K. L. Kotloff, J. P. Winickoff, B. Ivanoff, J. D. Clemens, D. L. Swerdlow et al., Global burden of Shigella infections: implications for vaccine development and implementation of control strategies, Bull. World Health Organ, p.77, 1999.

C. Parsot, Shigella type III secretion effectors: how, where, when, for what purposes?, Current Opinion in Microbiology, vol.12, issue.1, pp.110-116, 2009.
DOI : 10.1016/j.mib.2008.12.002

J. Humann and L. L. Lenz, Bacterial Peptidoglycan-Degrading Enzymes and Their Impact on Host Muropeptide Detection, Journal of Innate Immunity, vol.1, issue.2, pp.88-97, 2009.
DOI : 10.1159/000181181

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2659621

E. M. Prager and P. Jolles, Animal lysozymes c and g: An overview, EXS, vol.75, pp.9-31, 1996.
DOI : 10.1007/978-3-0348-9225-4_2

P. Jolles, J. Jolles, S. E. Girardin, R. Tournebize, M. Mavris et al., What's new in lysozyme research? Always a model system, today as yesterday, CARD4/Nod1 mediates NF-kappaB and JNK activation by invasive Shigella flexneri, EMBO Rep, pp.165-189, 1984.

D. J. Philpott and S. E. Girardin, The role of Toll-like receptors and Nod proteins in bacterial infection, Molecular Immunology, vol.41, issue.11, p.41, 2004.
DOI : 10.1016/j.molimm.2004.06.012

G. H. Lowell, R. P. Macdermott, P. L. Summers, A. A. Reeder, M. J. Bertovich et al., Antibody-dependent cell-mediated antibacterial activity: K lymphocytes, monocytes, and granulocytes are effective against Shigella, J. Immunol, pp.125-2778, 1980.

Y. Weinrauch, D. Drujan, S. D. Shapiro, J. Weiss, and A. Zychlinsky, Neutrophil elastase targets virulence factors of enterobacteria, Nature, vol.61, issue.6884, pp.91-94, 2002.
DOI : 10.1038/417091a

W. Bellamy, M. Takase, H. Wakabayashi, K. Kawase, and M. Tomita, -terminal region of bovine lactoferrin, Journal of Applied Bacteriology, vol.86, issue.6, pp.73-472, 1992.
DOI : 10.1111/j.1365-2672.1992.tb05007.x

URL : https://hal.archives-ouvertes.fr/halshs-01408054

W. R. Bellamy, H. Wakabayashi, M. Takase, K. Kawase, S. Shimamura et al., Role of cell-binding in the antibacterial mechanism of lactoferricin B, J. Appl. Bacteriol, pp.75-478, 1993.

L. Callewaert, K. G. Vanoirbeek, I. Lurquin, C. W. Michiels, and A. Aertsen, The Rcs Two-Component System Regulates Expression of Lysozyme Inhibitors and Is Induced by Exposure to Lysozyme, Journal of Bacteriology, vol.191, issue.6, p.191, 2009.
DOI : 10.1128/JB.01549-08

S. Yum, M. J. Kim, Y. Xu, X. L. Jin, H. Y. Yoo et al., Structural basis for the recognition of lysozyme by MliC, a periplasmic lysozyme inhibitor in Gram-negative bacteria, Biochemical and Biophysical Research Communications, vol.378, issue.2, pp.378-244, 2009.
DOI : 10.1016/j.bbrc.2008.11.039

I. G. Boneca, O. Dussurget, D. Cabanes, M. A. Nahori, S. Sousa et al., A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system, Proc. Natl. Acad. Sci. U S A, pp.997-1002, 2007.
URL : https://hal.archives-ouvertes.fr/pasteur-00139188

G. Wang, A. Olczak, L. S. Forsberg, and R. J. Maier, Oxidative Stress-induced Peptidoglycan Deacetylase in Helicobacter pylori, Journal of Biological Chemistry, vol.284, issue.11, pp.284-6790, 2009.
DOI : 10.1074/jbc.M808071200

G. Wang, S. E. Maier, L. F. Lo, G. Maier, S. Dosi et al., Peptidoglycan Deacetylation in Helicobacter pylori Contributes to Bacterial Survival by Mitigating Host Immune Responses, Infection and Immunity, vol.78, issue.11, pp.78-4660, 2010.
DOI : 10.1128/IAI.00307-10

