C. A. Fux, J. W. Costerton, P. S. Stewart, and P. Stoodley, Survival strategies of infectious biofilms, Trends in Microbiology, vol.13, issue.1, pp.34-40, 2005.
DOI : 10.1016/j.tim.2004.11.010

A. Mandlik, A. Swierczynski, A. Das, and H. Ton-that, Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development, Trends in Microbiology, vol.16, issue.1, pp.33-40, 2008.
DOI : 10.1016/j.tim.2007.10.010

J. W. Costerton, P. S. Stewart, E. P. Greenberg, R. J. Lamont, and H. F. Jenkinson, Bacterial Biofilms: A Common Cause of Persistent Infections, Science, vol.284, issue.5418, pp.407-450, 1999.
DOI : 10.1126/science.284.5418.1318

J. Kreth, J. Merritt, and F. Qi, Bacterial and Host Interactions of Oral Streptococci, DNA and Cell Biology, vol.28, issue.8, pp.397-403, 2009.
DOI : 10.1089/dna.2009.0868

S. Paju and F. A. Scannapieco, Oral biofilms, periodontitis, and pulmonary infections, Oral Diseases, vol.38, issue.6, pp.508-512, 2007.
DOI : 10.1046/j.1532-5415.2002.50106.x

F. A. Scannapieco, R. B. Bush, and S. Paju, Associations Between Periodontal Disease and Risk for Atherosclerosis, Cardiovascular Disease, and Stroke. A Systematic Review, Annals of Periodontology, vol.8, issue.1, pp.38-53, 2003.
DOI : 10.1902/annals.2003.8.1.38

S. Fujitani, M. C. Rowlinson, G. , and W. L. , Penicillin G???Resistant Viridans Group Streptococcal Endocarditis and Interpretation of the American Heart Association's Guidelines for the Treatment of Infective Endocarditis, Clinical Infectious Diseases, vol.46, issue.7, pp.1064-1066, 2008.
DOI : 10.1086/529199

E. Giannitsioti, C. Chirouze, A. Bouvet, I. Beguinot, F. Delahaye et al., Characteristics and regional variations of group D streptococcal endocarditis in France, Clinical Microbiology and Infection, vol.13, issue.8, pp.770-776, 2007.
DOI : 10.1111/j.1469-0691.2007.01753.x

URL : https://hal.archives-ouvertes.fr/hal-00465359

K. Westling, I. Julander, P. Ljungman, S. Jalal, C. E. Nord et al., Viridans group streptococci in blood culture isolates in a Swedish university hospital: antibiotic susceptibility and identification of erythromycin resistance genes, International Journal of Antimicrobial Agents, vol.28, issue.4, pp.292-296, 2006.
DOI : 10.1016/j.ijantimicag.2006.05.032

A. E. Stephenson, H. Wu, J. Novak, M. Tomana, K. Mintz et al., The Fap1 fimbrial adhesin is a glycoprotein: antibodies specific for the glycan moiety block the adhesion of Streptococcus parasanguis in an in vitro tooth model, Molecular Microbiology, vol.43, issue.1, pp.147-157, 2002.
DOI : 10.1016/0300-9084(88)90286-6

H. Wu and P. M. Fives-taylor, Identification of dipeptide repeats and a cell wall sorting signal in the fimbriae-associated adhesin, Fap1, of Streptococcus parasanguis, Molecular Microbiology, vol.66, issue.5, pp.1070-1081, 1999.
DOI : 10.1046/j.1365-2958.1998.00805.x

H. Wu, K. P. Mintz, M. Ladha, and P. M. Fives-taylor, Isolation and characterization of Fap1, a fimbriae-associated adhesin of Streptococcus parasanguis FW213, Molecular Microbiology, vol.28, issue.3, pp.487-500, 1998.
DOI : 10.1016/0022-1759(85)90337-0

Y. Q. Xiong, B. A. Bensing, A. S. Bayer, H. F. Chambers, and P. M. Sullam, Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis, Microbial Pathogenesis, vol.45, issue.4, pp.297-301, 2008.
DOI : 10.1016/j.micpath.2008.06.004

P. Shivshankar, C. Sanchez, L. F. Rose, and C. J. Orihuela, adhesin PsrP binds to Keratin 10 on lung cells, Molecular Microbiology, vol.155, issue.4, pp.663-679, 2009.
DOI : 10.1111/j.1365-2958.2009.06796.x

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2753542

M. Y. Mistou, S. Dramsi, S. Brega, C. Poyart, and P. Trieu-cuot, Molecular Dissection of the secA2 Locus of Group B Streptococcus Reveals that Glycosylation of the Srr1 LPXTG Protein Is Required for Full Virulence, Journal of Bacteriology, vol.191, issue.13, pp.4195-4206, 2009.
DOI : 10.1128/JB.01673-08

