeba castellanii are lectins that bind cellulose and localize to distinct structures in developing and mature cyst walls, PLoS Negl Trop Dis, vol.13, p.7352, 2019.

P. T. Manna, C. Gadelha, A. E. Puttick, and M. C. Field, ENTH and ANTH domain proteins participate in AP2-independent clathrin-mediated endocytosis, J Cell Sci, vol.128, pp.2130-2142, 2015.

F. Marciano-cabral and G. Cabral, Acanthamoeba spp. as agents of disease in humans, Clin Microbiol Rev, vol.16, pp.273-307, 2003.

T. J. Marrie, D. Haldane, and G. Bezanson, Nosocomial Legionnaires' disease: Clinical and radiographic patterns, Can J Infect Dis, vol.3, p.253, 1992.

A. J. Martínez and G. S. Visvesvara, Balamuthia mandrillaris infection, J Med Microbiol, vol.50, pp.205-207, 2001.

A. Mattana, C. Serra, E. Mariotti, G. Delogu, P. L. Fiori et al., Acanthamoeba castellanii promotion of in vitro survival and transmission of coxsackie B3 viruses, Eukaryot Cell, vol.5, pp.665-671, 2006.

F. E. Mattar and T. J. Byers, Morphological changes and the requirements for macromolecule synthesis during excystment of Acanthamoeba castellanii, J Cell Biol, vol.49, pp.507-519, 1971.

N. Maycock and R. Jayaswal, Update on Acanthamoeba Keratitis: Diagnosis, treatment, and outcomes, Cornea, vol.35, pp.713-733, 2016.

T. Mazur, E. Hadas, and I. Iwanicka, The duration of the cyst stage and the viability and virulence of Acanthamoeba isolates, Trop Med Parasitol, vol.46, pp.102-108, 1995.

M. R. Mcclelland, L. T. Vaszar, and F. T. Kagawa, Pneumonia and osteomyelitis due to Legionella longbeachae in a woman with systemic lupus erythematosus, Clin Infect Dis, vol.38, pp.102-106, 2004.

J. E. Mcdade, C. C. Shepard, D. W. Fraser, T. R. Tsai, M. A. Redus et al., Legionnaires' disease: Isolation of a bacterium and demonstration of its role in other respiratory disease, N Engl J Med, vol.297, pp.1197-1203, 1977.

F. Memari, M. Niyyati, and Z. Joneidi, Pathogenic Acanthamoeba T4 genotype isolated from mucosal tissue of a patient with HIV infection: A case report, Iran J Parasitol, vol.12, pp.143-147, 2017.

L. Mengue, M. Régnacq, W. Aucher, E. Portier, Y. Héchard et al., Legionella pneumophila prevents proliferation of its natural host, Acanthamoeba castellanii. Sci Rep, vol.6, p.36448, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01437135

L. Mengue, F. Richard, Y. Caubet, S. Rolland, Y. Héchard et al., Legionella pneumophila decreases velocity of Acanthamoeba castellanii, Exp Parasitol, vol.183, pp.124-127, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01651847

C. Michard, D. Sperandio, N. Baïlo, J. Pizarro-cerdá, L. Leclaire et al., The Legionella kinase legk2 targets the arp2/3 complex to inhibit actin nucleation on phagosomes and allow bacterial evasion of the late endocytic pathway, MBio, vol.6, pp.1-14, 2015.
URL : https://hal.archives-ouvertes.fr/pasteur-01165092

F. Michel, M. Soler-lopez, C. Petosa, P. Cramer, U. Siebenlist et al., Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family, EMBO J, vol.20, pp.6180-6190, 2001.

R. D. Miller, Legionella pneumophila cell envelope: Permeability to hydrophobic molecules, Curr Microbiol, vol.9, pp.349-354, 1983.

N. Mizushima and M. Komatsu, Autophagy: Renovation of cells and tissues, Cell, vol.147, pp.728-741, 2011.

N. Mizushima, T. Yoshimori, and Y. Ohsumi, The role of Atg proteins in autophagosome formation, Annu Rev Cell Dev Biol, vol.27, pp.107-132, 2011.

J. F. Moffat and L. S. Tompkins, A quantitative model of intracellular growth of Legionella pneumophila in Acanthamoeba castellanii, Infect Immun, vol.60, pp.296-301, 1992.