D. E. Blair, A. W. Schuttelkopf, J. I. Macrae, and D. M. Van-aalten, Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor, Proceedings of the National Academy of Sciences, vol.102, issue.43, pp.15429-15434, 2005.
DOI : 10.1073/pnas.0504339102

K. M. Davis, H. T. Akinbi, A. J. Standish, and J. N. Weiser, Resistance to Mucosal Lysozyme Compensates for the Fitness Deficit of Peptidoglycan Modifications by Streptococcus pneumoniae, PLoS Pathogens, vol.1, issue.12, p.1000241, 2008.
DOI : 10.1371/journal.ppat.1000241.t001

D. E. Blair and D. M. Van-aalten, -acetyl-glucosamine, FEBS Letters, vol.11, issue.1-3, pp.13-19, 2004.
DOI : 10.1016/j.febslet.2004.06.013

URL : https://hal.archives-ouvertes.fr/inria-00459156

S. R. Goldman, Y. Tu, and M. B. Goldberg, Differential Regulation by Magnesium of the Two MsbB Paralogs of Shigella flexneri, Journal of Bacteriology, vol.190, issue.10, pp.190-3526, 2008.
DOI : 10.1128/JB.00151-08

A. Allaoui, P. J. Sansonetti, and C. Parsot, MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is homologous to YscJ, a secretion factor of the Yersinia Yop proteins., Journal of Bacteriology, vol.174, issue.23, pp.174-7661, 1992.
DOI : 10.1128/jb.174.23.7661-7669.1992

G. Demarre, A. M. Guerout, C. Matsumoto-mashimo, D. A. Rowe-magnus, P. Marliere et al., A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncP??) conjugative machineries and their cognate Escherichia coli host strains, Research in Microbiology, vol.156, issue.2, pp.245-255, 2005.
DOI : 10.1016/j.resmic.2004.09.007

R. Menard, P. J. Sansonetti, and C. Parsot, Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells., Journal of Bacteriology, vol.175, issue.18, pp.175-5899, 1993.
DOI : 10.1128/jb.175.18.5899-5906.1993

M. Popowska, M. Kusio, P. Szymanska, and Z. Markiewicz, Inactivation of the Wall-Associated De-N-acetylase (PgdA) of Listeria monocytogenes Results in Greater Susceptibility of the Cells to Induced Autolysis, Journal of Microbiology and Biotechnology, vol.19, issue.9, pp.932-945, 2009.
DOI : 10.4014/jmb.0810.557

J. F. Pycock, W. E. Allen, and T. H. Morris, Rapid, single-step isolation of equine neutrophils on a discontinuous Percoll density gradient, Res. Vet. Sci, pp.42-411, 1987.

R. S. Rosenthal and R. Dziarski, [20] Isolation of peptidoglycan and soluble peptidoglycan fragments, Methods Enzymol, vol.235, pp.253-285, 1994.
DOI : 10.1016/0076-6879(94)35146-5

C. Buchrieser, P. Glaser, C. Rusniok, H. Nedjari, H. D-'hauteville et al., The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri, Molecular Microbiology, vol.11, issue.4, pp.38-760, 2000.
DOI : 10.1038/358167a0

F. Caufrier, A. Martinou, C. Dupont, and V. Bouriotis, Carbohydrate esterase family 4 enzymes: substrate specificity, Carbohydrate Research, vol.338, issue.7, pp.687-692, 2003.
DOI : 10.1016/S0008-6215(03)00002-8

N. K. Bui, S. Turk, S. Buckenmaier, F. Stevenson-jones, B. Zeuch et al., Vollmer, Development of screening assays and discovery of initial inhibitors of pneumococcal peptidoglycan deacetylase PgdA, Biochem. Pharmacol, pp.82-125, 2011.