M. Sattler, J. Schleucher, and C. Griesinger, Progress in NMR Spectroscropy, pp.93-158, 1999.

M. Ottiger, F. Delaglio, and A. Bax, Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR Spectra, Journal of Magnetic Resonance, vol.131, issue.2, pp.373-378, 1998.
DOI : 10.1006/jmre.1998.1361

K. Pervushin, R. Riek, G. Wider, and K. Wuthrich, Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution, Proceedings of the National Academy of Sciences, vol.40, issue.6, pp.12366-12371, 1997.
DOI : 10.1007/BF02192855

B. A. Johnson and R. A. Blevins, NMR View: A computer program for the visualization and analysis of NMR data, Journal of Biomolecular NMR, vol.88, issue.5, pp.603-614, 1994.
DOI : 10.1007/BF00404272

B. Bardiaux, A. Bernard, W. Rieping, M. Habeck, T. E. Malliavin et al., Influence of different assignment conditions on the determination of symmetric homodimeric structures with ARIA, Proteins: Structure, Function, and Bioinformatics, vol.121, issue.Part 5, pp.569-585, 2009.
DOI : 10.1002/prot.22268

W. Rieping, M. Habeck, B. Bardiaux, A. Bernard, T. E. Malliavin et al., ARIA2: Automated NOE assignment and data integration in NMR structure calculation, Bioinformatics, vol.23, issue.3, pp.381-382, 2007.
DOI : 10.1093/bioinformatics/btl589

URL : http://citeseerx.ist.psu.edu/viewdoc/summary?doi=

A. T. Brunger, P. D. Adams, G. M. Clore, W. L. Delano, P. Gros et al., Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, Acta Crystallographica Section D Biological Crystallography, vol.54, issue.5, pp.905-921, 1998.
DOI : 10.1107/S0907444998003254

G. M. Clore, A. M. Gronenborn, and A. Bax, A Robust Method for Determining the Magnitude of the Fully Asymmetric Alignment Tensor of Oriented Macromolecules in the Absence of Structural Information, Journal of Magnetic Resonance, vol.133, issue.1, pp.216-221, 1998.
DOI : 10.1006/jmre.1998.1419

M. Nilges, A. Bernard, B. Bardiaux, T. Malliavin, M. Habeck et al., Accurate NMR Structures Through Minimization of an Extended Hybrid Energy, Structure, vol.16, issue.9, pp.1305-1312, 2008.
DOI : 10.1016/j.str.2008.07.008

P. Emsley and K. Cowtan, : model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2132, 2004.
DOI : 10.1107/S0907444904019158

G. N. Murshudov, A. A. Vagin, and E. J. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-255, 1997.
DOI : 10.1107/S0907444996012255

P. V. Konarev, V. V. Volkov, A. V. Sokolova, M. H. Koch, and D. I. Svergun, : a Windows PC-based system for small-angle scattering data analysis, Journal of Applied Crystallography, vol.36, issue.5, pp.1277-1282, 2003.
DOI : 10.1107/S0021889803012779

M. V. Petoukhov and D. I. Svergun, New methods for domain structure determination of proteins from solution scattering data, Journal of Applied Crystallography, vol.36, issue.3, pp.540-544, 2003.
DOI : 10.1107/S0021889803000591

W. Wriggers and P. Chacon, for the registration of protein structures??with low-resolution bead models from??X-ray solution scattering, Journal of Applied Crystallography, vol.34, issue.6, pp.773-776, 2001.
DOI : 10.1107/S0021889801012869

T. Ruiz, I. Mechin, J. Bar, W. Rypniewski, G. Kopperschlager et al., The 10.8-?? structure of Saccharomyces cerevisiae phosphofructokinase determined by cryoelectron microscopy: localization of the putative fructose 6-phosphate binding sites, Journal of Structural Biology, vol.143, issue.2, pp.124-134, 2003.
DOI : 10.1016/S1047-8477(03)00140-0

URL : https://hal.archives-ouvertes.fr/hal-00129132

J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y. H. Li et al., SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields, Journal of Structural Biology, vol.116, issue.1, pp.190-199, 1996.
DOI : 10.1006/jsbi.1996.0030

M. Radermacher, T. Ruiz, H. Wieczorek, and G. Gruber, The Structure of the V1-ATPase Determined by Three-Dimensional Electron Microscopy of Single Particles, Journal of Structural Biology, vol.135, issue.1, pp.26-37, 2001.
DOI : 10.1006/jsbi.2001.4395

S. J. Ludtke, P. R. Baldwin, and W. Chiu, EMAN: Semiautomated Software for High-Resolution Single-Particle Reconstructions, Journal of Structural Biology, vol.128, issue.1, pp.82-97, 1999.
DOI : 10.1006/jsbi.1999.4174

