Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen α

Protein and Cell

Volumn 6, Issue 10, 2015, Pages 757-766

  Zhang, Xinyue ^a   Wu, Meng ^a   Zhuo, Wei ^a   Gu, Jinke ^a   Zhang, Sensen ^a   Ge, Jingpeng ^a   Yang, Maojun ^a  

^a Tsinghua University   (China)

Author keywords

bone sialoprotein binding protein (Bbp); fibrinogen; Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMM); serine aspartate repeat (Sdr); Staphylococcus aureus

Indexed keywords

BINDING PROTEIN; BONE SIALOPROTEIN BINDING PROTEIN; FIBRINOGEN; HYBRID PROTEIN; LIGAND; PEPTIDE; PROTEIN A; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; BONE SIALOPROTEIN-BINDING PROTEIN, STAPHYLOCOCCUS AUREUS; CARRIER PROTEIN; PEPTIDE FRAGMENT; PROTEIN BINDING;

ALPHA HELIX; ARTICLE; BINDING AFFINITY; CHEMICAL MUTAGENESIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; DNA PROTEIN COMPLEX; GENE EXPRESSION; HYDROGEN BOND; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; MOLECULAR CLONING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS INFECTION; SURFACE PLASMON RESONANCE; SYNTHESIS; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR MODEL; MUTATION; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CARRIER PROTEINS; CRYSTALLOGRAPHY, X-RAY; FIBRINOGEN; LIGANDS; MODELS, MOLECULAR; MUTATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STAPHYLOCOCCUS AUREUS;

EID: 84943361374     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-015-0205-x     Document Type: Article

References (34)

