D. De-biase and E. Pennacchietti, operon, Molecular Microbiology, vol.70, issue.Suppl. 6, pp.770-786, 2012.
DOI : 10.1111/mmi.12020
URL : https://hal.archives-ouvertes.fr/pasteur-00952127

P. Lund, A. Tramonti, D. Biase, and D. , Coping with low pH: molecular strategies in neutralophilic bacteria, FEMS Microbiology Reviews, vol.38, issue.6, pp.1091-1125, 2014.
DOI : 10.1111/1574-6976.12076
URL : https://hal.archives-ouvertes.fr/pasteur-01180153

M. F. Tsai, P. Mccarthy, and C. Miller, Substrate selectivity in glutamate-dependent acid resistance in enteric bacteria, Proceedings of the National Academy of Sciences, vol.110, issue.15, pp.5898-5902, 2013.
DOI : 10.1073/pnas.1301444110

D. Ma, P. Lu, and Y. Shi, Substrate Selectivity of the Acid-activated Glutamate/??-Aminobutyric acid (GABA) Antiporter GadC from Escherichia coli, Journal of Biological Chemistry, vol.288, issue.21, pp.15148-15153, 2013.
DOI : 10.1074/jbc.M113.474502

H. Gut, E. Pennacchietti, R. A. John, F. Bossa, G. Capitani et al., Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB, The EMBO Journal, vol.14, issue.11, pp.2643-2651, 2006.
DOI : 10.1038/sj.emboj.7601107

D. Ma, P. Lu, C. Yan, C. Fan, P. Yin et al., Structure and mechanism of a glutamate???GABA antiporter, Nature, vol.31, issue.7391, pp.632-636, 2012.
DOI : 10.1074/jbc.274.47.33244

H. C. Scholz, Z. Hubalek, I. Sedlacek, G. Vergnaud, H. Tomaso et al., Brucella microti sp. nov., isolated from the common vole Microtus arvalis, Brucella microti sp. nov., isolated from the common vole Microtus arvalis, pp.375-382, 2008.
DOI : 10.1099/ijs.0.65356-0
URL : https://hal.archives-ouvertes.fr/hal-00220401

H. C. Scholz, E. Hofer, G. Vergnaud, P. Le-fleche, A. M. Whatmore et al., , in Lower Austria, Vector-Borne and Zoonotic Diseases, vol.9, issue.2, pp.153-156, 2009.
DOI : 10.1089/vbz.2008.0036

H. C. Scholz, Z. Hubalek, J. Nesvadbova, H. Tomaso, G. Vergnaud et al., from Soil, Emerging Infectious Diseases, vol.14, issue.8, pp.1316-1317, 2008.
DOI : 10.3201/eid1408.080286
URL : https://hal.archives-ouvertes.fr/hal-00356292

T. Eisenberg, H. P. Hamann, U. Kaim, K. Schlez, H. Seeger et al., Isolation of Potentially Novel Brucella spp. from Frogs, Applied and Environmental Microbiology, vol.78, issue.10, pp.3753-3755, 2012.
DOI : 10.1128/AEM.07509-11

R. V. Tiller, J. E. Gee, D. R. Lonsway, S. Gribble, S. C. Bell et al., Identification of an unusual Brucella strain (BO2) from a lung biopsy in a 52 year-old patient with chronic destructive pneumonia, BMC Microbiology, vol.10, issue.1, p.23, 2010.
DOI : 10.1186/1471-2180-10-23

H. C. Scholz, K. Nockler, C. Gollner, P. Bahn, G. Vergnaud et al., Brucella inopinata sp. nov., isolated from a breast implant infection, INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY, vol.60, issue.4, pp.801-808, 2010.
DOI : 10.1099/ijs.0.011148-0
URL : https://hal.archives-ouvertes.fr/hal-01160732

A. Occhialini, M. P. Jimenez-de-bagues, B. Saadeh, D. Bastianelli, N. Hanna et al., The Glutamic Acid Decarboxylase System of the New Species Brucella microti Contributes to Its Acid Resistance and to Oral Infection of Mice, Journal of Infectious Diseases, vol.206, issue.9, pp.1424-1432, 2012.
DOI : 10.1093/infdis/jis522
URL : https://hal.archives-ouvertes.fr/pasteur-00952116

