J. M. Musser, S. J. Mattingly, R. Quentin, A. Goudeau, and R. K. Selander, Identification of a high-virulence clone of type III Streptococcus agalactiae (group B streptococcus) causing invasive neonatal disease, Proc Natl Acad Sci, vol.86, pp.4731-4735, 1989.

C. R. Phares, R. Lynfield, M. M. Farley, J. Mohle-boetani, and L. H. Harrison, , 2008.

, Epidemiology of invasive group B streptococcal disease in the United States, JAMA, vol.299, pp.2056-2065, 1999.

C. Poyart, H. Réglier-poupet, A. Tazi, A. Billoët, and N. Dmytruk, Invasive group B streptococcal infections in infants, France. Emerging Infectious Diseases, vol.14, pp.1647-1649, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00307826

A. Tazi, O. Disson, S. Bellais, A. Bouaboud, and N. Dmytruk, The surface protein, 2010.

, HvgA mediates group B streptococcus hypervirulence and meningeal tropism in neonates, J Exp Med, vol.207, pp.2313-2322

A. Six, S. Bellais, A. Bouaboud, A. Fouet, and C. Gabriel, Srr2, a multifaceted adhesin expressed by ST-17 hypervirulent group B streptococcus involved in binding to both fibrinogen and plasminogen, Mol Microbiol, vol.97, pp.1209-1222, 2015.
URL : https://hal.archives-ouvertes.fr/pasteur-01299767

M. Madzivhandila, P. V. Adrian, C. L. Cutland, L. Kuwanda, and S. A. Madhi, , 2013.

, Distribution of pilus islands of group B streptococcus associated with maternal colonization and invasive disease in South Africa, J Med Microbiol, vol.62, pp.249-253

C. D. Rinaudo, R. Rosini, C. L. Galeotti, F. Berti, and F. Necchi, Specific involvement of pilus type 2a in biofilm formation in group B streptococcus, PLoS ONE, vol.5, p.9216, 2010.

A. C. Springman, D. W. Lacher, E. A. Waymire, S. L. Wengert, and P. Singh, Pilus distribution among lineages of group B streptococcus: an evolutionary and clinical perspective, BMC Microbiol, vol.14, p.159, 2014.

S. Teatero, E. Ramoutar, A. Mcgeer, A. Li, and R. G. Melano, Clonal Complex, p.17, 2016.

, group B streptococcus strains causing invasive disease in neonates and adults originate from the same genetic pool, Sci Rep, vol.6, 20047.

M. Brochet, E. Couvé, M. Zouine, T. Vallaeys, and C. Rusniok, Genomic diversity and evolution within the species Streptococcus agalactiae, Microbes Infect, vol.8, pp.1227-1243, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00084225

M. Lazzarin, R. Cozzi, E. Malito, M. Martinelli, D. Onofrio et al., Noncanonical sortase-mediated assembly of pilus type 2b in group B streptococcus, FASEB J, vol.29, pp.4629-4640, 2015.

R. Cozzi, E. Malito, M. Lazzarin, A. Nuccitelli, and A. Castagnetti, Phylogenetic lineage and pilus protein Spb1/SAN1518 affect opsonin-independent phagocytosis and intracellular survival of group B streptococcus, Microbes Infect, vol.10, pp.369-382, 2011.

S. Dramsi, E. Caliot, I. Bonne, S. Guadagnini, and M. Prévost, Assembly and role of pili in group B streptococci, Mol Microbiol, vol.60, pp.1401-1413, 2006.

Y. Konto-ghiorghi, E. Mairey, A. Mallet, G. Duménil, and E. Caliot, Dual role for pilus in adherence to epithelial cells and biofilm formation in Streptococcus agalactiae, PLoS Pathog, vol.5, p.1000422, 2009.

I. C. Sutcliffe, G. W. Black, and D. J. Harrington, Bioinformatic insights into the biosynthesis of the Group B carbohydrate in Streptococcus agalactiae, Microbiology (Reading, Engl), vol.154, pp.1354-1363, 2008.

I. Rosinski-chupin, E. Sauvage, O. Sismeiro, A. Villain, D. Cunha et al., Single nucleotide resolution RNA-seq uncovers new regulatory mechanisms in the opportunistic pathogen Streptococcus agalactiae, BMC Genomics, vol.16, p.419, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01169621

S. Jiang, M. J. Cieslewicz, D. L. Kasper, and M. R. Wessels, Regulation of virulence by a two-component system in group B Streptococcus, J Bacteriol, vol.187, pp.1105-1113, 2005.

M. Lamy, M. Zouine, J. Fert, M. Vergassola, and E. Couvé, CovS/CovR of group B streptococcus: a two-component global regulatory system involved in virulence, Mol Microbiol, vol.54, pp.1250-1268, 2004.
URL : https://hal.archives-ouvertes.fr/hal-00019892

A. Lembo, M. A. Gurney, K. Burnside, A. Banerjee, and M. De-los-reyes, Regulation of CovR expression in Group B streptococcus impacts blood-brain barrier penetration, Mol Microbiol, vol.77, pp.431-443, 2010.

S. Jiang, S. E. Park, P. Yadav, L. C. Paoletti, and M. R. Wessels, Regulation and function of pilus island 1 in group B streptococcus, J Bacteriol, vol.194, pp.2479-2490, 2012.

R. Rosini, C. D. Rinaudo, M. Soriani, P. Lauer, and M. Mora, Identification of novel genomic islands coding for antigenic pilus-like structures in Streptococcus agalactiae, Mol Microbiol, vol.61, pp.126-141, 2006.

D. Maione, I. Margarit, C. D. Rinaudo, V. Masignani, and M. Mora, Identification of a universal group B streptococcus vaccine by multiple genome screen, Science, vol.309, pp.148-150, 2005.