M. Molmeret, O. Alli, M. Radulic, M. Susa, M. Doric et al., The Cterminus of IcmT is essential for pore formation and for intracellular trafficking of Legionella pneumophila within Acanthamoeba polyphaga, Mol Microbiol, vol.43, pp.1139-1150, 2002.

M. Molmeret, D. M. Bitar, L. Han, and Y. A. Kwaik, Cell biology of the intracellular infection by Legionella pneumophila. Microbes Infect, vol.6, pp.129-168, 2004.

A. B. Molofsky and M. S. Swanson, Differentiate to thrive: Lessons from the Legionella pneumophila life cycle, Mol Microbiol, vol.53, pp.29-40, 2004.

E. Moon, C. D. Hong, Y. Kong, and H. , Protein kinase C signaling molecules regulate encystation of Acanthamoeba, Exp Parasitol, vol.132, pp.524-529, 2012.

E. Moon, S. Kim, Y. Hong, D. Chung, . Il et al., Autophagy inhibitors as a potential antiamoebic treatment for Acanthamoeba keratitis, Antimicrob Agents Chemother, vol.59, pp.4020-4025, 2015.

E. Moon, Y. Hong, D. Chung, Y. Goo, and H. Kong, Identification of protein arginine methyltransferase 5 as a regulator for encystation of Acanthamoeba, Korean J Parasitol, vol.54, pp.133-138, 2016.

E. K. Moon, D. Chung, . Il, Y. Hong, and H. H. Kong, Atg3-mediated lipidation of atg8 is involved in encystation of Acanthamoeba, Korean J Parasitol, vol.49, pp.103-108, 2011.

E. K. Moon, D. Chung, . Il, Y. Hong, and H. H. Kong, Expression levels of encystation mediating factors in fresh strain of Acanthamoeba castellanii cyst ESTs, Exp Parasitol, vol.127, pp.811-816, 2011.

E. K. Moon, D. Chung, . Il, Y. C. Hong, and H. H. Kong, Characterization of a serine proteinase mediating encystation of Acanthamoeba, Eukaryot Cell, vol.7, pp.1513-1517, 2008.

E. K. Moon, D. Chung, . Il, Y. C. Hong, and H. H. Kong, Autophagy protein 8 mediating autophagosome in encysting Acanthamoeba, Mol Biochem Parasitol, vol.168, pp.43-48, 2009.

E. K. Moon, Y. Hong, D. Chung, . Il, Y. K. Goo et al., Down-regulation of cellulose synthase inhibits the formation of endocysts in Acanthamoeba, Korean J Parasitol, vol.52, pp.131-135, 2014.

E. K. Moon, Y. Hong, D. Chung, . Il, and H. H. Kong, Cysteine protease involving in autophagosomal degradation of mitochondria during encystation of Acanthamoeba, Mol Biochem Parasitol, vol.185, pp.121-126, 2012.

E. K. Moon, Y. Hong, D. Chung, . Il, and H. H. Kong, Identification of Atg8 isoform in encysting Acanthamoeba, Korean J Parasitol, vol.51, pp.497-502, 2013.

E. K. Moon, Y. Hong, H. A. Lee, F. S. Quan, and H. H. Kong, DNA methylation of gene expression in Acanthamoeba castellanii encystation, Korean J Parasitol, vol.55, pp.115-120, 2017.

E. K. Moon and H. H. Kong, Short-cut pathway to synthesize cellulose of encysting Acanthamoeba, Korean J Parasitol, vol.50, pp.361-364, 2012.

E. K. Moon, H. H. Kong, Y. Hong, H. A. Lee, and F. S. Quan, Identification and characterization of protein arginine methyltransferase 1 in Acanthamoeba castellanii, Korean J Parasitol, vol.55, pp.109-114, 2017.

E. K. Moon, Y. H. Xuan, D. Chung, . Il, Y. Hong et al., Microarray analysis of differentially expressed genes between cysts and trophozoites of Acanthamoeba castellanii, Korean J Parasitol, vol.49, pp.341-347, 2011.

S. M. Moss, I. R. Taylor, D. Ruggero, J. E. Gestwicki, K. M. Shokat et al., A Legionella pneumophila kinase phosphorylates the Hsp70 chaperone family to inhibit eukaryotic protein synthesis, Cell Host Microbe, vol.25, pp.454-462, 2019.