C. Plummer, H. Wu, S. W. Kerrigan, G. Meade, D. Cox et al., A serine-rich glycoprotein of Streptococcus sanguis mediates adhesion to platelets via GPIb, British Journal of Haematology, vol.65, issue.1, pp.101-109, 2005.
DOI : 10.1046/j.1365-2958.1998.00805.x

D. Takamatsu, B. A. Bensing, H. Cheng, G. A. Jarvis, I. R. Siboo et al., surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ib??, Molecular Microbiology, vol.34, issue.2, pp.380-392, 2005.
DOI : 10.1111/j.1365-2958.2005.04830.x

H. Wu, S. Bu, P. Newell, Q. Chen, and P. Fives-taylor, Two Gene Determinants Are Differentially Involved in the Biogenesis of Fap1 Precursors in Streptococcus parasanguis, Journal of Bacteriology, vol.189, issue.4, pp.1390-1398, 2007.
DOI : 10.1128/JB.00836-06

R. Fronzes, H. Remaut, and G. Waksman, Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria, The EMBO Journal, vol.39, issue.17, pp.2271-2280, 2008.
DOI : 10.1038/emboj.2008.155

M. G. Bowden, A. P. Heuck, K. Ponnuraj, E. Kolosova, D. Choe et al., Evidence for the "Dock, Lock, and Latch" Ligand Binding Mechanism of the Staphylococcal Microbial Surface Component Recognizing Adhesive Matrix Molecules (MSCRAMM) SdrG, Journal of Biological Chemistry, vol.283, issue.1, pp.638-647, 2008.
DOI : 10.1074/jbc.M706252200

H. Ton-that and O. Schneewind, Assembly of pili in Gram-positive bacteria, Trends in Microbiology, vol.12, issue.5, pp.228-234, 2004.
DOI : 10.1016/j.tim.2004.03.004

U. Samen, D. J. Reinscheid, D. J. Reinscheid, and F. Borges, The Surface Protein Srr-1 of Streptococcus agalactiae Binds Human Keratin 4 and Promotes Adherence to Epithelial HEp-2 Cells, Infection and Immunity, vol.75, issue.11, pp.5405-5414, 2007.
DOI : 10.1128/IAI.00717-07

H. Wu, M. Zeng, and P. Fives-taylor, The Glycan Moieties and the N-Terminal Polypeptide Backbone of a Fimbria-Associated Adhesin, Fap1, Play Distinct Roles in the Biofilm Development of Streptococcus parasanguinis, Infection and Immunity, vol.75, issue.5, pp.2181-2188, 2001.
DOI : 10.1128/IAI.01544-06

M. D. Shoulders and R. T. Raines, Collagen Structure and Stability, Annual Review of Biochemistry, vol.78, issue.1, pp.929-958, 2009.
DOI : 10.1146/annurev.biochem.77.032207.120833

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2846778

T. Asakura, K. Ohgo, K. Komatsu, M. Kanenari, and K. Okuyama, C Solid-State NMR and X-ray Diffraction Methods, Macromolecules, vol.38, issue.17, pp.7397-7403, 2005.
DOI : 10.1021/ma050936y

M. Sangappa, S. S. Somashekar, and R. , Crystal structure of raw pure Mysore silk fibre based on (Ala-Gly)2-Ser-Gly peptide sequence using Linked-Atom-Least-Squares method, Journal of Biosciences, vol.24, issue.2, pp.259-268, 2005.
DOI : 10.1007/BF02703707

M. L. Plassmeyer, K. Reiter, R. L. Shimp, S. Kotova, P. D. Smith et al., Structure of the Plasmodium falciparum Circumsporozoite Protein, a Leading Malaria Vaccine Candidate, Journal of Biological Chemistry, vol.284, issue.39, pp.26951-26963, 2009.
DOI : 10.1074/jbc.M109.013706

P. S. Handley, F. F. Correia, K. Russell, B. Rosan, and J. M. Dirienzo, Association of a novel high molecular weight, serine-rich protein (SrpA) with fibril-mediated adhesion of the oral biofilm bacterium Streptococcus cristatus, Oral Microbiology and Immunology, vol.165, issue.3, pp.131-140, 2005.
DOI : 10.1046/j.1365-2958.1999.01670.x

M. Hilleringmann, P. Ringler, S. A. Muller, G. De-angelis, R. Rappuoli et al., Molecular architecture of Streptococcus pneumoniae TIGR4 pili, The EMBO Journal, vol.15, issue.24, pp.3921-3930, 2009.
DOI : 10.1128/JB.01808-06

L. A. Kelley and M. J. Sternberg, Protein structure prediction on the Web: a case study using the Phyre server, Nature Protocols, vol.5, issue.3, pp.363-371, 2009.
DOI : 10.1093/nar/gkm977