M. Barnham, The gut as a source of the haemolytic streptococci causing infection in surgery of the intestinal and biliary tracts, J Infect, vol.6, issue.2, pp.129-168, 1983.

M. A. Barocchi, A pneumococcal pilus influences virulence and host inflammatory responses, Proc Natl Acad Sci, vol.103, issue.8, pp.2857-62, 2006.

A. Basset, Expression of the type 1 pneumococcal pilus is bistable and negatively regulated by the structural component RrgA, Infect Immun, vol.79, issue.8, pp.2974-83, 2011.

A. Basset, An epigenetic switch mediates bistable expression of the type 1 pilus genes in Streptococcus pneumoniae, J Bacteriol, vol.194, issue.5, pp.1088-91, 2012.

A. Basset, Toll-like receptor (TLR) 2 mediates inflammatory responses to oligomerized RrgA pneumococcal pilus type 1 protein, J Biol Chem, vol.288, issue.4, pp.2665-75, 2013.

A. Beaussart, Molecular mapping of the cell wall polysaccharides of the human pathogen Streptococcus agalactiae, Nanoscale, vol.6, issue.24, pp.14820-14827, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01194015

S. Beckert, B. Kreikemeyer, and A. Podbielski, Group A streptococcal rofA gene is involved in the control of several virulence genes and eukaryotic cell attachment and internalization, Infect Immun, vol.69, issue.1, pp.534-541, 2001.

S. Bellais, Capsular switching in group B Streptococcus CC17 hypervirulent clone: a future challenge for polysaccharide vaccine development, J Infect Dis, vol.206, issue.11, pp.1745-52, 2012.
URL : https://hal.archives-ouvertes.fr/pasteur-01300172

C. Beloin, A. Roux, and J. M. Ghigo, Escherichia coli biofilms, vol.322, pp.249-89, 2008.
URL : https://hal.archives-ouvertes.fr/pasteur-00473297

A. Berardi, Group B streptococcus late-onset disease and milk transmission, Acta Paediatr, vol.102, issue.3, p.95, 2013.

H. Bierne and S. Dramsi, Spatial positioning of cell wall-anchored virulence factors in Grampositive bacteria, Curr Opin Microbiol, vol.15, issue.6, pp.715-738, 2012.

N. Bisharat, Hyperinvasive neonatal group B streptococcus has arisen from a bovine ancestor, J Clin Microbiol, vol.42, issue.5, pp.2161-2168, 2004.

H. M. Blumberg, Invasive group B streptococcal disease: the emergence of serotype V, J Infect Dis, vol.173, issue.2, pp.365-73, 1996.

J. F. Bohnsack, Serotype III Streptococcus agalactiae from bovine milk and human neonatal infections, Emerg Infect Dis, vol.10, issue.8, pp.1412-1421, 2004.

G. R. Bolduc and L. C. Madoff, The group B streptococcal alpha C protein binds alpha1beta1integrin through a novel KTD motif that promotes internalization of GBS within human epithelial cells. Microbiology, pp.4039-4088, 2007.

A. Bourgogne, L. C. Thomson, and B. E. Murray, Bicarbonate enhances expression of the endocarditis and biofilm associated pilus locus, ebpR-ebpABC, in Enterococcus faecalis, BMC Microbiol, vol.10, p.17, 2010.

S. Brega, SecA localization and SecA-dependent secretion occurs at new division septa in group B Streptococcus, PLoS One, vol.8, issue.6, p.65832, 2013.
URL : https://hal.archives-ouvertes.fr/pasteur-01300164

J. L. Brittan and A. H. Nobbs, Group B Streptococcus pili mediate adherence to salivary glycoproteins. Microbes Infect, vol.17, pp.360-368, 2015.

M. Brochet, Genomic diversity and evolution within the species Streptococcus agalactiae, Microbes Infect, vol.8, issue.5, pp.1227-1270, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00084225

W. V. Brown and E. B. Collins, End products and fermentation balances for lactic streptococci grown aerobically on low concentrations of glucose, Appl Environ Microbiol, vol.33, issue.1, pp.38-42, 1977.

J. M. Budzik, Intramolecular amide bonds stabilize pili on the surface of bacilli, Proc Natl Acad Sci, vol.106, issue.47, pp.19992-19999, 2009.

M. Buscetta, PbsP, a cell wall-anchored protein that binds plasminogen to promote hematogenous dissemination of group B Streptococcus, Mol Microbiol, vol.101, issue.1, pp.27-41, 2016.
URL : https://hal.archives-ouvertes.fr/pasteur-01308716

M. Buscetta, FbsC, a novel fibrinogen-binding protein, promotes Streptococcus agalactiae-host cell interactions, J Biol Chem, vol.289, issue.30, pp.21003-21015, 2014.
URL : https://hal.archives-ouvertes.fr/pasteur-01299770

É. Caliot, Role of the Group B antigen of Streptococcus agalactiae: a peptidoglycananchored polysaccharide involved in cell wall biogenesis, PLoS Pathog, vol.8, issue.6, p.p, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01191122

E. Campisi, Genomic Analysis Reveals Multi-Drug Resistance Clusters in Group B Streptococcus CC17 Hypervirulent Isolates Causing Neonatal Invasive Disease in Southern Mainland China, Front Microbiol, vol.7, p.1265, 2016.

J. B. Cantey, Late and very late onset group B Streptococcus sepsis: one and the same?, World J Pediatr, vol.10, issue.1, pp.24-32, 2014.

A. F. Carlin, Group B streptococcal capsular sialic acids interact with siglecs (immunoglobulin-like lectins) on human leukocytes, J Bacteriol, vol.189, issue.4, pp.1231-1238, 2007.

D. O. Chaffin, The serotype of type Ia and III group B streptococci is determined by the polymerase gene within the polycistronic capsule operon, J Bacteriol, vol.182, issue.16, pp.4466-77, 2000.

