R. Figueira and D. W. Holden, Functions of the Salmonella pathogenicity island 2 (SPI-2) type III secretion system effectors, Microbiology, vol.158, issue.Pt_5, pp.1147-1161, 2012.
DOI : 10.1099/mic.0.058115-0

M. A. Stein, K. Y. Leung, M. Zwick, F. Garciadelportillo, and B. B. Finlay, Identification of a Salmonella virulence gene required for formation of filamentous structures containing lysosomal membrane glycoproteins within epithelial cells, Molecular Microbiology, vol.17, issue.1, pp.151-164, 1996.
DOI : 10.1016/0378-1119(85)90120-9

C. R. Beuzón, Salmonella maintains the integrity of its intracellular vacuole through the action of SifA, The EMBO Journal, vol.19, issue.13, pp.3235-3249, 2000.
DOI : 10.1093/emboj/19.13.3235

G. Portillo, F. Zwick, M. B. Leung, K. Y. Finlay, and B. B. , Salmonella induces the formation of filamentous structures containing lysosomal membrane glycoproteins in epithelial cells, Proc. Natl. Acad. Sci. USA 90, pp.10544-10548, 1993.

L. J. Mota, A. E. Ramsden, M. Liu, J. D. Castle, and D. W. Holden, -induced tubular network and reveals an interaction between bacterial effectors and post-Golgi trafficking, Cellular Microbiology, vol.110, issue.Pt 13, pp.1236-1253, 2009.
DOI : 10.1111/j.1462-5822.2009.01329.x
URL : https://hal.archives-ouvertes.fr/hal-00707780

N. Schroeder, The Virulence Protein SopD2 Regulates Membrane Dynamics of Salmonella-Containing Vacuoles, PLoS Pathogens, vol.277, issue.7, p.1001002, 2010.
DOI : 10.1371/journal.ppat.1001002.t004
URL : https://hal.archives-ouvertes.fr/hal-00610105

V. Krieger and D. Liebl, Reorganization of the Endosomal System in Salmonella-Infected Cells: The Ultrastructure of Salmonella-Induced Tubular Compartments, PLoS Pathogens, vol.19, issue.9, p.1004374, 2014.
DOI : 10.1371/journal.ppat.1004374.s031

E. A. Miao and S. I. Miller, A conserved amino acid sequence directing intracellular type III secretion by Salmonella typhimurium, Proc. Natl. Acad. Sci. USA 97, pp.7539-7544, 2000.
DOI : 10.1073/pnas.97.13.7539

S. Méresse, Is host lipidation of pathogen effector proteins a general virulence mechanism? Front, Microbiol, vol.2, p.73, 2011.

A. T. Reinicke, A Salmonella typhimurium Effector Protein SifA Is Modified by Host Cell Prenylation and S-Acylation Machinery, Journal of Biological Chemistry, vol.280, issue.15, pp.14620-14627, 2005.
DOI : 10.1074/jbc.M500076200

E. Boucrot, C. R. Beuzón, D. W. Holden, J. Gorvel, and S. Méresse, Salmonella typhimurium SifA Effector Protein Requires Its Membrane-anchoring C-terminal Hexapeptide for Its Biological Function, Journal of Biological Chemistry, vol.278, issue.16, pp.14196-14202, 2003.
DOI : 10.1074/jbc.M207901200

M. B. Ohlson, Structure and Function of Salmonella SifA Indicate that Its Interactions with SKIP, SseJ, and RhoA Family GTPases Induce Endosomal Tubulation, Cell Host & Microbe, vol.4, issue.5, pp.434-446, 2008.
DOI : 10.1016/j.chom.2008.08.012

L. Diacovich, Interaction between the SifA Virulence Factor and Its Host Target SKIP Is Essential for Salmonella Pathogenesis, Journal of Biological Chemistry, vol.284, issue.48, pp.33151-33160, 2009.
DOI : 10.1074/jbc.M109.034975
URL : https://hal.archives-ouvertes.fr/hal-00431846

C. V. Srikanth, Salmonella Pathogenesis and Processing of Secreted Effectors by Caspase-3, Science, vol.330, issue.6002, pp.390-393, 2010.
DOI : 10.1126/science.1194598

E. Boucrot, T. Henry, J. Borg, J. Gorvel, and S. Méresse, 12979 | DOi: 10.1038/srep12979 16 The intracellular fate of Salmonella depends on the recruitment of kinesin, Science, vol.5, issue.308, pp.1174-1178, 2005.

