Purinergic Signaling during Inflammation, New England Journal of Medicine, vol.367, issue.24, pp.2322-2333, 2012. ,
DOI : 10.1056/NEJMra1205750
Immune cell regulation by autocrine purinergic signalling, Nature Reviews Immunology, vol.3, issue.3, pp.201-212, 2011. ,
DOI : 10.1038/nri2938
Nucleotides released by apoptotic cells act as a find-me signal to promote phagocytic clearance, Nature, vol.127, issue.7261, pp.282-286, 2009. ,
DOI : 10.1038/nature08296
ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1?? and IL-18 secretion in an autocrine way, Proceedings of the National Academy of Sciences, vol.105, issue.23, pp.8067-8072, 2008. ,
DOI : 10.1073/pnas.0709684105
ATP Release Guides Neutrophil Chemotaxis via P2Y2 and A3 Receptors, Science, vol.314, issue.5806, pp.1792-1795, 2006. ,
DOI : 10.1126/science.1132559
Autocrine regulation of T-cell activation by ATP release and P2X7 receptors, The FASEB Journal, vol.23, issue.6, pp.1685-1693, 2009. ,
DOI : 10.1096/fj.08-126458
Extracellular ATP in the Immune System: More Than Just a "Danger Signal", Science Signaling, vol.2, issue.56, p.6, 2009. ,
DOI : 10.1126/scisignal.256pe6
Immunoregulation through extracellular nucleotides, Blood, vol.120, issue.3, pp.511-518, 2012. ,
DOI : 10.1182/blood-2012-01-406496
Adenosine receptors: therapeutic aspects for inflammatory and immune diseases, Nat. Rev. Drug Discov, vol.7, pp.759-770, 2008. ,
DOI : 10.1201/9781420005776
The 'danger' sensors that STOP the immune response: the A2 adenosine receptors? Trends Immunol, pp.299-304, 2005. ,
P2X receptors as cell-surface ATP sensors in health and disease, Nature, vol.279, issue.7102, pp.527-532, 2006. ,
DOI : 10.1038/nature04886
Cellular function and molecular structure of ecto-nucleotidases, Purinergic Signalling, vol.44, issue.Pt 2, pp.437-502, 2012. ,
DOI : 10.1007/s11302-012-9309-4
Adenosine generation catalyzed by CD39 and CD73 expressed on regulatory T cells mediates immune suppression, The Journal of Experimental Medicine, vol.261, issue.6, pp.1257-1265, 2007. ,
DOI : 10.1074/jbc.275.3.2057
Possible Effects of Microbial Ecto-Nucleoside Triphosphate Diphosphohydrolases on Host-Pathogen Interactions, Microbiology and Molecular Biology Reviews, vol.72, issue.4, pp.765-781, 2008. ,
DOI : 10.1128/MMBR.00013-08
A bacterial ecto-triphosphate diphosphohydrolase similar to human CD39 is essential for intracellular multiplication of Legionella pneumophila, Cellular Microbiology, vol.63, issue.8, pp.1922-1935, 2007. ,
DOI : 10.1242/jcs.00329
Enzymatic Properties of an Ecto-nucleoside Triphosphate Diphosphohydrolase from Legionella pneumophila: SUBSTRATE SPECIFICITY AND REQUIREMENT FOR VIRULENCE, Journal of Biological Chemistry, vol.283, issue.19, pp.12909-12918, 2008. ,
DOI : 10.1074/jbc.M801006200
Crystal Structure of a Legionella pneumophila Ecto -Triphosphate Diphosphohydrolase, A Structural and Functional Homolog of the Eukaryotic NTPDases, Crystal structure of a Legionella pneumophila ecto-triphosphate diphosphohydrolase, a structural and functional homolog of the eukaryotic NTPDases, pp.228-238, 2010. ,
DOI : 10.1016/j.str.2009.11.014
synthesizes adenosine to escape host immune responses, The Journal of Experimental Medicine, vol.162, issue.11, pp.2417-2427, 2009. ,