C. Chang, Cell surface display of minor pilin adhesins in the form of a simple heterodimeric assembly in Corynebacterium diphtheriae, Mol Microbiol, vol.79, issue.5, pp.1236-1283, 2011.

Y. C. Chang and V. Nizet, The interplay between Siglecs and sialylated pathogens

, Glycobiology, vol.24, issue.9, pp.818-843, 2014.

Y. C. Chang, Group B Streptococcus engages an inhibitory Siglec through sialic acid mimicry to blunt innate immune and inflammatory responses in vivo, PLoS Pathog, vol.10, issue.1, p.1003846, 2014.

M. Charrel-dennis, TLR-independent type I interferon induction in response to an extracellular bacterial pathogen via intracellular recognition of its DNA, Cell Host Microbe, vol.4, issue.6, pp.543-54, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00346660

D. Chattopadhyay, Phylogenetic lineage and pilus protein Spb1/SAN1518 affect opsonin-independent phagocytosis and intracellular survival of Group B Streptococcus. Microbes Infect, vol.13, pp.369-82, 2011.

M. Chen, Streptococcus agalactiae isolates of serotypes Ia, III and V from human and cow are able to infect tilapia, Vet Microbiol, vol.180, issue.1-2, pp.129-164, 2015.

R. , A. N. , and M. E. , A note on a lytic phenomenon shown by group B streptococci. The Australian journal of experimental biology and medical science, vol.22, p.4, 1944.

M. J. Cieslewicz, Structural and genetic diversity of group B streptococcus capsular polysaccharides, Infect Immun, vol.73, issue.5, pp.3096-103, 2005.

J. O. Cisar, Mutants of Actinomyces viscosus T14V lacking type 1, type 2, or both types of fimbriae, Infect Immun, vol.56, issue.11, pp.2984-2993, 1988.

C. M. Phyllis, Streptococcal Infection in Childbirth and Septic Abortion: Source of Infection and Grouping of Haemolytic Strains. The Lancet, vol.226, p.2, 1935.

R. Cozzi, New insights into the role of the glutamic acid of the E-box motif in group B Streptococcus pilus 2a assembly, FASEB J, vol.26, issue.5, pp.2008-2026, 2012.

V. Da-cunha, Streptococcus agalactiae clones infecting humans were selected and fixed through the extensive use of tetracycline, Nat Commun, vol.5, p.4544, 2014.
URL : https://hal.archives-ouvertes.fr/pasteur-01299769

Z. Dangor, Review on the association of Group B Streptococcus capsular antibody and protection against invasive disease in infants, Expert Rev Vaccines, vol.14, issue.1, pp.135-184, 2015.

M. Dangwetngam, Serotype distribution and antimicrobial susceptibilities of Streptococcus agalactiae isolated from infected cultured tilapia (Oreochromis niloticus) in Thailand: Nine-year perspective, J Med Microbiol, vol.65, issue.3, pp.247-54, 2016.

C. Danne and S. Dramsi, Pili of gram-positive bacteria: roles in host colonization, Res Microbiol, vol.163, issue.9, pp.645-58, 2012.

C. Danne, Single cell stochastic regulation of pilus phase variation by an attenuationlike mechanism, PLoS Pathog, vol.10, issue.1, p.1003860, 2014.
URL : https://hal.archives-ouvertes.fr/pasteur-01299772

C. Danne, Molecular characterization of a Streptococcus gallolyticus genomic island encoding a pilus involved in endocarditis, J Infect Dis, vol.204, issue.12, pp.1960-70, 2011.
URL : https://hal.archives-ouvertes.fr/hal-01000633

H. D. Davies, Multilocus sequence typing of serotype III group B streptococcus and correlation with pathogenic potential, J Infect Dis, vol.189, issue.6, pp.1097-102, 2004.

G. De-angelis, The Streptococcus pneumoniae pilus-1 displays a biphasic expression pattern, PLoS One, vol.6, issue.6, p.21269, 2011.

M. De-la-rosa, Granada medium for detection and identification of group B streptococci, J Clin Microbiol, vol.18, issue.4, pp.779-85, 1983.

D. De-mouy, Antibiotic susceptibility and mechanisms of erythromycin resistance in clinical isolates of Streptococcus agalactiae: French multicenter study, Antimicrob Agents Chemother, vol.45, issue.8, pp.2400-2402, 2001.

S. Debroy, Riboswitches. A riboswitch-containing sRNA controls gene expression by sequestration of a response regulator, Science, vol.345, pp.937-977, 2014.

C. M. Delannoy, Genomic comparison of virulent and non-virulent Streptococcus agalactiae in fish, J Fish Dis, vol.39, issue.1, pp.13-29, 2016.

L. Deng, Characterization of the linkage between the type III capsular polysaccharide and the bacterial cell wall of group B Streptococcus, J Biol Chem, vol.275, issue.11, pp.7497-504, 2000.

A. S. Devi and K. Ponnuraj, Cloning, expression, purification and ligand binding studies of novel fibrinogen-binding protein FbsB of Streptococcus agalactiae, Protein Expr Purif, vol.74, issue.2, pp.148-55, 2010.

H. C. Dillon, Anorectal and vaginal carriage of group B streptococci during pregnancy, J Infect Dis, vol.145, issue.6, pp.794-803, 1982.

S. Dramsi, Assembly and role of pili in group B streptococci, Mol Microbiol, vol.60, issue.6, pp.1401-1414, 2006.

S. Dramsi, Rga, a RofA-like regulator, is the major transcriptional activator of the PI-2a pilus in Streptococcus agalactiae, Microb Drug Resist, vol.18, issue.3, pp.286-97, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01004186

S. Dramsi, Epidemiologically and clinically relevant Group B Streptococcus isolates do not bind collagen but display enhanced binding to human fibrinogen, Microbes Infect, vol.14, issue.12, pp.1044-1052, 2012.
URL : https://hal.archives-ouvertes.fr/pasteur-01300174

S. Dramsi, P. Trieu-cuot, and H. Bierne, Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria, Res Microbiol, vol.156, issue.3, pp.289-97, 2005.

C. S. Easmon, Group B streptococcus, pp.135-142, 1986.

M. S. Edwards, Capsular sialic acid prevents activation of the alternative complement pathway by type III, group B streptococci, J Immunol, vol.128, issue.3, pp.1278-83, 1982.

K. Ekelund, Emergence of invasive serotype VIII group B streptococcal infections in Denmark, J Clin Microbiol, vol.41, issue.9, pp.4442-4446, 2003.

M. Emaneini, Comparison of virulence factors and capsular types of Streptococcus agalactiae isolated from human and bovine infections, Microb Pathog, vol.91, pp.1-4, 2016.

M. M. Farley, Group B streptococcal disease in nonpregnant adults, Clin Infect Dis, vol.33, issue.4, pp.556-61, 2001.

M. M. Farley, A population-based assessment of invasive disease due to group B Streptococcus in nonpregnant adults, N Engl J Med, vol.328, issue.25, pp.1807-1818, 1993.

S. Faro, Group B beta-hemolytic streptococci and puerperal infections, Am J Obstet Gynecol, vol.139, issue.6, pp.686-695, 1981.
DOI : 10.1016/0002-9378(81)90486-5

A. Filleron, Group B streptococci in milk and late neonatal infections: an analysis of cases in the literature, Arch Dis Child Fetal Neonatal Ed, vol.99, issue.1, pp.41-48, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02049016

L. A. Finch and D. R. Martin, Human and bovine group B streptococci: two distinct populations, J Appl Bacteriol, vol.57, issue.2, pp.273-281, 1984.
DOI : 10.1111/j.1365-2672.1984.tb01391.x

URL : https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-2672.1984.tb01391.x

A. Firon, Extracellular nucleotide catabolism by the Group B Streptococcus ectonucleotidase NudP increases bacterial survival in blood, J Biol Chem, vol.289, issue.9, pp.5479-89, 2014.
URL : https://hal.archives-ouvertes.fr/pasteur-01299774

A. Firon, The Abi-domain protein Abx1 interacts with the CovS histidine kinase to control virulence gene expression in group B Streptococcus, PLoS Pathog, vol.9, issue.2, p.p, 2013.
URL : https://hal.archives-ouvertes.fr/pasteur-01300159

N. Fittipaldi, Mutations in the gene encoding the ancillary pilin subunit of the

, Streptococcus suis srtF cluster result in pili formed by the major subunit only, PLoS One, vol.5, issue.1, p.8426, 2010.

A. L. Flores-mireles, Urinary tract infections: epidemiology, mechanisms of infection and treatment options, Nat Rev Microbiol, vol.13, issue.5, pp.269-84, 2015.

K. Frank and M. J. Sippl, High-performance signal peptide prediction based on sequence alignment techniques, Bioinformatics, vol.24, pp.2172-2178, 2008.

M. and F. R. , Fatal Infections by Haemolytic Streptococcus Group B. The Lancet, vol.231, 1938.

A. H. Gaspar and H. Ton-that, Assembly of distinct pilus structures on the surface of Corynebacterium diphtheriae, J Bacteriol, vol.188, issue.4, pp.1526-1559, 2006.

C. Gianfaldoni, Streptococcus pneumoniae pilus subunits protect mice against lethal challenge, Infect Immun, vol.75, issue.2, pp.1059-62, 2007.
DOI : 10.1128/iai.01400-06

URL : https://iai.asm.org/content/75/2/1059.full.pdf

P. Glaser, Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease, Mol Microbiol, vol.45, issue.6, pp.1499-513, 2002.

A. B. Granok, The RofA binding site in Streptococcus pyogenes is utilized in multiple transcriptional pathways, J Bacteriol, vol.182, issue.6, pp.1529-1569, 2000.

R. Grifantini, Peroxide stimulon and role of PerR in group A Streptococcus, J Bacteriol, vol.193, issue.23, pp.6539-51, 2011.

H. Gutekunst, B. J. Eikmanns, and D. J. Reinscheid, Analysis of RogB-controlled virulence mechanisms and gene repression in Streptococcus agalactiae, Infect Immun, vol.71, issue.9, pp.5056-64, 2003.

H. Gutekunst, B. J. Eikmanns, and D. J. Reinscheid, The novel fibrinogen-binding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells, Infect Immun, vol.72, issue.6, pp.3495-504, 2004.

P. S. Handley, P. L. Carter, and J. Fielding, Streptococcus salivarius strains carry either fibrils or fimbriae on the cell surface, J Bacteriol, vol.157, issue.1, pp.64-72, 1984.

L. H. Harrison, D. M. Dwyer, and J. A. Johnson, Emergence of serotype V group B streptococcal infection among infants and adults, J Infect Dis, vol.171, issue.2, p.513, 1995.

C. Hemsley, MgrA, an orthologue of Mga, Acts as a transcriptional repressor of the genes within the rlrA pathogenicity islet in Streptococcus pneumoniae, J Bacteriol, vol.185, issue.22, pp.6640-6647, 2003.

A. P. Hendrickx, Expression of two distinct types of pili by a hospital-acquired Enterococcus faecium isolate. Microbiology, pp.3212-3235, 2008.

A. P. Hendrickx, Isopeptide bonds of the major pilin protein BcpA influence pilus structure and bundle formation on the surface of Bacillus cereus, Mol Microbiol, vol.85, issue.1, pp.152-63, 2012.

M. E. Hensler, S. Miyamoto, and V. Nizet, Group B streptococcal beta-hemolysin/cytolysin directly impairs cardiomyocyte viability and function, PLoS One, vol.3, issue.6, p.2446, 2008.

M. E. Hensler, CAMP factor is not essential for systemic virulence of Group B Streptococcus. Microb Pathog, vol.44, pp.84-92, 2008.

K. Hiller, PrediSi: prediction of signal peptides and their cleavage positions, Nucleic Acids Res, vol.32, pp.375-384, 2004.

M. Hilleringmann, Pneumococcal pili are composed of protofilaments exposing adhesive clusters of Rrg A, PLoS Pathog, vol.4, issue.3, p.1000026, 2008.

T. Hiramune, Phase variation of pili of Corynebacterium pilosum, Zentralbl Veterinarmed B, vol.38, issue.4, pp.303-308, 1991.

E. Honda and R. Yanagawa, Attachment of Corynebacterium renale to tissue culture cells by the pili, Am J Vet Res, vol.36, issue.11, pp.1663-1669, 1975.

E. Honda and R. Yanagawa, Pili-mediated attachment of Corynebacterium renale to mucous membrane of urinary bladder of mice, Am J Vet Res, vol.39, issue.1, pp.155-163, 1978.

T. A. Hooven, The essential genome of Streptococcus agalactiae, BMC Genomics, vol.17, p.406, 2016.

M. Isaka, The YvqE two-component system controls biofilm formation and acid production in Streptococcus pyogenes, APMIS, vol.124, issue.7, pp.574-85, 2016.

H. Ito, E. Ono, and R. Yanagawa, Comparison of surface hydrophobicity of piliated and nonpiliated clones of Corynebacterium renale and Corynebacterium pilosum, Vet Microbiol, vol.14, issue.2, pp.165-71, 1987.

N. S. Jakubovics, S. A. Yassin, and A. H. Rickard, Community interactions of oral streptococci

, Adv Appl Microbiol, vol.87, pp.43-110, 2014.

S. M. Jiang, Regulation of virulence by a two-component system in group B streptococcus, J Bacteriol, vol.187, issue.3, pp.1105-1118, 2005.

S. Jiang, Regulation and function of pilus island 1 in group B streptococcus, J Bacteriol, vol.194, issue.10, pp.2479-90, 2012.

C. H. Jones, FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae, Proc Natl Acad Sci, vol.92, issue.6, pp.2081-2086, 1995.

N. Jones, Multilocus sequence typing system for group B streptococcus, J Clin Microbiol, vol.41, issue.6, pp.2530-2536, 2003.

N. Jones, Enhanced invasiveness of bovine-derived neonatal sequence type 17 group B streptococcus is independent of capsular serotype, Clin Infect Dis, vol.42, issue.7, pp.915-939, 2006.

H. J. Jørgensen, Streptococcus agalactiae in the environment of bovine dairy herdsrewriting the textbooks?, Vet Microbiol, vol.184, pp.64-72, 2016.

J. K. Kajfasz, Transcription of Oxidative Stress Genes Is Directly Activated by SpxA1 and, to a Lesser Extent, by SpxA2 in Streptococcus mutans, J Bacteriol, vol.197, issue.13, pp.2160-70, 2015.

H. J. Kang and E. N. Baker, Intramolecular isopeptide bonds give thermodynamic and proteolytic stability to the major pilin protein of Streptococcus pyogenes, Infect Immun, vol.73, issue.6, pp.3342-50, 2005.

M. C. Lamy, Rapid detection of the "highly virulent" group B Streptococcus ST-17 clone, Microbes Infect, vol.8, issue.7, pp.1714-1736, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00084738

M. C. Lamy, CovS/CovR of group B streptococcus: a two-component global regulatory system involved in virulence, Mol Microbiol, vol.54, issue.5, pp.1250-68, 2004.
URL : https://hal.archives-ouvertes.fr/hal-00019892

R. C. Lancefield, A Serological Differentiation of Human and Other Groups of Hemolytic Streptococci, J Exp Med, vol.57, issue.4, pp.571-95, 1933.

R. C. Lancefield and E. H. Freimer, Type-specific polysaccharide antigens of group B streptococci, J Hyg, vol.64, issue.2, pp.191-203, 1966.

R. C. Lancefield and R. Hare, The Serological Differentiation of Pathogenic and NonPathogenic Strains of Hemolytic Streptococci from Parturient Women, J Exp Med, vol.61, issue.3, pp.335-384, 1935.

S. Landwehr-kenzel and P. Henneke, Interaction of Streptococcus agalactiae and Cellular Innate Immunity in Colonization and Disease. Front Immunol, vol.5, p.519, 2014.

M. F. Lartigue, Variability of neuD transcription levels and capsular sialic acid expression among serotype III group B Streptococcus strains. Microbiology, pp.3282-91, 2011.

P. Lauer, Genome analysis reveals pili in Group B Streptococcus. Science, vol.309, p.105, 2005.

M. Lazzarin, Noncanonical sortase-mediated assembly of pilus type 2b in group B Streptococcus, FASEB J, vol.29, issue.11, pp.4629-4669, 2015.

C. Lembke, Characterization of biofilm formation by clinically relevant serotypes of group A streptococci, Appl Environ Microbiol, vol.72, issue.4, pp.2864-75, 2006.

A. Lembo, Regulation of CovR expression in Group B Streptococcus impacts bloodbrain barrier penetration, Mol Microbiol, vol.77, issue.2, pp.431-474, 2010.

P. Lemire, Role of capsular polysaccharide in Group B Streptococccus interactions with dendritic cells. Microbes Infect, vol.14, pp.1064-76, 2012.

P. Lemire, M. Houde, and M. Segura, Encapsulated group B Streptococcus modulates dendritic cell functions via lipid rafts and clathrin-mediated endocytosis, Cell Microbiol, vol.14, issue.11, pp.1707-1726, 2012.

F. Levent, Early outcomes of group B streptococcal meningitis in the 21st century

, Pediatr Infect Dis J, vol.29, issue.11, pp.1009-1021, 2010.

C. Lier, Analysis of the type II-A CRISPR-Cas system of Streptococcus agalactiae reveals Microbiol, vol.43, pp.3727-3760, 2005.

F. Luo, S. Lizano, and D. E. Bessen, Heterogeneity in the polarity of Nra regulatory effects on streptococcal pilus gene transcription and virulence, Infect Immun, vol.76, issue.6, pp.2490-2497, 2008.

L. C. Madoff, Phenotypic diversity in the alpha C protein of group B streptococci, Infect Immun, vol.59, issue.8, pp.2638-2682, 1991.

J. A. Maeland, Survey of immunological features of the alpha-like proteins of Streptococcus agalactiae, Clin Vaccine Immunol, vol.22, issue.2, pp.153-162, 2015.

V. Magalhães, Group B Streptococcus hijacks the host plasminogen system to promote brain endothelial cell invasion, PLoS One, vol.8, issue.5, p.63244, 2013.

H. C. Maisey, A group B streptococcal pilus protein promotes phagocyte resistance and systemic virulence, FASEB J, vol.22, issue.6, pp.1715-1739, 2008.

A. Mandlik, Corynebacterium diphtheriae employs specific minor pilins to target human pharyngeal epithelial cells, Mol Microbiol, vol.64, issue.1, pp.111-135, 2007.

A. Mandlik, Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development, Trends Microbiol, vol.16, issue.1, pp.33-40, 2008.

A. G. Manetti, Environmental acidification drives S. pyogenes pilus expression and microcolony formation on epithelial cells in a FCT-dependent manner, PLoS One, vol.5, issue.11, 2010.

A. G. Manetti, Identification of CiaR Regulated Genes That Promote Group B Streptococcal Virulence and Interaction with Brain Endothelial Cells, PLoS One, vol.11, issue.4, p.153891, 2016.

R. Mu, Identification of a group B streptococcal fibronectin binding protein, SfbA, that contributes to invasion of brain endothelium and development of meningitis, Infect Immun, vol.82, issue.6, pp.2276-86, 2014.

M. Nakata, Mode of expression and functional characterization of FCT-3 pilus regionencoded proteins in Streptococcus pyogenes serotype M49, Infect Immun, vol.77, issue.1, pp.32-44, 2009.

M. Nakata, A. Podbielski, and B. Kreikemeyer, MsmR, a specific positive regulator of the Streptococcus pyogenes FCT pathogenicity region and cytolysin-mediated translocation system genes, Mol Microbiol, vol.57, issue.3, pp.786-803, 2005.
DOI : 10.1111/j.1365-2958.2005.04730.x

S. R. Nallapareddy, Conservation of Ebp-type pilus genes among Enterococci and demonstration of their role in adherence of Enterococcus faecalis to human platelets, Infect Immun, vol.79, issue.7, pp.2911-2931, 2011.

A. L. Nelson, RrgA is a pilus-associated adhesin in Streptococcus pneumoniae, Mol Microbiol, vol.66, issue.2, pp.329-369, 2007.
DOI : 10.1111/j.1365-2958.2007.05908.x

URL : http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2007.05908.x/pdf

A. H. Nobbs, Sortase A utilizes an ancillary protein anchor for efficient cell wall anchoring of pili in Streptococcus agalactiae, Infect Immun, vol.76, issue.8, pp.3550-60, 2008.

N. and M. R. , Sur une mammite contagieuse des vaches laitieres, Annales de l'Institut Pasteur, 1887, vol.1, issue.1, p.17

O. Higgins and A. C. , A clinical review of maternal bacteremia, Int J Gynaecol Obstet, vol.124, issue.3, pp.226-235, 2014.

N. Okahashi, Pili of oral Streptococcus sanguinis bind to salivary amylase and promote the biofilm formation, Microb Pathog, vol.50, issue.3-4, pp.148-54, 2011.

S. Orrskog, Pilus adhesin RrgA interacts with complement receptor 3, thereby affecting macrophage function and systemic pneumococcal disease, MBio, vol.4, issue.1, pp.535-547, 2012.
DOI : 10.1128/mbio.00535-12

URL : https://mbio.asm.org/content/4/1/e00535-12.full.pdf

H. Pailhories, R. Quentin, and M. F. Lartigue, The transcription of the neuD gene is stronger in serotype III group B streptococci strains isolated from cerebrospinal fluid than in strains isolated from vagina, FEMS Microbiol Lett, vol.349, issue.1, pp.71-76, 2013.

R. J. Palmer, Coaggregation-mediated interactions of streptococci and actinomyces detected in initial human dental plaque, J Bacteriol, vol.185, issue.11, pp.3400-3409, 2003.

L. C. Paoletti, R. A. Ross, and K. D. Johnson, Cell growth rate regulates expression of group B Streptococcus type III capsular polysaccharide, Infect Immun, vol.64, issue.4, pp.1220-1226, 1996.

L. J. Paoletti, J. Bradford, and L. C. Paoletti, A serotype VIII strain among colonizing group B streptococcal isolates in, J Clin Microbiol, vol.37, issue.11, pp.3759-60, 1999.

S. Papasergi, The GBS PI-2a pilus is required for virulence in mice neonates, PLoS One, vol.6, issue.4, p.18747, 2011.
URL : https://hal.archives-ouvertes.fr/hal-01190509

S. Papasergi, Analysis of the Streptococcus agalactiae exoproteome, J Proteomics, vol.89, pp.154-64, 2013.
URL : https://hal.archives-ouvertes.fr/pasteur-01300162

S. E. Park, S. Jiang, and M. R. Wessels, CsrRS and environmental pH regulate group B streptococcus adherence to human epithelial cells and extracellular matrix, Infect Immun, vol.80, issue.11, pp.3975-84, 2012.