1. Adams PD, Grosse-Kunstleve RW, Hung LW, Ioerger TR, McCoy AJ, Moriarty NW, Read RJ, Sacchettini JC, Sauter NK, Terwilliger TC (2002) PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58:1948–1954
2. Davis SL, Gurusiddappa S, McCrea KW, Perkins S, Hook M (2001) SdrG, a fibrinogen-binding bacterial adhesin of the microbial surface components recognizing adhesive matrix molecules subfamily from Staphylococcus epidermidis, targets the thrombin cleavage site in the Bbeta chain. J Biol Chem 276:27799–27805
3. Deivanayagam C, Wann ER, Chen W, Carson M, Rajashankar KR, Höök M, Narayana SV (2002) A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A. EMBO J 21:6660–6672
4. Deresinski S, Herrera V (2010) Immunotherapies for Staphylococcus aureus: current challenges and future prospects. Infect Control Hosp Epidemiol 31(Suppl 1):S45–47
5. Downer R, Roche F, Park PW, Mecham RP, Foster TJ (2002) The elastin-binding protein of Staphylococcus aureus (EbpS) is expressed at the cell surface as an integral membrane protein and not as a cell wall-associated protein. J Biol Chem 277:243–250
6. Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60:2126–2132
7. Gailit J, Clarke C, Newman D, Tonnesen MG, Mosesson MW, Clark RA (1997) Human fibroblasts bind directly to fibrinogen at RGD sites through integrin αvβ3. Exp Cell Res 232:118–126
8. Ganesh VK, Rivera JJ, Smeds E, Ko YP, Bowden MG, Wann ER, Gurusiddappa S, Fitzgerald JR, Hook M (2008) A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. PLoS Pathog 4:e1000226
9. Ganesh VK, Barbu EM, Deivanayagam CC, Le B, Anderson AS, Matsuka YV, Lin SL, Foster TJ, Narayana SV, Hook M (2011) Structural and biochemical characterization of Staphylococcus aureus clumping factor B/ligand interactions. J Biol Chem 286:25963–25972
10. Ganss B, Kim RH, Sodek J (1999) Bone sialoprotein. Crit Rev Oral Biol Med 10:79–98
11. Gillaspy AF, Lee CY, Sau S, Cheung AL, Smeltzer MS (1998) Factors affecting the collagen binding capacity of Staphylococcus aureus. Infect Immun 66:3170–3178
12. Hultenby K, Reinholt FP, Norgard M, Oldberg A, Wendel M, Heinegard D (1994) Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Eur J Cell Biol 63:230–239
13. Hunter GK, Goldberg HA (1993) Nucleation of hydroxyapatite by bone sialoprotein. Proc Natl Acad Sci USA 90:8562–8565
14. Jancarik J, Scott WG, Milligan DL, Koshland DE, Kim S-H (1991) Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium. J Mol Biol 221:31–34
15. Josefsson E, McCrea KW, Ni Eidhin D, O’Connell D, Cox J, Hook M, Foster TJ (1998) Three new members of the serine-aspartate repeat protein multigene family of Staphylococcus aureus. Microbiology 144(Pt 12):3387–3395
16. Kluytmans J, van Belkum A, Verbrugh H (1997) Nasal carriage of Staphylococcus aureus: epidemiology, underlying mechanisms, and associated risks. Clin Microbiol Rev 10:505–520
17. Kollman JM, Pandi L, Sawaya MR, Riley M, Doolittle RF (2009) Crystal structure of human fibrinogen. Biochemistry 48:3877–3886
18. Lowy FD (1998) Staphylococcus aureus infections. N Engl J Med 339:520–532
19. McCrea KW, Hartford O, Davis S, Eidhin DN, Lina G, Speziale P, Foster TJ, Hook M (2000) The serine-aspartate repeat (Sdr) protein family in Staphylococcus epidermidis. Microbiology 146(Pt 7):1535–1546
20. McDevitt D, Francois P, Vaudaux P, Foster TJ (1994) Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus. Mol Microbiol 11:237–248
21. Mosesson MW, Siebenlist KR, Meh DA (2001) The structure and biological features of fibrinogen and fibrin. Ann N Y Acad Sci 936:11–30
22. Ni Eidhin D, Perkins S, Francois P, Vaudaux P, Hook M, Foster TJ (1998) Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus. Mol Microbiol 30:245–257
23. Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 276:307–326
24. Patti JM, Allen BL, McGavin MJ, Hook M (1994) MSCRAMM-mediated adherence of microorganisms to host tissues. Annu Rev Microbiol 48:585–617
25. Peacock SJ, Moore CE, Justice A, Kantzanou M, Story L, Mackie K, O’Neill G, Day NP (2002) Virulent combinations of adhesin and toxin genes in natural populations of Staphylococcus aureus. Infect Immun 70:4987–4996
26. Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, Choe D, Xu Y, Hook M, Narayana SV (2003) A “dock, lock, and latch” structural model for a staphylococcal adhesin binding to fibrinogen. Cell 115:217–228
27. Rivera J, Vannakambadi G, Hook M, Speziale P (2007) Fibrinogen-binding proteins of Gram-positive bacteria. Thromb Haemost 98:503–511
28. Ryden C, Maxe I, Franzen A, Ljungh A, Heinegard D, Rubin K (1987) Selective binding of bone matrix sialoprotein to Staphylococcus aureus in osteomyelitis. Lancet 2:515
29. Tung H, Guss B, Hellman U, Persson L, Rubin K, Ryden C (2000) A bone sialoprotein-binding protein from Staphylococcus aureus: a member of the staphylococcal Sdr family. Biochem J 345(Pt 3):611–619
30. Vazquez V, Liang X, Horndahl JK, Ganesh VK, Smeds E, Foster TJ, Hook M (2011) Fibrinogen is a ligand for the Staphylococcus aureus microbial surface components recognizing adhesive matrix molecules (MSCRAMM) bone sialoprotein-binding protein (Bbp). J Biol Chem 286:29797–29805
31. Wang X, Ge J, Liu B, Hu Y, Yang M (2013) Structures of SdrD from Staphylococcus aureus reveal the molecular mechanism of how the cell surface receptors recognize their ligands. Protein Cell 4:277–285
32. Wann ER, Gurusiddappa S, Hook M (2000) The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen. J Biol Chem 275:13863–13871
33. Xiang H, Feng Y, Wang J, Liu B, Chen Y, Liu L, Deng X, Yang M (2012) Crystal structures reveal the multi-ligand binding mechanism of Staphylococcus aureus ClfB. PLoS pathog 8:e1002751
34. Zetola N, Francis JS, Nuermberger EL, Bishai WR (2005) Community-acquired meticillin-resistant Staphylococcus aureus: an emerging threat. Lancet Infect Dis 5:275–286