H. Moura, S. Wallace, and G. S. Visvesvara, Acanthamoeba healyi n. sp. and the isoenzyme and immunoblot profiles of Acanthamoeba spp., groups 1 and 3, J Protozool, vol.39, pp.573-83, 1992.

A. Mousnier, G. N. Schroeder, C. A. Stoneham, E. C. So, J. A. Garnett et al., A new method to determine in vivo interactomes reveals binding of the Legionella pneumophila effector PieE to multiple rab GTPases, MBio, vol.5, 2014.

T. Murata, A. Delprato, A. Ingmundson, D. K. Toomre, D. G. Lambright et al., The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotideexchange factor, Nat Cell Biol, vol.8, pp.971-977, 2006.

H. Nagai, J. C. Kagan, X. Zhu, R. A. Kahn, and C. R. Roy, A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes, Science (80-), vol.295, pp.679-682, 2002.

J. Naujoks, C. Tabeling, B. D. Dill, C. Hoffmann, A. S. Brown et al., IFNs modify the proteome of Legionella-containing vacuoles and restrict infection via IRG1-derived itaconic acid, PLoS Pathog, vol.12, p.1005408, 2016.

R. J. Neff and R. H. Neff, The biochemistry of amoebic encystment, Symp Soc Exp Biol, vol.23, pp.51-81, 1969.

H. J. Newton, D. Ang, I. R. Van-driel, and E. L. Hartland, Molecular pathogenesis of infections caused by Legionella pneumophila, Clin Microbiol Rev, vol.23, pp.274-298, 2010.

H. J. Newton, F. M. Sansom, J. Dao, C. Cazalet, H. Bruggemann et al., Significant role for ladC in initiation of Legionella pneumophila infection, Infect Immun, vol.76, pp.3075-3085, 2008.

A. Niewmierzycka and S. Clarke, S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae: Identification of a novel protein arginine methyltransferase, J Biol Chem, vol.274, pp.814-824, 1999.

W. M. Oldham and H. E. Hamm, Heterotrimeric G protein activation by G-proteincoupled receptors, Nat Rev Mol Cell Biol, vol.9, pp.60-71, 2008.

T. Orfeo and E. Bateman, Transcription by RNA polymerase II during Acanthamoeba differentiation, Biochim Biophys Acta -Gene Struct Expr, vol.1443, pp.297-304, 1998.

M. Ott, P. Messner, J. Heesemann, R. Marre, and J. Hacker, Temperature-dependent expression of flagella in Legionella, J Gen Microbiol, vol.137, pp.1955-1961, 1991.

F. C. Page, A revised classification of the Gymnamoebia (Protozoa: Sarcodina), 1976.

, Zool J Linn Soc, vol.58, pp.61-77

S. Pal, S. N. Vishwanath, H. Erdjument-bromage, P. Tempst, and S. Sif, Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes, Mol Cell Biol, vol.24, pp.9630-9645, 2004.

C. Palmer, Y. Tsai, and ?. Cp-k-ae, U (1993) Detection of Legionella species in sewage and ocean water by polymerase chain reaction, direct fluorescentantibody, and plate culture methods, Appl Environ Microbiol, vol.59, pp.3618-3624, 1993.

D. Paolo, G. , D. Camilli, and P. , Phosphoinositides in cell regulation and membrane dynamics, Nature, vol.443, pp.651-657, 2006.

Z. Peng, R. Omaruddin, and E. Bateman, Stable transfection of Acanthamoeba castellanii, Biochim Biophys Acta -Mol Cell Res, vol.1743, pp.93-100, 2005.

H. Petersen and M. Luxton, A comparative analysis of soil fauna populations and their role in decomposition processes, Oikos, vol.39, p.288, 1982.

F. Peurois, G. Peyroche, and J. Cherfils, Small GTPase peripheral binding to membranes: Molecular determinants and supramolecular organization, Biochem Soc Trans, vol.47, pp.13-22, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02363297

K. Picazarri, K. Nakada-tsukui, and T. Nozaki, Autophagy during proliferation and encystation in the protozoan parasite Entamoeba invadens, Infect Immun, vol.76, pp.278-288, 2008.

T. D. Pollard, E. Shelton, R. R. Weihing, and E. D. Korn, Ultrastructural characterization of F-actin isolated from Acanthamoeba castellanii and identification of cytoplasmic filaments as F-actin by reaction with rabbit heavy meromyosin, J Mol Biol, vol.50, pp.91-115, 1970.

D. Popovic, D. Vucic, and I. Dikic, Ubiquitination in disease pathogenesis and treatment, Nat Med, vol.20, pp.1242-1253, 2014.

A. Portela and M. Esteller, Epigenetic modifications and human disease, Nat Biotechnol, vol.28, pp.1057-1068, 2010.

J. L. Potter and R. A. Weisman, Differentiation in Acanthamoeba: ?-glucan synthesis during encystment, BBA -Gen Subj, vol.237, pp.65-74, 1971.

J. L. Potter and R. A. Weisman, Correlation of cellulose synthesis in vivo and in vitro during the encystment of Acanthamoeba, Dev Biol, vol.28, pp.472-479, 1972.

A. Prashar, S. Bhatia, Z. Tabatabaeiyazdi, C. Duncan, R. A. Garduño et al., Mechanism of invasion of lung epithelial cells by filamentous Legionella pneumophila, Cell Microbiol, vol.14, pp.1632-1655, 2012.

C. Price, A. Kwaik, and Y. , The transcriptome of Legionella pneumophilainfected human monocyte-derived macrophages, PLoS One, vol.9, p.114914, 2014.

M. Pussard and R. Pons, Morphologie de la paroi kystique et taxonomie du genre Acanthamoeba (Protozoa, Amoebida), Protistologica, vol.8, pp.557-598, 1977.

J. Qiu and Z. Q. Luo, Legionella and Coxiella effectors: Strength in diversity and activity, Nat Rev Microbiol, vol.15, pp.591-605, 2017.

D. Raoult and M. Boyer, Amoebae as genitors and reservoirs of giant viruses, Intervirology, vol.53, pp.321-329, 2010.

C. Rechnitzer and J. Blom, Engulfment of the Philadelphia strain of Legionella pneumophila within pseudopod coils in human phagocytes. Comparison with other Legionella strains and species, Apmis, vol.97, pp.105-119, 1989.

S. Reddy, R. Devlin, C. Menaa, R. Nishimura, S. J. Choi et al., Isolation and characterization of a cDNA clone encoding a novel peptide (OSF) that enhances osteoclast formation and bone resorption, J Cell Physiol, vol.177, pp.636-645, 1998.

A. M. Richards, V. Dwingelo, J. E. Price, C. T. Kwaik, and Y. A. , Cellular microbiology and molecular ecology of Legionella-amoeba interaction, Virulence, vol.4, pp.307-314, 2013.

B. Ritter, A. Y. Denisov, J. Philie, P. D. Allaire, V. Legendre-guillemin et al., The NECAP PHear domain increases clathrin accessory protein binding potential, EMBO J, vol.26, pp.4066-4077, 2007.

B. Ritter, A. Y. Denisov, J. Philie, C. Deprez, E. C. Tung et al., Two WXXF-based motifs in NECAPs define the specificity of accessory protein binding to AP-1 and AP-2, EMBO J, vol.23, pp.3701-3710, 2004.

B. Ritter, S. Murphy, H. Dokainish, M. Girard, M. V. Gudheti et al., NECAP1 Regulates AP-2 interactions to control vesicle size, number, and cargo during clathrin-mediated endocytosis, PLoS Biol, vol.11, p.1001670, 2013.

B. Ritter, J. Philie, M. Girard, E. C. Tung, F. Blondeau et al., Identification of a family of endocytic proteins that define a new ?-adaptin earbinding motif, EMBO Rep, vol.4, pp.1089-1093, 2003.

M. G. Rittig, J. C. Jagoda, B. Wilske, R. Murgia, M. Cinco et al., Coiling phagocytosis discriminates between different spirochetes and is enhanced by phorbol myristate acetate and granulocytemacrophage colony-stimulating factor, Infect Immun, vol.66, pp.627-662, 1998.

T. Y. Riyahi, F. Frese, M. Steinert, N. N. Omosigho, G. Glöckner et al., RpkA, a highly conserved GPCR with a lipid kinase domain, has a role in phagocytosis and anti-bacterial defense, PLoS One, vol.6, p.27311, 2011.

F. G. Rodgers and F. C. Gibson, Opsonin-independent adherence and intracellular development of Legionella pneumophila within U-937 cells, Can J Microbiol, vol.39, pp.718-722, 1993.

F. G. Rodgers, P. W. Greaves, A. D. Macrae, and M. J. Lewis, Electron microscopic evidence of flagella and pili on Legionella pneumophila, J Clin Pathol, vol.33, pp.1184-1188, 1980.

S. Rodríguez-zaragoza, Ecology of free-living amoebae, Crit Rev Microbiol, vol.20, pp.225-241, 1994.

M. Rolando, L. Gomez-valero, and C. Buchrieser, Bacterial remodelling of the host epigenome: Functional role and evolution of effectors methylating host histones, Cell Microbiol, vol.17, pp.1098-1107, 2015.
URL : https://hal.archives-ouvertes.fr/pasteur-01326517

O. Rossier and N. P. Cianciotto, Type II protein secretion is a subset of the pilDdependent processes that facilitate intracellular infection by Legionella pneumophila, Infect Immun, vol.69, pp.2092-2098, 2001.

O. Rossier, J. Dao, and N. P. Cianciotto, A type II secreted RNase of Legionella pneumophila facilitates optimal intracellular infection of Hartmannella vermiformis, Microbiology, vol.155, pp.882-890, 2009.

O. Rossier, S. R. Starkenburg, and N. P. Cianciotto, Legionella pneumophila type II protein secretion promotes virulence in the A/J mouse model of Legionnaires' disease pneumonia, Infect Immun, vol.72, pp.310-321, 2004.

T. J. Rowbotham, Preliminary report on the pathogenicity of Legionella pneumophila for freshwater and soil amoebae, J Clin Pathol, vol.33, pp.1179-1183, 1980.

R. W. Rubin, M. C. Hill, P. Hepworth, and J. Boehmer, Isolation and electrophoretic analysis of nucleoli, phenol-soluble nuclear proteins, and outer cyst walls from Acanthamoeba castellanii during encystation initiation, J Cell Biol, vol.68, pp.740-751, 1976.

A. Salameh, N. Bello, J. Becker, and T. Zangeneh, Fatal granulomatous amoebic encephalitis caused by Acanthamoeba in a patient with kidney transplant: A case report, Open Forum Infect Dis, vol.2, p.104, 2015.

A. Samba-louaka, V. Delafont, M. Rodier, E. Cateau, and Y. Héchard, Free-living amoebae and squatters in the wild: ecological and molecular features, FEMS Microbiol Rev, vol.43, pp.415-434, 2019.

J. Samuelson, G. G. Bushkin, A. Chatterjee, and P. W. Robbins, Strategies to discover the structural components of cyst and oocyst walls, Eukaryot Cell, vol.12, pp.1578-1587, 2013.

G. Sandström, A. Saeed, and H. Abd, Acanthamoeba-bacteria: a model to study host interaction with human pathogens, Curr Drug Targets, vol.12, pp.936-977, 2011.

T. K. Sawyer, Acanthamoeba griffini, a new species of marine amoeba, J Protozool, vol.18, pp.650-654, 1971.

R. A. Scheltema, J. P. Hauschild, O. Lange, D. Hornburg, E. Denisov et al., The Q exactive HF, a benchtop mass spectrometer with a pre-filter, high-performance quadrupole and an ultra-high-field orbitrap analyzer, Mol Cell Proteomics, vol.13, pp.3698-3708, 2014.

L. Schmarda, , 1871.

J. Schmölders, C. Manske, A. Otto, C. Hoffmann, B. Steiner et al., Comparative proteomics of purified pathogen vacuoles correlates intracellular replication of Legionella pneumophila with the small GTPase rasrelated protein 1 (Rap1), Mol Cell Proteomics, vol.16, pp.622-641, 2017.

J. M. Schroeder, G. C. Booton, J. Hay, I. A. Niszl, D. V. Seal et al., Use of subgenic 18S ribosomal DNA PCR and sequencing for genus and genotype identification of Acanthamoebae from humans with keratitis and from sewage sludge, J Clin Microbiol, vol.39, pp.1903-1911, 2001.

M. K. Schuhmacher, M. Rolando, A. Bröhm, S. Weirich, S. Kudithipudi et al., The Legionella pneumophila methyltransferase RomA methylates also non-histone Proteins during Infection, J Mol Biol, vol.430, pp.1912-1925, 2018.

L. Scola, B. Audic, S. Robert, C. Jungang, L. De-lamballerie et al., A giant virus in amoebae, Science, vol.80, p.2033, 2003.

L. L. Shadwick, M. W. Brown, A. K. Tice, and F. W. Spiegel, A new amoeba with protosteloid fruiting: Luapeleamoeba hula n. g. n. sp. (Acanthamoebidae, Centramoebida, Amoebozoa), Acta Protozool, vol.55, pp.123-134, 2016.

L. L. Shadwick, F. W. Spiegel, J. Shadwick, M. W. Brown, and J. D. Silberman, Eumycetozoa = Amoebozoa?: SSUrDNA phylogeny of protosteloid slime molds and its significance for the amoebozoan supergroup, PLoS One, vol.4, p.6754, 2009.

X. Shen, S. Banga, Y. Liu, L. Xu, P. Gao et al., Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response, Cell Microbiol, vol.11, pp.911-926, 2009.

S. Shin, Innate immunity to intracellular pathogens. Lessons learned from Legionella pneumophila, Advances in Applied Microbiology, pp.43-71, 2012.

S. Shin, C. L. Case, K. A. Archer, C. V. Nogueira, K. S. Kobayashi et al., Type IV secretion-dependent activation of host MAP kinases induces an increased proinflammatory cytokine response to Legionella pneumophila, PLoS Pathog, vol.4, p.1000220, 2008.

R. Siddiqui and N. A. Khan, Biology and pathogenesis of Acanthamoeba, vol.5, p.6, 2012.

A. V. Smirnov, E. Chao, E. S. Nassonova, and T. Cavalier-smith, A revised classification of naked Lobose amoebae (Amoebozoa: Lobosa), Protist, vol.162, pp.545-570, 2011.

A. Sol, E. Lipo, D. A. De-jesús-díaz, C. Murphy, M. Devereux et al., Legionella pneumophila translocated translation inhibitors are required for bacterial-induced host cell cycle arrest, Proc Natl Acad Sci, vol.116, pp.3221-3228, 2019.

S. M. Song, B. I. Han, E. K. Moon, Y. R. Lee, H. S. Yu et al., Autophagy protein 16-mediated autophagy is required for the encystation of Acanthamoeba castellanii, Mol Biochem Parasitol, vol.183, pp.158-165, 2012.

T. W. Steele, C. Moore, and N. Sangster, Distribution of Legionella longbeachae serogroup 1 and other legionellae in potting soils in Australia, Appl Environ Microbiol, vol.56, pp.2984-2992, 1990.

J. N. Steenbergen and A. Casadevall, The origin and maintenance of virulence for the human pathogenic fungus Cryptococcus neoformans, Microbes Infect, vol.5, pp.667-675, 2003.

J. N. Steenbergen, H. A. Shuman, and A. Casadevall, Cryptococcus neoformans interactions with amoebae suggest an explanation for its virulence and intracellular pathogenic strategy in macrophages, Proc Natl Acad Sci, vol.98, pp.15245-15250, 2001.

B. Steiner, A. L. Swart, A. Welin, S. Weber, N. Personnic et al., ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila, EMBO Rep, vol.18, pp.1817-1836, 2017.

B. Steiner, S. Weber, and H. Hilbi, Formation of the Legionella-containing vacuole: phosphoinositide conversion, GTPase modulation and ER dynamics, Int J Med Microbiol, vol.308, pp.49-57, 2018.

B. Steiner, S. Weber, A. Kaech, U. Ziegler, and H. Hilbi, The large GTPase atlastin controls ER remodeling around a pathogen vacuole, Commun Integr Biol, vol.11, pp.1-5, 2018.

M. Steinert, L. Emödy, R. Amann, and J. Hacker, Resuscitation of viable but nonculturable Legionella pneumophila Philadelphia JR32 by Acanthamoeba castellanii, Appl Environ Microbiol, vol.63, pp.2047-53, 1997.