R. E. Parker, Association between genotypic diversity and biofilm production in group B Streptococcus, BMC Microbiol, vol.16, p.86, 2016.
DOI : 10.1186/s12866-016-0704-9

URL : https://bmcmicrobiol.biomedcentral.com/track/pdf/10.1186/s12866-016-0704-9

J. M. Patti and M. Höök, Microbial adhesins recognizing extracellular matrix macromolecules
DOI : 10.1016/0955-0674(94)90104-x

, Curr Opin Cell Biol, vol.6, issue.5, pp.752-760, 1994.

D. Pérez-pascual, RovS and its associated signaling peptide form a cell-to-cell communication system required for Streptococcus agalactiae pathogenesis, MBio, issue.6, 2015.

B. Périchon, Regulation of PI-2b Pilus Expression in Hypervirulent Streptococcus agalactiae ST-17 BM110, PLoS One, vol.12, issue.1, p.169840, 2017.

T. N. Petersen, SignalP 4.0: discriminating signal peptides from transmembrane regions, Nat Methods, vol.8, issue.10, pp.785-791, 2011.

A. Pezzicoli, Pilus backbone contributes to group B Streptococcus paracellular translocation through epithelial cells, J Infect Dis, vol.198, issue.6, pp.890-898, 2008.

M. Pierno, FbsA-driven fibrinogen polymerization: a bacterial "deceiving strategy, Phys Rev Lett, vol.96, issue.2, p.28108, 2006.

G. Pietrocola, FbsA, a fibrinogen-binding protein from Streptococcus agalactiae, mediates platelet aggregation, Blood, vol.105, issue.3, pp.1052-1061, 2005.

G. C. Port, SpxA1 and SpxA2 Act Coordinately To Fine-Tune Stress Responses and Virulence in Streptococcus pyogenes, MBio, vol.8, issue.2, 2017.

C. Poyart, Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus agalactiae involves a novel two-component regulatory system, J Bacteriol, vol.183, issue.21, pp.6324-6358, 2001.

C. Poyart, Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae, Infect Immun, vol.69, issue.8, pp.5098-106, 2001.

C. Poyart, Attenuated virulence of Streptococcus agalactiae deficient in D-alanyllipoteichoic acid is due to an increased susceptibility to defensins and phagocytic cells, Mol Microbiol, vol.49, issue.6, pp.1615-1640, 2003.

C. Poyart, Characterization of the Tn916-like transposon Tn3872 in a strain of abiotrophia defectiva (Streptococcus defectivus) causing sequential episodes of endocarditis in a child, Antimicrob Agents Chemother, vol.44, issue.3, pp.790-793, 2000.

D. G. Pritchard, B. M. Gray, and H. C. Dillon, Characterization of the group-specific polysaccharide of group B Streptococcus, Arch Biochem Biophys, vol.235, issue.2, pp.385-92, 1984.

C. A. Pritzlaff, Genetic basis for the beta-haemolytic/cytolytic activity of group B Streptococcus, Mol Microbiol, vol.39, issue.2, pp.236-283, 2001.

D. Quach, The CiaR response regulator in group B Streptococcus promotes intracellular survival and resistance to innate immune defenses, J Bacteriol, vol.191, issue.7, pp.2023-2055, 2009.

P. Ragunathan, Metal binding is critical for the folding and function of laminin binding protein, Lmb of Streptococcus agalactiae, PLoS One, vol.8, issue.6, p.67517, 2013.

L. Rajagopal, Understanding the regulation of Group B Streptococcal virulence factors

, Future Microbiol, vol.4, issue.2, pp.201-222, 2009.

L. Rajagopal, Regulation of cytotoxin expression by converging eukaryotic-type and two-component signalling mechanisms in Streptococcus agalactiae, Mol Microbiol, vol.62, issue.4, pp.941-57, 2006.

A. Reiss, Bacterial pore-forming cytolysins induce neuronal damage in a rat model of neonatal meningitis, J Infect Dis, vol.203, issue.3, pp.393-400, 2011.

V. P. Richards, Comparative genomics and the role of lateral gene transfer in the evolution of bovine adapted Streptococcus agalactiae, Infect Genet Evol, vol.11, issue.6, pp.1263-75, 2011.
URL : https://hal.archives-ouvertes.fr/halsde-00623049

C. D. Rinaudo, Specific involvement of pilus type 2a in biofilm formation in group B Streptococcus, PLoS One, vol.5, issue.2, p.9216, 2010.

J. Rodriguez-granger, Non-haemolytic and non-pigmented group b streptococcus, an infrequent cause of early onset neonatal sepsis, vol.73, p.89, 2015.

M. Rosa-fraile, S. Dramsi, and B. Spellerberg, Group B streptococcal haemolysin and pigment, a tale of twins, FEMS Microbiol Rev, vol.38, issue.5, pp.932-978, 2014.

M. Rosa-fraile, Identification of serum and urine proteins responsible for enhanced pigment production by group B streptococci as amylases, Clin Diagn Lab Immunol, vol.3, issue.5, pp.594-600, 1996.

J. W. Rosch, Convergence of regulatory networks on the pilus locus of Streptococcus pneumoniae, vol.76, pp.3187-96, 2008.

R. Rosini, Identification of novel genomic islands coding for antigenic pilus-like structures in Streptococcus agalactiae, Mol Microbiol, vol.61, issue.1, pp.126-167, 2006.

I. Rosinski-chupin, Reductive evolution in Streptococcus agalactiae and the emergence of a host adapted lineage, BMC Genomics, vol.14, p.252, 2013.
URL : https://hal.archives-ouvertes.fr/pasteur-00818470

R. A. Ross, L. C. Madoff, and L. C. Paoletti, Regulation of cell component production by growth rate in the group B Streptococcus, J Bacteriol, vol.181, issue.17, pp.5389-94, 1999.

C. E. Rubens, Identification of cpsD, a gene essential for type III capsule expression in group B streptococci, Mol Microbiol, vol.8, issue.5, pp.843-55, 1993.

C. E. Rubens, Transposon mutagenesis of type III group B Streptococcus: correlation of capsule expression with virulence, Proc Natl Acad Sci, vol.84, pp.7208-7220, 1920.

R. Saar-dover, D-alanylation of lipoteichoic acids confers resistance to cationic peptides in group B streptococcus by increasing the cell wall density, PLoS Pathog, vol.8, issue.9, 2012.
URL : https://hal.archives-ouvertes.fr/pasteur-01300170

M. Salloum, Diversity of prophage DNA regions of Streptococcus agalactiae clonal lineages from adults and neonates with invasive infectious disease, PLoS One, vol.6, issue.5, p.p, 2011.

U. Samen, Rga is a regulator of adherence and pilus formation in Streptococcus agalactiae. Microbiology, pp.2319-2346, 2011.

I. Santi, CsrRS regulates group B Streptococcus virulence gene expression in response to environmental pH: a new perspective on vaccine development, J Bacteriol, vol.191, issue.17, 2009.

I. Santi, BibA induces opsonizing antibodies conferring in vivo protection against group B Streptococcus, J Infect Dis, vol.200, issue.4, pp.564-70, 2009.

I. Santi, BibA: a novel immunogenic bacterial adhesin contributing to group B Streptococcus survival in human blood, Mol Microbiol, vol.63, issue.3, pp.754-67, 2007.

A. Schubert, The fibrinogen receptor FbsA promotes adherence of Streptococcus agalactiae to human epithelial cells, Infect Immun, vol.72, issue.11, pp.6197-205, 2004.

A. Schubert, A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites, Mol Microbiol, vol.46, issue.2, pp.557-69, 2002.

A. Schuchat, Group B streptococcus, Lancet, vol.353, issue.9146, pp.51-57, 1999.

J. R. Scott and D. Zähner, Pili with strong attachments: Gram-positive bacteria do it differently, Mol Microbiol, vol.62, issue.2, pp.320-350, 2006.

H. S. Seo, Characterization of fibrinogen binding by glycoproteins Srr1 and Srr2 of Streptococcus agalactiae, J Biol Chem, vol.288, issue.50, pp.35982-96, 2013.

H. S. Seo, Binding of glycoprotein Srr1 of Streptococcus agalactiae to fibrinogen promotes attachment to brain endothelium and the development of meningitis, PLoS Pathog, vol.8, issue.10, p.1002947, 2012.

H. S. Seo, Y. Q. Xiong, and P. M. Sullam, Role of the serine-rich surface glycoprotein Srr1 of Streptococcus agalactiae in the pathogenesis of infective endocarditis, PLoS One, vol.8, issue.5, p.64204, 2013.

P. Sharma, Role of pilus proteins in adherence and invasion of Streptococcus agalactiae to the lung and cervical epithelial cells, J Biol Chem, vol.288, issue.6, pp.4023-4057, 2013.

T. R. Sheen, Serine-rich repeat proteins and pili promote Streptococcus agalactiae colonization of the vaginal tract, J Bacteriol, vol.193, issue.24, pp.6834-6876, 2011.

S. D. Siegel, C. Wu, and H. Ton-that, A Type I Signal Peptidase Is Required for Pilus Assembly in the Gram-Positive, Biofilm-Forming Bacterium Actinomyces oris, J Bacteriol, vol.198, issue.15, pp.2064-73, 2016.

J. Sillanpää, A collagen-binding adhesin, Acb, and ten other putative MSCRAMM and pilus family proteins of Streptococcus gallolyticus subsp. gallolyticus (Streptococcus bovis Group, biotype I), J Bacteriol, vol.191, issue.21, pp.6643-53, 2009.

A. Six, Srr2, a multifaceted adhesin expressed by ST-17 hypervirulent Group B Streptococcus involved in binding to both fibrinogen and plasminogen, Mol Microbiol, vol.97, issue.6, pp.1209-1231, 2015.
URL : https://hal.archives-ouvertes.fr/pasteur-01299767

A. Six, Molecular Characterization of Nonhemolytic and Nonpigmented Group B
URL : https://hal.archives-ouvertes.fr/pasteur-01288318

, Streptococci Responsible for Human Invasive Infections, J Clin Microbiol, vol.54, issue.1, pp.75-82, 2016.

B. Spellerberg, Identification of genetic determinants for the hemolytic activity of Streptococcus agalactiae by ISS1 transposition, J Bacteriol, vol.181, issue.10, pp.3212-3221, 1999.

B. Spellerberg, Lmb, a protein with similarities to the LraI adhesin family, mediates attachment of Streptococcus agalactiae to human laminin, Infect Immun, vol.67, issue.2, pp.1482-91, 1998.

M. K. Yeung and P. A. Ragsdale, Synthesis and function of Actinomyces naeslundii T14V type 1

, fimbriae require the expression of additional fimbria-associated genes, Infect Immun, vol.65, issue.7, pp.2629-2668, 1997.

P. G. Young, Structural conservation, variability, and immunogenicity of the T6 backbone pilin of serotype M6 Streptococcus pyogenes, Infect Immun, vol.82, issue.7, pp.2949-57, 2014.

P. G. Young, Structure and activity of Streptococcus pyogenes SipA: a signal peptidaselike protein essential for pilus polymerisation, PLoS One, vol.9, issue.6, p.99135, 2014.

D. Zähner and J. R. Scott, SipA is required for pilus formation in Streptococcus pyogenes serotype M3, J Bacteriol, vol.190, issue.2, pp.527-562, 2008.

K. M. Zangwill, A. Schuchat, and J. D. Wenger, report from a multistate active surveillance system, Group B streptococcal disease in the United States, vol.41, pp.25-32, 1990.

C. Zheng, Two Spx regulators modulate stress tolerance and virulence in Streptococcus suis serotype 2, PLoS One, vol.9, issue.9, p.108197, 2014.

Y. Zong, A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen

, EMBO J, vol.24, issue.24, pp.4224-4260, 2005.