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Volumn 115, Issue 2, 2003, Pages 217-228

A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; FIBRINOGEN;

EID: 0142227210     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00809-2     Document Type: Article
Times cited : (252)

References (38)
  • 1
    • 0027258750 scopus 로고
    • The fibrinogen sequences that interact with thrombin
    • Binnie C.G., Lord S.T. The fibrinogen sequences that interact with thrombin. Blood. 81:1993;3186-3192.
    • (1993) Blood , vol.81 , pp. 3186-3192
    • Binnie, C.G.1    Lord, S.T.2
  • 2
    • 0022924074 scopus 로고
    • Specificity of thrombin and its action on fibrinogen
    • Blomback B. Specificity of thrombin and its action on fibrinogen. Ann. N Y Acad. Sci. 485:1986;120-123.
    • (1986) Ann. N Y Acad. Sci. , vol.485 , pp. 120-123
    • Blomback, B.1
  • 3
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software system for macromolecular structure determination
    • Brunger A.T. Crystallography and NMR system. a new software system for macromolecular structure determination Acta Crystallogr. D. Biol. Crystallogr. 45:1998;905-921.
    • (1998) Acta Crystallogr. D. Biol. Crystallogr. , vol.45 , pp. 905-921
    • Brunger, A.T.1
  • 6
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: A common cause of persistent infections
    • Costerton J.W., Stewart P.S., Greenberg E.P. Bacterial biofilms. a common cause of persistent infections Science. 284:1999;1318-1322.
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 7
    • 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 Bβ chain
    • Davis S.L., Gurusiddappa S., McCrea K.W., Perkins S., Hook M. 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 Bβ chain. J. Biol. Chem. 276:2001;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
  • 9
    • 12244313428 scopus 로고    scopus 로고
    • A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: Crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A
    • Deivanayagam C.C.S., Wann E.R., Chen W., Carson M., Rajashankar K.R., Hook M., Narayana S.V.L. 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. 21:2002;6660-6672.
    • (2002) EMBO J. , vol.21 , pp. 6660-6672
    • Deivanayagam, C.C.S.1    Wann, E.R.2    Chen, W.3    Carson, M.4    Rajashankar, K.R.5    Hook, M.6    Narayana, S.V.L.7
  • 10
    • 0035029378 scopus 로고    scopus 로고
    • Biofilms and device-associated infections
    • Donlan R.M. Biofilms and device-associated infections. Emerg. Infect. Dis. 7:2001;277-281.
    • (2001) Emerg. Infect. Dis. , vol.7 , pp. 277-281
    • Donlan, R.M.1
  • 11
    • 0032436996 scopus 로고    scopus 로고
    • Surface protein adhesins of Staphylococcus aureus
    • Foster T.J., Hook M. Surface protein adhesins of Staphylococcus aureus. Trends Microbiol. 6:1998;484-488.
    • (1998) Trends Microbiol. , vol.6 , pp. 484-488
    • Foster, T.J.1    Hook, M.2
  • 12
    • 0033016317 scopus 로고    scopus 로고
    • Coagulase-negative staphylococci: Role as pathogens
    • Huebner J., Goldman D.A. Coagulase-negative staphylococci. role as pathogens Annu. Rev. Med. 50:1999;223-236.
    • (1999) Annu. Rev. Med. , vol.50 , pp. 223-236
    • Huebner, J.1    Goldman, D.A.2
  • 13
    • 0035164511 scopus 로고    scopus 로고
    • Identification and characterization of a novel 38.5-kilodalton cell surface protein of Staphylococcus aureus with extended-spectrum binding activity for extracellular matrix and plasma proteins
    • Hussain M., Becker K., Eiff C.V., Schrenzel J., Peters G., Herrmann M. Identification and characterization of a novel 38.5-kilodalton cell surface protein of Staphylococcus aureus with extended-spectrum binding activity for extracellular matrix and plasma proteins. J. Bacteriol. 183:2001;6778-6786.
    • (2001) J. Bacteriol. , vol.183 , pp. 6778-6786
    • Hussain, M.1    Becker, K.2    Eiff, C.V.3    Schrenzel, J.4    Peters, G.5    Herrmann, M.6
  • 14
    • 0029096724 scopus 로고
    • Staphylococcus aureus expresses a major histocompatibility complex class II analog
    • Jönsson K., McDevitti D., McGavin M.H., Patti J.M., Hook M. Staphylococcus aureus expresses a major histocompatibility complex class II analog. J. Biol. Chem. 270:1995;21457-21460.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21457-21460
    • Jönsson, K.1    McDevitti, D.2    McGavin, M.H.3    Patti, J.M.4    Hook, M.5
  • 15
    • 0016269452 scopus 로고
    • The identification of fibrinopeptide B as a chemotactic agent derived from human fibrinogen
    • Kay A.B., Pepper D.S., McKenzie R. The identification of fibrinopeptide B as a chemotactic agent derived from human fibrinogen. Br. J. Haematol. 24:1974;669-677.
    • (1974) Br. J. Haematol. , vol.24 , pp. 669-677
    • Kay, A.B.1    Pepper, D.S.2    McKenzie, R.3
  • 17
    • 0025740508 scopus 로고
    • Thrombin Glu-39 restricts the P′3 specificity to nonacidic residues
    • Le Bonniec B.F., MacGillvray R.T.A., Esmon C.T. Thrombin Glu-39 restricts the P′3 specificity to nonacidic residues. J. Biol. Chem. 266:1991;13796-13803.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13796-13803
    • Le Bonniec, B.F.1    MacGillvray, R.T.A.2    Esmon, C.T.3
  • 18
    • 0025055597 scopus 로고
    • Analysis of fibrinogen Aα-fusion proteins. Mutants which inhibit thrombin equivalently are not equally good substrates