L. Holm, S. Kaariainen, P. Rosenstrom, and A. Schenkel, Searching protein structure databases with DaliLite v.3, Bioinformatics, vol.24, issue.23, pp.2780-2781, 2008.
DOI : 10.1093/bioinformatics/btn507

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2639270

K. Ponnuraj, M. G. Bowden, S. Davis, S. Gurusiddappa, D. Moore et al., A ???dock, lock, and latch??? Structural Model for a Staphylococcal Adhesin Binding to Fibrinogen, Cell, vol.115, issue.2, pp.217-228, 2003.
DOI : 10.1016/S0092-8674(03)00809-2

Q. Liu, K. Ponnuraj, Y. Xu, V. K. Ganesh, J. Sillanpaa et al., The Enterococcus faecalis MSCRAMM ACE Binds Its Ligand by the Collagen Hug Model, Journal of Biological Chemistry, vol.282, issue.27, pp.19629-19637, 2007.
DOI : 10.1074/jbc.M611137200

C. C. Deivanayagam, E. R. Wann, W. Chen, M. Carson, K. R. Rajashankar et al., A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A, The EMBO Journal, vol.21, issue.24, pp.6660-6672, 2002.
DOI : 10.1093/emboj/cdf619

Y. Tanaka, S. Sakamoto, M. Kuroda, S. Goda, Y. G. Gao et al., A Helical String of Alternately Connected Three-Helix Bundles for the Cell Wall-Associated Adhesion Protein Ebh from Staphylococcus aureus, Structure, vol.16, issue.3, pp.488-496, 2008.
DOI : 10.1016/j.str.2007.12.018

N. Takahashi and T. Yamada, Acid-induced acid tolerance and acidogenicity of non-mutans streptococci, Oral Microbiology and Immunology, vol.70, issue.1, pp.43-48, 1999.
DOI : 10.1016/0003-9969(90)90054-E

J. Welin-neilands and G. Svensater, Acid Tolerance of Biofilm Cells of Streptococcus mutans, Applied and Environmental Microbiology, vol.73, issue.17, pp.5633-5638, 2007.
DOI : 10.1128/AEM.01049-07

G. Svensater, U. B. Larsson, E. C. Greif, D. G. Cvitkovitch, H. et al., Acid tolerance response and survival by oral bacteria, Oral Microbiology and Immunology, vol.175, issue.5, pp.266-273, 1997.
DOI : 10.1111/j.1365-2958.1993.tb01198.x

S. Guglielmetti, I. Tamagnini, M. Minuzzo, S. Arioli, C. Parini et al., Study of the Adhesion of Bifidobacterium bifidum MIMBb75 to Human Intestinal Cell Lines, Current Microbiology, vol.48, issue.2, pp.167-172, 2009.
DOI : 10.1007/s00284-009-9415-x

H. O. Ito, S. Soutome, and M. Inoue, Inhibition of fibronectin binding of some bacterial cells by subtle pH increase within the physiological range, Journal of Microbiological Methods, vol.55, issue.1, pp.29-34, 2003.
DOI : 10.1016/S0167-7012(03)00111-8

S. B. Kim, S. J. Park, C. G. Lee, N. C. Choi, K. et al., Bacteria transport through goethite-coated sand: Effects of solution pH and coated sand content, Colloids and Surfaces B: Biointerfaces, vol.63, issue.2, pp.236-242, 2008.
DOI : 10.1016/j.colsurfb.2007.12.003

I. W. Davis, A. Leaver-fay, V. B. Chen, J. N. Block, G. J. Kapral et al., MolProbity: all-atom contacts and structure validation for proteins and nucleic acids, Nucleic Acids Research, vol.35, issue.Web Server, pp.375-383, 2007.
DOI : 10.1093/nar/gkm216

URL : http://doi.org/10.1093/nar/gkm216

R. A. Laskowski, M. W. Macarthur, D. S. Moss, T. , and J. M. , PROCHECK: a program to check the stereochemical quality of protein structures, Journal of Applied Crystallography, vol.26, issue.2, pp.283-291, 1993.
DOI : 10.1107/S0021889892009944

G. Vriend, WHAT IF: A molecular modeling and drug design program, Journal of Molecular Graphics, vol.8, issue.1, p.52, 1990.
DOI : 10.1016/0263-7855(90)80070-V

S. Figure and S. , Gel filtration profile of Fap1-NR performed on a Superdex-75 XK 16/60 column (GE healthcare) The void volume (V o ) and Fap1-NR elution volume are labelled

S. Figure and S. , Superimposition of the 800MHz 15 N-1 H TROSY-HSQC spectra of Fap1 fragments. Fap1-NR shown in black with both 800MHz 1 H-15 N HSQC spectra of Fap1-NR ? and Fap1-NR ? in green and in red respectively at pH 8 and 303K