DOI : 10.1042/bj2850345
Staphylococcus aureus Degrades Neutrophil Extracellular Traps to Promote Immune Cell Death, Science, vol.342, issue.6160, pp.863-866, 2013. ,
DOI : 10.1126/science.1242255
Ecto-5???-Nucleotidase: A Candidate Virulence Factor in Streptococcus sanguinis Experimental Endocarditis, PLoS ONE, vol.39, issue.6, p.38059, 2012. ,
DOI : 10.1371/journal.pone.0038059.s005
Group B Streptococcus: global incidence and vaccine development, Nature Reviews Microbiology, vol.60, issue.12, pp.932-942, 2006. ,
DOI : 10.1038/nrmicro1552
Group B streptococcal disease in infants aged younger than 3 months: systematic review and meta-analysis, The Lancet, vol.379, issue.9815, pp.547-556 ,
DOI : 10.1016/S0140-6736(11)61651-6
Prevention of perinatal group B streptococcal disease?revised guidelines from CDC, MMWR Recomm. Rep, vol.59, pp.1-36, 2010. ,
Interaction of Neonatal Phagocytes with Group B Streptococcus: Recognition and Response, Infection and Immunity, vol.74, issue.6, pp.3085-3095, 2006. ,
DOI : 10.1128/IAI.01551-05
Innate immunity of the newborn: basic mechanisms and clinical correlates, Nature Reviews Immunology, vol.21, issue.5, pp.379-390, 2007. ,
DOI : 10.1038/nri2075
Innate Immune Function by Toll-like Receptors: Distinct Responses in Newborns and the Elderly, Immunity, vol.37, issue.5, pp.771-783, 2012. ,
DOI : 10.1016/j.immuni.2012.10.014
The Adenosine System Selectively Inhibits TLR-Mediated TNF-?? Production in the Human Newborn, The Journal of Immunology, vol.177, issue.3, pp.1956-1966, 2006. ,
DOI : 10.4049/jimmunol.177.3.1956
Soluble Ecto-5???-nucleotidase (5???-NT), Alkaline Phosphatase, and Adenosine Deaminase (ADA1) Activities in Neonatal Blood Favor Elevated Extracellular Adenosine, Journal of Biological Chemistry, vol.288, issue.38, pp.27315-27326, 2013. ,
DOI : 10.1074/jbc.M113.484212
Identification of immunoreactive extracellular proteins of Streptococcus agalactiae in bovine mastitis, Canadian Journal of Microbiology, vol.54, issue.11, pp.899-905, 2008. ,
DOI : 10.1139/W08-083
Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease, Molecular Microbiology, vol.181, issue.6, pp.1499-1513, 2002. ,
DOI : 10.1046/j.1365-2958.2002.03126.x
Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies, J. Biol. Chem, vol.271, pp.8046-8052, 1996. ,
Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling, Biophysical Journal, vol.78, issue.3, pp.1606-1619, 2000. ,
DOI : 10.1016/S0006-3495(00)76713-0
Gene splicing and mutagenesis by PCR-driven overlap extension, Nature Protocols, vol.2, issue.4, pp.924-932, 2007. ,
DOI : 10.1038/nprot.2007.132
The Abi-domain Protein Abx1 Interacts with the CovS Histidine Kinase to Control Virulence Gene Expression in Group B Streptococcus, PLoS Pathogens, vol.18, issue.2, p.1003179, 2013. ,
DOI : 10.1371/journal.ppat.1003179.s007
URL : https://hal.archives-ouvertes.fr/pasteur-01300159
Dual Role for Pilus in Adherence to Epithelial Cells and Biofilm Formation in Streptococcus agalactiae, PLoS Pathogens, vol.21, issue.1, p.1000422, 2009. ,
DOI : 10.1371/journal.ppat.1000422.s004