A. Dumont, SKIP, the Host Target of the Salmonella Virulence Factor SifA, Promotes Kinesin-1-Dependent Vacuolar Membrane Exchanges, Traffic, vol.552, issue.7, pp.899-911, 2010.
DOI : 10.1111/j.1600-0854.2010.01069.x
URL : https://hal.archives-ouvertes.fr/hal-00503009

D. G. Mcewan, PLEKHM1 Regulates Salmonella-Containing Vacuole Biogenesis and Infection, Cell Host & Microbe, vol.17, issue.1, pp.58-71, 2015.
DOI : 10.1016/j.chom.2014.11.011

S. Pernigo, A. Lamprecht, R. A. Steiner, and M. P. Dodding, Structural Basis for Kinesin-1:Cargo Recognition, Science, vol.340, issue.6130, pp.356-359, 2013.
DOI : 10.1126/science.1234264

T. Henry, The Salmonella effector protein PipB2 is a linker for kinesin-1, Proc. Natl. Acad. Sci. USA 103, pp.13497-13502, 2006.
DOI : 10.1073/pnas.0605443103
URL : https://hal.archives-ouvertes.fr/hal-00165593

A. Arbeloa, EspM2 is a RhoA guanine nucleotide exchange factor, Cellular Microbiology, vol.1164, issue.5, pp.654-664, 2010.
DOI : 10.1111/j.1462-5822.2009.01423.x

J. K. White, Genome-wide Generation and Systematic Phenotyping of Knockout Mice Reveals New Roles for Many Genes, Cell, vol.154, issue.2, pp.452-464, 2013.
DOI : 10.1016/j.cell.2013.06.022

W. Trust and S. Institute, WTSI Mouse Resources portal. http://www.sanger.ac.uk/mouseportal/search?query= plekhm2 Date of access, 2015.

C. R. Beuzón and D. W. Holden, Use of mixed infections with Salmonella strains to study virulence genes and their interactions in vivo, Microbes and Infection, vol.3, issue.14-15, pp.1345-1352, 2001.
DOI : 10.1016/S1286-4579(01)01496-4

. Hensel, pathogenicity island 2 are required for bacterial virulence and proliferation in macrophages, Molecular Microbiology, vol.63, issue.1, pp.163-174, 1998.
DOI : 10.1046/j.1365-2958.1998.01047.x

N. F. Brown, Mutational analysis of Salmonella translocated effector members SifA and SopD2 reveals domains implicated in translocation, subcellular localization and function, Microbiology, vol.152, issue.8, pp.2323-2343, 2006.
DOI : 10.1099/mic.0.28995-0

P. Nawabi, D. M. Catron, and K. Haldar, Esterification of cholesterol by a type III secretion effector during intracellular Salmonella infection, Molecular Microbiology, vol.473, issue.1, pp.173-185, 2008.
DOI : 10.1128/IAI.71.1.1-12.2003

M. Christen, Activation of a Bacterial Virulence Protein by the GTPase RhoA, Science Signaling, vol.2, issue.95, p.71, 2009.
DOI : 10.1126/scisignal.2000430

M. B. Ohlson, K. Fluhr, C. L. Birmingham, J. H. Brumell, and S. I. Miller, SseJ Deacylase Activity by Salmonella enterica Serovar Typhimurium Promotes Virulence in Mice, Infection and Immunity, vol.73, issue.10, pp.6249-6259, 2005.
DOI : 10.1128/IAI.73.10.6249-6259.2005

C. R. Beuzón, S. P. Salcedo, and D. W. Holden, Growth and killing of a Salmonella enterica serovar Typhimurium sifA mutant strain in the cytosol of different host cell lines, Microbiology, vol.148, issue.9, pp.2705-2715, 2002.
DOI : 10.1099/00221287-148-9-2705

L. K. Jackson, P. Nawabi, C. Hentea, E. A. Roark, and K. Haldar, The Salmonella virulence protein SifA is a G protein antagonist, Proc. Natl. Acad. Sci. USA 105, pp.14141-14146, 2008.
DOI : 10.1073/pnas.0801872105

K. Mcgourty, Salmonella Inhibits Retrograde Trafficking of Mannose-6-Phosphate Receptors and Lysosome Function, Science, vol.338, issue.6109, pp.963-967, 2012.
DOI : 10.1126/science.1227037

A. Dumont, N. Schroeder, J. Gorvel, and S. Méresse, Analysis of Kinesin Accumulation on Salmonella-Containing Vacuoles, Methods Mol. Biol, vol.394, pp.275-287, 2007.
DOI : 10.1007/978-1-59745-512-1_13

X. Yu, K. Mcgourty, M. Liu, K. E. Unsworth, and D. W. Holden, pH Sensing by Intracellular Salmonella Induces Effector Translocation, Science, vol.328, issue.5981, pp.1040-1043, 2010.
DOI : 10.1126/science.1189000

M. Ansaldi, M. Lepelletier, and V. Méjean, Site-Specific Mutagenesis by Using an Accurate Recombinant Polymerase Chain Reaction Method, Analytical Biochemistry, vol.234, issue.1, pp.110-111, 1996.
DOI : 10.1006/abio.1996.0060

K. A. Datsenko and B. L. Wanner, One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products, Proc. Natl. Acad. Sci. USA 97, pp.6640-6645, 2000.
DOI : 10.1073/pnas.120163297

W. Zhao and S. Méresse, A Method to Introduce an Internal Tag Sequence into a Salmonella Chromosomal Gene, Methods Mol. Biol, vol.1225, pp.81-92, 2015.
DOI : 10.1007/978-1-4939-1625-2_5

J. E. Shea, C. R. Beuzón, C. Gleeson, R. Mundy, and D. W. Holden, Influence of the Salmonella typhimurium pathogenicity island 2 type III secretion system on bacterial growth in the mouse, Infect. Immun, vol.67, pp.213-219, 1999.