H. Stenmark, Rab GTPases as coordinators of vesicle traffic, Nat Rev Mol Cell Biol, vol.10, pp.513-525, 2009.

J. R. Stewart and R. A. Weisman, A chemical and autoradiographic study of cellulose synthesis during the encystment of Acanthamoeba castellanii, Arch Biochem Biophys, vol.161, pp.488-498, 1974.

M. Watarai, I. Derre, J. Kirby, J. D. Growney, W. F. Dietrich et al., Legionella pneumophila is internalized by a macropinocytotic uptake pathway controlled by the Dot/Icm system and the mouse Lgn1 locus, J Exp Med, vol.194, pp.1081-1095, 2001.

M. M. Weber and R. Faris, Subversion of the endocytic and secretory pathways by bacterial effector proteins, Front Cell Dev Biol, vol.6, p.1, 2018.

S. S. Weber, C. Ragaz, and H. Hilbi, The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE, Cell Microbiol, vol.11, pp.442-460, 2009.

R. A. Weisman, Differentiation in Acanthamoeba castellanii, Annu Rev Microbiol, vol.30, pp.189-219, 1976.

R. A. Weisman, R. S. Spiegel, and J. G. Mccauley, Differentiation in Acanthamoeba: Glycogen levels and glycogen synthetase activity during encystment, BBA -Gen Subj, vol.201, pp.45-53, 1970.

J. E. Weldon and I. Pastan, A guide to taming a toxin -Recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer, FEBS J, vol.278, pp.4683-4700, 2011.

K. Wennerberg, K. L. Rossman, and C. J. Der, The Ras superfamily at a glance, J Cell Sci, vol.118, pp.843-846, 2005.

R. C. White, F. F. Gunderson, J. Y. Tyson, K. H. Richardson, T. J. Portlock et al., Type II secretion-dependent aminopeptidase lapa and acyltransferase plac are redundant for nutrient acquisition during Legionella pneumophila intracellular infection of amoebas, Cianciotto NP, vol.9, pp.528-546, 2018.

E. S. Wittchen, A. Aghajanian, and K. Burridge, Isoform-specific differences between Rap1A and Rap1B GTPases in the formation of endothelial cell junctions, Small GTPases, vol.2, pp.65-76, 2011.

A. Wittrup and J. Lieberman, Knocking down disease: A progress report on siRNA therapeutics, Nat Rev Genet, vol.16, pp.543-552, 2015.

L. Xu, X. Shen, A. Bryan, S. Banga, M. S. Swanson et al., Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector, PLoS Pathog, vol.6, p.1000822, 2010.

U. Zähringer, Y. A. Knirel, B. Lindner, J. H. Helbig, A. Sonesson et al., The lipopolysaccharide of Legionella pneumophila serogroup 1 (strain Philadelphia 1): chemical structure and biological significance, Prog Clin Biol Res, vol.392, pp.113-152, 1995.

W. Zhu, S. Banga, Y. Tan, C. Zheng, R. Stephenson et al., Comprehensive identification of protein substrates of the Dot/Icm type IV transporter of Legionella pneumophila, PLoS One, vol.6, p.17638, 2011.

G. K. Zorzi, R. S. Schuh, V. J. Maschio, N. T. Brazil, M. B. Rott et al., Box Behnken design of siRNA-loaded liposomes for the treatment of a murine model of ocular keratitis caused by Acanthamoeba, Colloids Surfaces B Biointerfaces, vol.173, pp.725-732, 2019.

T. Zusman, G. Yerushalmi, and G. Segal, Functional similarities between the Icm/Dot pathogenesis systems of Coxiella burnetii and Legionella pneumophila, Infect Immun, vol.71, pp.3714-3723, 2003.

, Annexe 4 : Protéines dont le taux est diminué après 48 h d'infection d'A

L. Castellanii-neff-par and . Paris, Les protéines surlignées en jaune correspondent aux protéines étudiées durant les travaux de thèse

, ACA1_063250 MYND finger domain containing protein, vol.4, pp.47-50

, ACA1_182950 Farnesyl pyrophosphate synthetase, vol.4, pp.38-40

. Mengue, Annexe 6 : Legionella pneumophila decreases velocity of Acanthamoeba castellanii, 2017.