The SrtA Sortase of Streptococcus agalactiae Is Required for Cell Wall Anchoring of Proteins Containing the LPXTG Motif, for Adhesion to Epithelial Cells, and for Colonization of the Mouse Intestine, Infection and Immunity, vol.73, issue.6, pp.3342-3350, 2005. ,
DOI : 10.1128/IAI.73.6.3342-3350.2005
URL : https://hal.archives-ouvertes.fr/hal-00019655
X-ray structure of the Escherichia coli periplasmic 5-nucleotidase containing a dimetal catalytic site, Nat. Struct. Biol, vol.6, pp.448-453, 1999. ,
E. coli 5???-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion, Journal of Molecular Biology, vol.309, issue.1, pp.255-266, 2001. ,
DOI : 10.1006/jmbi.2001.4657
Mechanism of hydrolysis of phosphate esters by the dimetal center of 5???-nucleotidase based on crystal structures, Journal of Molecular Biology, vol.309, issue.1, pp.239-254, 2001. ,
DOI : 10.1006/jmbi.2001.4656
5???-nucleotidase to substrate specificity and catalysis, FEBS Letters, vol.284, issue.5, pp.460-466, 2013. ,
DOI : 10.1016/j.febslet.2013.01.010
Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria, Research in Microbiology, vol.156, issue.3, pp.289-297, 2005. ,
DOI : 10.1016/j.resmic.2004.10.011
Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria, Microbiology and Molecular Biology Reviews, vol.70, issue.1, pp.192-221, 2006. ,
DOI : 10.1128/MMBR.70.1.192-221.2006
Architects at the bacterial surface ??? sortases and the assembly of pili with isopeptide bonds, Nature Reviews Microbiology, vol.77, issue.3, pp.166-176, 2011. ,
DOI : 10.1038/nrmicro2520
Surface Proteins of Streptococcus agalactiae and Related Proteins in Other Bacterial Pathogens, Clinical Microbiology Reviews, vol.18, issue.1, pp.102-127, 2005. ,
DOI : 10.1128/CMR.18.1.102-127.2005
Lipoproteins Are Critical TLR2 Activating Toxins in Group B Streptococcal Sepsis, The Journal of Immunology, vol.180, issue.9, pp.6149-6158, 2008. ,
DOI : 10.4049/jimmunol.180.9.6149
URL : https://hal.archives-ouvertes.fr/hal-00276062
Streptococcus Adherence and Colonization, Microbiology and Molecular Biology Reviews, vol.73, issue.3, pp.407-450, 2009. ,
DOI : 10.1128/MMBR.00014-09
The surface protein HvgA mediates group B streptococcus hypervirulence and meningeal tropism in neonates, The Journal of Experimental Medicine, vol.59, issue.11, pp.2313-2322, 2010. ,
DOI : 10.1111/j.1365-2958.2005.04555.x
A hemolytic pigment of Group B Streptococcus allows bacterial penetration of human placenta, The Journal of Experimental Medicine, vol.66, issue.RR-10, pp.1265-1281, 2013. ,
DOI : 10.1186/1477-7827-5-46
The Role of the P2X7 Receptor in Infectious Diseases, PLoS Pathogens, vol.282, issue.1, p.1002212, 2011. ,
DOI : 10.1371/journal.ppat.1002212.t001
Ecto-5???-Nucleotidase (CD73) Decreases Mortality and Organ Injury in Sepsis, The Journal of Immunology, vol.187, issue.8, pp.4256-4267, 2011. ,
DOI : 10.4049/jimmunol.1003379
Activation of the Nlrp3 Inflammasome by Streptococcus pyogenes Requires Streptolysin O and NF-??B Activation but Proceeds Independently of TLR Signaling and P2X7 Receptor, The Journal of Immunology, vol.183, issue.9, pp.5823-5829, 2009. ,
DOI : 10.4049/jimmunol.0900444
, attacks the neutrophil extracellular traps and is needed for full virulence, Molecular Microbiology, vol.75, issue.3, pp.518-531, 2013. ,
DOI : 10.1111/mmi.12295