    • Lord S.T., Byrd P.A., Hede K.L., Wei C., Colby T.J. Analysis of fibrinogen Aα-fusion proteins. Mutants which inhibit thrombin equivalently are not equally good substrates. J. Biol. Chem. 265:1990;838-843.
    • (1990) J. Biol. Chem. , vol.265 , pp. 838-843
    • Lord, S.T.1    Byrd, P.A.2    Hede, K.L.3    Wei, C.4    Colby, T.J.5
  • 19
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J.U., Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature. 356:1992;83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 20
    • 0030868145 scopus 로고    scopus 로고
    • Crystal structure of fibrinogen-Aα peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16
    • Malkowski M.G., Martin P.D., Lord S.T., Edwards B.F. Crystal structure of fibrinogen-Aα peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16. Biochem. J. 326:1997;815-822.
    • (1997) Biochem. J. , vol.326 , pp. 815-822
    • Malkowski, M.G.1    Martin, P.D.2    Lord, S.T.3    Edwards, B.F.4
  • 21
    • 0026657151 scopus 로고
    • The structure of residues 7-16 of the Aα-chain of human fibrinogen bound to bovine thrombin at 2.3-Å resolution
    • Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F. The structure of residues 7-16 of the Aα-chain of human fibrinogen bound to bovine thrombin at 2.3-Å resolution. J. Biol. Chem. 267:1992;7911-7920.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7911-7920
    • Martin, P.D.1    Robertson, W.2    Turk, D.3    Huber, R.4    Bode, W.5    Edwards, B.F.6
  • 22
    • 0029819059 scopus 로고    scopus 로고
    • Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen A: Geometry of the catalytic triad and interactions of the P1′, P2′, and P3′ substrate residues
    • Martin P.D., Malkowski M.G., DiMaio J., Konishi Y., Ni F., Edwards B.F.P. Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen A. geometry of the catalytic triad and interactions of the P1′, P2′, and P3′ substrate residues Biochemistry. 35:1996;13030-13039.
    • (1996) Biochemistry , vol.35 , pp. 13030-13039
    • Martin, P.D.1    Malkowski, M.G.2    DiMaio, J.3    Konishi, Y.4    Ni, F.5    Edwards, B.F.P.6
  • 23
    • 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. Loss of clumping factor B fibrinogen binding activity by Staphylococcus aureus involves cessation of transcription, shedding and cleavage by metalloprotease. J. Biol. Chem. 276:2001;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
  • 25
    • 84920325457 scopus 로고
    • AmoRe and automated package for molecular replacement
    • Navaza J. AmoRe and automated package for molecular replacement. Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0032899735 scopus 로고    scopus 로고
    • Adherence of Staphylococcus aureus is enhanced by an endogenous secreted protein with broad binding activity
    • Palma M., Haggar A., Flock J.-I. Adherence of Staphylococcus aureus is enhanced by an endogenous secreted protein with broad binding activity. J. Bacteriol. 181:1999;2840-2845.
    • (1999) J. Bacteriol. , vol.181 , pp. 2840-2845
    • Palma, M.1    Haggar, A.2    Flock, J.-I.3
  • 28
    • 0035943662 scopus 로고    scopus 로고
    • Extracellular fibrinogen-binding protein, Efb, from Staphylococcus aureus blocks platelet aggregation due to its binding to the α-chain
    • Palma M., Shannon O., Quezada H.C., Berg A., Flock J.-I. Extracellular fibrinogen-binding protein, Efb, from Staphylococcus aureus blocks platelet aggregation due to its binding to the α-chain. J. Biol. Chem. 276:2001;31691-31697.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31691-31697
    • Palma, M.1    Shannon, O.2    Quezada, H.C.3    Berg, A.4    Flock, J.-I.5
  • 29
    • 0028074251 scopus 로고
    • Microbial adhesins recognizing extracellular matrix macromolecules
    • Patti J.M., Hook M. Microbial adhesins recognizing extracellular matrix macromolecules. Curr. Opin. Cell Biol. 6:1994;752-758.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 752-758
    • Patti, J.M.1    Hook, M.2
  • 30
    • 0035976893 scopus 로고    scopus 로고
    • Structural organization of the fibrinogen-binding 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. Structural organization of the fibrinogen-binding region of the clumping factor B MSCRAMM of Staphylococcus aureus. J. Biol. Chem. 276:2001;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
  • 31
    • 0033836839 scopus 로고    scopus 로고
    • Nosocomial infections in combined medical-surgical intensive care units in the United States
    • Richards M.J., Edwards J.R., Culver D.H., Gaynes R.P. Nosocomial infections in combined medical-surgical intensive care units in the United States. Infect. Control Hosp. Epidemiol. 21:2000;510-515.
    • (2000) Infect. Control Hosp. Epidemiol. , vol.21 , pp. 510-515
    • Richards, M.J.1    Edwards, J.R.2    Culver, D.H.3    Gaynes, R.P.4
  • 32
    • 0017237180 scopus 로고
    • Chemotaxis for human monocytes by fibrinogen-derived peptides
    • Richardson D.L., Pepper D.S., Kay A.B. Chemotaxis for human monocytes by fibrinogen-derived peptides. Br. J. Haematol. 32:1976;507-513.
    • (1976) Br. J. Haematol. , vol.32 , pp. 507-513
    • Richardson, D.L.1    Pepper, D.S.2    Kay, A.B.3
  • 34
    • 0022924075 scopus 로고
    • Chemical basis of thrombin interactions with fibrinogen
    • Scheraga H.A. Chemical basis of thrombin interactions with fibrinogen. Ann. N Y Acad. