메뉴 건너뛰기




Volumn 154, Issue 2, 2008, Pages 550-558

Identification of the Staphylococcus aureus MSCRAMM clumping factor B (ClfB) binding site in the αC-domain of human fibrinogen

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CLUMPING FACTOR B PROTEIN; FIBRINOGEN; MICROBIAL SURFACE COMPONENT RECOGNIZING ADHESIVE MATRIX MOLECULE; UNCLASSIFIED DRUG;

EID: 39749134910     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.2007/010868-0     Document Type: Article
Times cited : (71)

References (41)
  • 1
    • 0023912859 scopus 로고
    • High-level expression of a functional human fibrinogen gamma chain in Escherichia coli
    • Bolyard, M. G. & Lord, S. T. (1988). High-level expression of a functional human fibrinogen gamma chain in Escherichia coli. Gene 66, 183-192.
    • (1988) Gene , vol.66 , pp. 183-192
    • Bolyard, M.G.1    Lord, S.T.2
  • 2
    • 33144477571 scopus 로고    scopus 로고
    • Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR
    • Burton, R. A., Tsurupa, G., Medved, L. & Tjandra, N. (2006). Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR. Biochemistry 45, 2257-2266.
    • (2006) Biochemistry , vol.45 , pp. 2257-2266
    • Burton, R.A.1    Tsurupa, G.2    Medved, L.3    Tjandra, N.4
  • 3
    • 0026721348 scopus 로고
    • Involvement of the alpha-chain in fibrin clot formation. Effect of monoclonal-antibodies
    • Cierniewski, C. S. & Budzynski, A. Z. (1992). Involvement of the alpha-chain in fibrin clot formation. Effect of monoclonal-antibodies. Biochemistry 31, 4248-4253.
    • (1992) Biochemistry , vol.31 , pp. 4248-4253
    • Cierniewski, C.S.1    Budzynski, A.Z.2
  • 5
    • 0019793959 scopus 로고
    • Alpha-chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XIIIa). Calcium ion regulatory aspects
    • Credo, R. B., Curtis, C. G. & Lorand, L. (1981). Alpha-chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XIIIa). Calcium ion regulatory aspects. Biochemistry 20, 3770-3778.
    • (1981) Biochemistry , vol.20 , pp. 3770-3778
    • Credo, R.B.1    Curtis, C.G.2    Lorand, L.3
  • 6
    • 0035958880 scopus 로고    scopus 로고
    • 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
    • Davis, S. L., Gurusiddappa, S., McCrea, K. W., 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.
    • (2001) J Biol Chem , vol.276 , pp. 27799-27805
    • Davis, S.L.1    Gurusiddappa, S.2    McCrea, K.W.3    Perkins, S.4    Hook, M.5
  • 7
    • 0021118122 scopus 로고
    • Fibrinogen and fibrin
    • Doolittle, R. F. (1984). Fibrinogen and fibrin. Annu Rev Biochem 53, 195-229.
    • (1984) Annu Rev Biochem , vol.53 , pp. 195-229
    • Doolittle, R.F.1
  • 8
    • 0002527348 scopus 로고
    • Staphylococcal coagulase; mode of action and antigenicity
    • Duthie, E. S. & Lorenz, L. L. (1952). Staphylococcal coagulase; mode of action and antigenicity. J Gen Microbiol 6, 95-107.
    • (1952) J Gen Microbiol , vol.6 , pp. 95-107
    • Duthie, E.S.1    Lorenz, L.L.2
  • 10
    • 0032480786 scopus 로고    scopus 로고
    • Analysis of A alpha 251 fibrinogen: The alpha C domain has a role in polymerization, albeit more subtle than anticipated from the analogous proteolytic fragment X
    • Gorkun, O. V., Henschen-Edman, A. H., Ping, L. F. & Lord, S. T. (1998). Analysis of A alpha 251 fibrinogen: the alpha C domain has a role in polymerization, albeit more subtle than anticipated from the analogous proteolytic fragment X. Biochemistry 37, 15434-15441.