M. A. Damiano, D. Bastianelli, A. Dahouk, S. Kohler, S. Cloeckaert et al., Glutamate Decarboxylase-Dependent Acid Resistance in Brucella spp.: Distribution and Contribution to Fitness under Extremely Acidic Conditions, Applied and Environmental Microbiology, vol.81, issue.2, pp.578-586, 2015.
DOI : 10.1128/AEM.02928-14
URL : https://hal.archives-ouvertes.fr/hal-01142767

S. Audic, M. Lescot, J. M. Claverie, and H. C. Scholz, Brucella microti: the genome sequence of an emerging pathogen, BMC Genomics, vol.10, issue.1, p.352, 2009.
DOI : 10.1186/1471-2164-10-352

M. P. Franco, M. Mulder, R. H. Gilman, and H. L. Smits, Human brucellosis, The Lancet Infectious Diseases, vol.7, issue.12, pp.775-786, 2007.
DOI : 10.1016/S1473-3099(07)70286-4

E. Pennacchietti, T. M. Lammens, G. Capitani, M. C. Franssen, R. A. John et al., Mutation of His465 Alters the pH-dependent Spectroscopic Properties of Escherichia coli Glutamate Decarboxylase and Broadens the Range of Its Activity toward More Alkaline pH, Journal of Biological Chemistry, vol.284, issue.46, pp.31587-31596, 2009.
DOI : 10.1074/jbc.M109.049577

G. Capitani, D. De-biase, C. Aurizi, H. Gut, F. Bossa et al., Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase, The EMBO Journal, vol.22, issue.16, pp.4027-4037, 2003.
DOI : 10.1093/emboj/cdg403

E. W. Rice, C. H. Johnson, M. E. Dunnigan, and D. J. Reasoner, Rapid glutamate decarboxylase assay for detection of Escherichia coli, Appl. Environ. Microb, vol.59, pp.4347-4349, 1993.

D. De-biase, A. Tramonti, R. A. John, and F. Bossa, Isolation, Overexpression, and Biochemical Characterization of the Two Isoforms of Glutamic Acid Decarboxylase fromEscherichia coli, Protein Expression and Purification, vol.8, issue.4, pp.430-438, 1996.
DOI : 10.1006/prep.1996.0121

D. De-biase, A. Tramonti, F. Bossa, and P. Visca, The response to stationary-phase stress conditions in Escherichia coli : role and regulation of the glutamic acid decarboxylase system, Molecular Microbiology, vol.15, issue.6, pp.1198-1211, 1999.
DOI : 10.1016/0378-1119(92)90026-L

U. K. Laemmli, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, Nature, vol.244, issue.5259, pp.680-685, 1970.
DOI : 10.1038/227680a0

J. J. Gillespie, A. R. Wattam, S. A. Cammer, J. L. Gabbard, M. P. Shukla et al., PATRIC: the Comprehensive Bacterial Bioinformatics Resource with a Focus on Human Pathogenic Species, Infection and Immunity, vol.79, issue.11, pp.4286-4298, 2011.
DOI : 10.1128/IAI.00207-11

B. Zhao and W. A. Houry, Acid stress response in enteropathogenic gammaproteobacteria: an aptitude for survivalThis paper is one of a selection of papers published in this special issue entitled ???Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting ??? Protein Folding: Principles and Diseases??? and has undergone the Journal's usual peer review process., Biochemistry and Cell Biology, vol.88, issue.2, pp.301-314, 2010.
DOI : 10.1139/O09-182

O. Leary, M. H. , B. Jr, and W. , PH jump studies of glutamate decarboxylase. Evidence for a pH-dependent conformation change, J. Biol. Chem, vol.249, pp.3737-3745, 1974.

P. D. Cotter, C. G. Gahan, and C. Hill, A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid, Molecular Microbiology, vol.23, issue.2, pp.465-475, 2001.
DOI : 10.1074/jbc.273.4.1939

M. P. Castanie-cornet, T. A. Penfound, D. Smith, J. F. Elliott, and J. W. Foster, Control of acid resistance in Escherichia coli, J. Bacteriol, vol.181, pp.3525-3535, 1999.