B. Masschalck, R. Van-houdt, and C. W. Michiels, High pressure increases bactericidal activity and spectrum of lactoferrin, lactoferricin and nisin, International Journal of Food Microbiology, vol.64, issue.3, pp.325-332, 2001.
DOI : 10.1016/S0168-1605(00)00485-2

B. Masschalck, R. Van-houdt, E. G. Van-haver, and C. W. Michiels, Inactivation of Gram-Negative Bacteria by Lysozyme, Denatured Lysozyme, and Lysozyme-Derived Peptides under High Hydrostatic Pressure, Applied and Environmental Microbiology, vol.67, issue.1, pp.67-339, 2001.
DOI : 10.1128/AEM.67.1.339-344.2001

S. C. Roy, V. K. Singh, and T. More, Electrophoretic detection of myeloperoxidase , protease, lactoferrin and lysozyme in buffalo polymorphonuclear granular acid extracts, Veterinary Research Communications, vol.21, issue.5, pp.325-334, 1997.
DOI : 10.1023/A:1005808203623

J. E. Moss, P. E. Fisher, B. Vick, E. A. Groisman, and A. Zychlinsky, The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella flexneri, Cellular Microbiology, vol.100, issue.6, pp.443-452, 2000.
DOI : 10.1016/S0966-842X(97)01044-5

A. Phalipon and P. J. Sansonetti, Shigella???s ways of manipulating the host intestinal innate and adaptive immune system: a tool box for survival?, Immunology and Cell Biology, vol.3, issue.2, pp.85-119, 2007.
DOI : 10.1038/sj.icb7100025

C. J. Czuprynski, P. A. Campbell, and P. M. Henson, Killing of Listeria monocytogenes by human neutrophils and monocytes, but not by monocytederived macrophages, J. Reticuloendothel. Soc, pp.34-63, 1983.

C. J. Czuprynski, P. M. Henson, and P. A. Campbell, Killing of Listeria monocytogenes by inflammatory neutrophils and mononuclear phagocytes from immune and nonimmune mice, J. Leukoc. Biol, p.35, 1984.

I. Mandic-mulec, J. Weiss, and A. Zychlinsky, Shigella flexneri is trapped in polymorphonuclear leukocyte vacuoles and efficiently killed, Infect. Immun, pp.65-110, 1997.

A. Bera, S. Herbert, A. Jakob, W. Vollmer, and F. Gotz, Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus, Molecular Microbiology, vol.68, issue.3, pp.55-778, 2005.
DOI : 10.1111/j.1365-2958.2004.04446.x

L. Hebert, P. Courtin, R. Torelli, M. Sanguinetti, M. P. Chapot-chartier et al., Enterococcus faecalis Constitutes an Unusual Bacterial Model in Lysozyme Resistance, Infection and Immunity, vol.75, issue.11, pp.75-5390, 2007.
DOI : 10.1128/IAI.00571-07

W. Vollmer and A. Tomasz, The pgdA gene encodes for a peptidoglycan Nacetylglucosamine deacetylase in Streptococcus pneumoniae, J. Biol. Chem, p.275, 2000.

E. Psylinakis, I. G. Boneca, K. Mavromatis, A. Deli, E. Hayhurst et al., Bouriotis, Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis, J. Biol. Chem, vol.280, 2005.

M. Meyrand, A. Boughammoura, P. Courtin, C. Mezange, A. Guillot et al., Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis, Microbiology, vol.153, issue.10, pp.3275-3285, 2007.
DOI : 10.1099/mic.0.2007/005835-0

J. P. Dillard and K. T. Hackett, Mutations Affecting Peptidoglycan Acetylation in Neisseria gonorrhoeae and Neisseria meningitidis, Infection and Immunity, vol.73, issue.9, pp.73-5697, 2005.
DOI : 10.1128/IAI.73.9.5697-5705.2005

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1231103

W. Vollmer and A. , Peptidoglycan N-Acetylglucosamine Deacetylase, a Putative Virulence Factor in Streptococcus pneumoniae, Infection and Immunity, vol.70, issue.12, pp.7176-7178, 2002.
DOI : 10.1128/IAI.70.12.7176-7178.2002

G. Nigro, L. L. Fazio, M. C. Martino, G. Rossi, I. Tattoli et al., Muramylpeptide shedding modulates cell sensing of Shigella flexneri, Cellular Microbiology, vol.66, issue.3, pp.682-695, 2008.
DOI : 10.1016/0167-7012(90)90056-C