    • (1998) Biochemistry , vol.37 , pp. 15434-15441
    • Gorkun, O.V.1    Henschen-Edman, A.H.2    Ping, L.F.3    Lord, S.T.4
  • 13
    • 0029096724 scopus 로고
    • Staphylococcus aureus expresses a major histocompatibility complex class II analog
    • Jonsson, K., McDevitt D., McGavin, M. H., Patti, J. M. & Hook M. (1995). Staphylococcus aureus expresses a major histocompatibility complex class II analog. J Biol Chem 270, 21457-21460.
    • (1995) J Biol Chem , vol.270 , pp. 21457-21460
    • Jonsson, K.1    McDevitt, D.2    McGavin, M.H.3    Patti, J.M.4    Hook, M.5
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0021930956 scopus 로고
    • Expression of a cloned human fibrinogen cDNA in Escherichia coli synthesis of an A alpha polypeptide
    • Lord, S. T. (1985). Expression of a cloned human fibrinogen cDNA in Escherichia coli synthesis of an A alpha polypeptide. DNA 4, 33-38.
    • (1985) DNA , vol.4 , pp. 33-38
    • Lord, S.T.1
  • 16
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S. K., Liu, G., Ton-That, H. & Schneewind, O. (1999). Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285, 760-763.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 17
    • 0035839473 scopus 로고    scopus 로고
    • Loss of clumping factor B fibrinogen binding activity by Staphylococcus aureus involves cessation of transcription, shedding and cleavage by metalloprotease
    • McAleese, F. M., Walsh, E. J., Sieprawska, M., Potempa, J. & Foster, T. J. (2001). Loss of clumping factor B fibrinogen binding activity by Staphylococcus aureus involves cessation of transcription, shedding and cleavage by metalloprotease. J Biol Chem 276, 29969-29978.
    • (2001) J Biol Chem , vol.276 , pp. 29969-29978
    • McAleese, F.M.1    Walsh, E.J.2    Sieprawska, M.3    Potempa, J.4    Foster, T.J.5
  • 18
    • 0028334112 scopus 로고
    • Molecular chacterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus
    • McDevitt, D., Francois, P., Vaudaux, P. & Foster, T. J. (1994). Molecular chacterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus. Mol Microbiol 11, 237-248.
    • (1994) Mol Microbiol , vol.11 , pp. 237-248
    • McDevitt, D.1    Francois, P.2    Vaudaux, P.3    Foster, T.J.4
  • 19
    • 0029095204 scopus 로고
    • Indentification of the ligand-binding domain of the surface-located fibrogen receptor (clumping factor) of Staphylococcus aureus
    • McDevitt, D., Francois, P., Vaudaux, P. & Foster, T. J. (1995). Indentification of the ligand-binding domain of the surface-located fibrogen receptor (clumping factor) of Staphylococcus aureus. Mol Microbiol 16, 895-907.
    • (1995) Mol Microbiol , vol.16 , pp. 895-907
    • McDevitt, D.1    Francois, P.2    Vaudaux, P.3    Foster, T.J.4
  • 20
    • 0030758696 scopus 로고    scopus 로고
    • Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen
    • McDevitt, D., Nanavaty, T., House-Pompeo, K., Bell, E., Turner, N., McIntire, L., Foster, T. & Hook M. (1997). Characterization of the interaction between the Staphylococcus aureus clumping factor (ClfA) and fibrinogen. Eur J Biochem 247, 416-424.
    • (1997) Eur J Biochem , vol.247 , pp. 416-424
    • McDevitt, D.1    Nanavaty, T.2    House-Pompeo, K.3    Bell, E.4    Turner, N.5    McIntire, L.6    Foster, T.7    Hook, M.8
  • 21
    • 0027212845 scopus 로고
    • Identification of a Staphylococcus aureus extracellular matrix-binding protein with broad specificity
    • McGavin, M. H., Krajewska-Pietrasik D., Ryden, C. & Hook, M. (1993). Identification of a Staphylococcus aureus extracellular matrix-binding protein with broad specificity. Infect Immun 61, 2479-2485.
    • (1993) Infect Immun , vol.61 , pp. 2479-2485
    • McGavin, M.H.1    Krajewska-Pietrasik, D.2    Ryden, C.3    Hook, M.4
  • 22
    • 0021110096 scopus 로고
    • Structural organization of C-terminal parts of fibrinogen A alpha-chains
    • Medved, L. V., Gorkun, O. V. & Privalov, P. L. (1983). Structural organization of C-terminal parts of fibrinogen A alpha-chains. FEBS Lett 160, 291-295.
    • (1983) FEBS Lett , vol.160 , pp. 291-295
    • Medved, L.V.1    Gorkun, O.V.2    Privalov, P.L.3
  • 23
    • 0021905372 scopus 로고
    • The role of fibrinogen alpha C-domains in the fibrin assembly process
    • Medved, L. V., Gorkun, O. V., Manyakov, V. F. & Belitser, V. A. (1985). The role of fibrinogen alpha C-domains in the fibrin assembly process. FEBS Lett 181, 109-112.
    • (1985) FEBS Lett , vol.181 , pp. 109-112
    • Medved, L.V.1    Gorkun, O.V.2    Manyakov, V.F.3    Belitser, V.A.4
  • 24
    • 34447265067 scopus 로고    scopus 로고
    • Both complement- and fibrinogen-dependent mechanisms contribute to platelet aggregation mediated by Staphylococcus aureus dumping factor B
    • Miajlovic, H., Loughman, A., Brennan, M., Cox, D. & Foster, T. J. (2007). Both complement- and fibrinogen-dependent mechanisms contribute to platelet aggregation mediated by Staphylococcus aureus dumping factor B. Infect Immun 75, 3335-3343.
    • (2007) Infect Immun , vol.75 , pp. 3335-3343
    • Miajlovic, H.1    Loughman, A.2    Brennan, M.3    Cox, D.4    Foster, T.J.5
  • 25
    • 0027992980 scopus 로고
    • Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria
    • Navarre, W. W. & Schneewind, O. (1994). Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol Microbiol 14, 115-121.
    • (1994) Mol Microbiol , vol.14 , pp. 115-121
    • Navarre, W.W.1    Schneewind, O.2
  • 26
    • 15444353754 scopus 로고    scopus 로고
    • Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus
    • Ni Eidhin, D., Perkins, S., Francois, P., Vaudaux, P., Hook, M. & Foster, T. J. (1998). Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus. Mol Microbiol 30, 245-257.
    • (1998) Mol Microbiol , vol.30 , pp. 245-257
    • Ni Eidhin, D.1    Perkins, S.2    Francois, P.3    Vaudaux, P.4    Hook, M.5    Foster, T.J.6
  • 27
    • 0036854622 scopus 로고    scopus 로고
    • Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human type I cytokeratin 10: Implications for nasal colonization
    • O'Brien, L. M., Walsh, E. J., Massey, R. C., Peacock, S. J. & Foster, T. J. (2002). Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human type I cytokeratin 10: implications for nasal colonization. Cell Microbiol 4, 759-770.
    • (2002) Cell Microbiol , vol.4 , pp. 759-770
    • O'Brien, L.M.1    Walsh, E.J.2    Massey, R.C.3    Peacock, S.J.4    Foster, T.J.5
  • 29
    • 0032557528 scopus 로고    scopus 로고
    • Multiple binding sites in the interaction between an extracellular fibrinogen-binding protein from Staphylococcus aureus and fibrinogen
    • Palma, M., Wade, D., Flock, M. & Flock J. I. (1998). Multiple binding sites in the interaction between an extracellular fibrinogen-binding protein from Staphylococcus aureus and fibrinogen. J Biol Chem 273, 13177-13181.
    • (1998) J Biol Chem , vol.273 , pp. 13177-13181
    • Palma, M.1    Wade, D.2    Flock, M.3    Flock, J.I.4
  • 31
    • 0035976893 scopus 로고    scopus 로고
    • Structural organization of the fibrinogen-bindihg region of the clumping factor B MSCRAMM of Staphylococcus aureus
    • Perkins, S., Walsh, E. J., Deivanayagam, C. C., Narayana, S. V., Foster, T. J. & Hook, M. (2001). Structural organization of the fibrinogen-bindihg region of the clumping factor B MSCRAMM of Staphylococcus aureus. J Biol Chem 276, 44721-44728.