P. L. Small and S. R. Waterman, Acid stress, anaerobiosis and gadCB: lessons from Lactococcus lactis and Escherichia coli, Trends in Microbiology, vol.6, issue.6, pp.214-216, 1998.
DOI : 10.1016/S0966-842X(98)01285-2

J. W. Sanders, K. Leenhouts, J. Burghoorn, J. R. Brands, G. Venema et al., A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation, Molecular Microbiology, vol.27, issue.2, pp.299-310, 1998.
DOI : 10.1007/s004380050315

J. W. Foster, Escherichia coli acid resistance: tales of an amateur acidophile, Nature Reviews Microbiology, vol.48, issue.11, pp.898-907, 2004.
DOI : 10.1146/annurev.mi.39.100185.001251

D. I. Dutyshev, E. L. Darii, N. P. Fomenkova, I. V. Pechik, K. M. Polyakov et al., glutamate decarboxylase (GAD??) in complex with glutarate at 2.05????? resolution, Acta Crystallographica Section D Biological Crystallography, vol.61, issue.3, pp.230-235, 2005.
DOI : 10.1107/S0907444904032147

M. P. Jimenez-de-bagues, S. Ouahrani-bettache, J. F. Quintana, O. Mitjana, N. Hanna et al., Replicates in Macrophages and Causes Death in Murine Models of Infection, The Journal of Infectious Diseases, vol.202, issue.1, pp.3-10, 2010.
DOI : 10.1086/653084
URL : https://hal.archives-ouvertes.fr/hal-00509064

M. P. Jimenez-de-bagues, M. Iturralde, M. A. Arias, J. Pardo, A. Cloeckaert et al., The New Strains Brucella inopinata BO1 and Brucella Species 83-210 Behave Biologically Like Classic Infectious Brucella Species and Cause Death in Murine Models of Infection, Journal of Infectious Diseases, vol.210, issue.3, pp.467-472, 2014.
DOI : 10.1093/infdis/jiu102

N. Hanna, M. P. Jimenez-de-bagues, S. Ouahrani-bettache, Z. El-yakhlifi, S. Kohler et al., The virB Operon Is Essential for Lethality of Brucella microti in the Balb/c Murine Model of Infection, Journal of Infectious Diseases, vol.203, issue.8, pp.1129-1135, 2011.
DOI : 10.1093/infdis/jiq163

J. P. Gorvel, E. Moreno, and I. Moriyon, Is Brucella an enteric pathogen?, Nature Reviews Microbiology, vol.6, issue.3, 2009.
DOI : 10.1038/nrmicro2012-c1
URL : https://hal.archives-ouvertes.fr/hal-00407895

A. R. Wattam, J. T. Foster, S. P. Mane, S. M. Beckstrom-sternberg, J. M. Beckstrom-sternberg et al., Comparative Phylogenomics and Evolution of the Brucellae Reveal a Path to Virulence, Journal of Bacteriology, vol.196, issue.5, pp.920-930, 2014.
DOI : 10.1128/JB.01091-13

S. Audic, M. Lescot, J. M. Claverie, A. Cloeckaert, and M. S. Zygmunt, The genome sequence of Brucella pinnipedialis B2/94 sheds light on the evolutionary history of the genus Brucella, BMC Evolutionary Biology, vol.52, issue.1, 0200.
DOI : 10.1080/10635150390235520
URL : https://hal.archives-ouvertes.fr/hal-01258246

I. Cozzani, R. Barsacchi, G. Dibenedetto, L. Saracchi, and G. Falcone, Regulation of breakdown and synthesis of L-glutamate decarboxylase in Clostridium perfringens, J. Bacteriol, vol.123, pp.1115-1123, 1975.

I. Cozzani and G. Bagnoli, The subunits of L-glutamate decarboxylase from Clostridium perfringens, Ital. J. Biochem, vol.22, pp.36-45, 1973.

I. Cozzani and G. Bagnoli, Reversible resolution of glutamate decarboxylase from Clostridium perfringens, Ital. J. Biochem, vol.20, pp.179-190, 1971.

S. M. Tennant, E. L. Hartland, T. Phumoonna, D. Lyras, J. I. Rood et al., Influence of Gastric Acid on Susceptibility to Infection with Ingested Bacterial Pathogens, Infection and Immunity, vol.76, issue.2, pp.639-645, 2008.
DOI : 10.1128/IAI.01138-07