    • (2001) J Biol Chem , vol.276 , pp. 44721-44728
    • Perkins, S.1    Walsh, E.J.2    Deivanayagam, C.C.3    Narayana, S.V.4    Foster, T.J.5    Hook, M.6
  • 32
    • 0025308106 scopus 로고
    • The coagulase of Staphylococcus aureus 8325-4. Sequence analysis and virulence of site-specific coagulase-deficient mutants
    • Phonimdaeng, P., O'Reilly, M., Nowlan, P., Bramley, A. J. & Foster, T. J. (1990). The coagulase of Staphylococcus aureus 8325-4. Sequence analysis and virulence of site-specific coagulase-deficient mutants. Mol Microbiol 4, 393-404.
    • (1990) Mol Microbiol , vol.4 , pp. 393-404
    • Phonimdaeng, P.1    O'Reilly, M.2    Nowlan, P.3    Bramley, A.J.4    Foster, T.J.5
  • 34
    • 0030070930 scopus 로고    scopus 로고
    • Comparative structural and functional features of the human fibrinogen alpha C domain and the isolated alpha C fragment. Characterization using monoclonal antibodies to defined COOH-terminal A alpha chain regions
    • Rudchenko, S., Trakht, I. & Sobel, J. H. (1996). Comparative structural and functional features of the human fibrinogen alpha C domain and the isolated alpha C fragment. Characterization using monoclonal antibodies to defined COOH-terminal A alpha chain regions. J Biol Chem 271, 2523-2530.
    • (1996) J Biol Chem , vol.271 , pp. 2523-2530
    • Rudchenko, S.1    Trakht, I.2    Sobel, J.H.3
  • 36
    • 0035936549 scopus 로고    scopus 로고
    • Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) alpha C-domains
    • Tsurupa, G. & Medved, L. (2001). Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) alpha C-domains. Biochemistry 40, 801-808.
    • (2001) Biochemistry , vol.40 , pp. 801-808
    • Tsurupa, G.1    Medved, L.2
  • 37
    • 0037150105 scopus 로고    scopus 로고
    • Structural organization of the fibrin(ogen) alpha C-domain
    • Tsurupa, G., Tsonev, L. & Medved, L. (2002). Structural organization of the fibrin(ogen) alpha C-domain. Biochemistry 41, 6449-6459.
    • (2002) Biochemistry , vol.41 , pp. 6449-6459
    • Tsurupa, G.1    Tsonev, L.2    Medved, L.3
  • 38
    • 10944263785 scopus 로고    scopus 로고
    • Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface components recognizing adhesive matrix molecules) adhesin of Staphylococcus aureus, also binds to the tail region of type I cytokeratin 10
    • Walsh, E. J., O'Brien, L. M., Liang, X., Hook, M. & Foster, T. J. (2004). Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface components recognizing adhesive matrix molecules) adhesin of Staphylococcus aureus, also binds to the tail region of type I cytokeratin 10. J Biol Chem 279, 50691-50699.
    • (2004) J Biol Chem , vol.279 , pp. 50691-50699
    • Walsh, E.J.1    O'Brien, L.M.2    Liang, X.3    Hook, M.4    Foster, T.J.5
  • 39
    • 0034607985 scopus 로고    scopus 로고
    • The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen
    • Wann, E. R., 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.
    • (2000) J Biol Chem , vol.275 , pp. 13863-13871
    • Wann, E.R.1    Gurusiddappa, S.2    Hook, M.3
  • 40
    • 0034972781 scopus 로고    scopus 로고
    • The structure and function of the αC domains of fibrinogen
    • Weisel, J. W. & Medved, L. (2001). The structure and function of the αC domains of fibrinogen. Ann N Y Acad Sci 936, 312-327.
    • (2001) Ann N Y Acad Sci , vol.936 , pp. 312-327
    • Weisel, J.W.1    Medved, L.2
  • 41
    • 0035940439 scopus 로고    scopus 로고
    • Crystal structure of native chicken fibrinogen at 2.7 Å resolution
    • Yang, Z., Kollman, J. M., Pandi, L. & Doolittle, R. F. (2001). Crystal structure of native chicken fibrinogen at 2.7 Å resolution. Biochemistry 40, 12515-12523.
    • (2001) Biochemistry , vol.40 , pp. 12515-12523
    • Yang, Z.1    Kollman, J.M.2    Pandi, L.3    Doolittle, R.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.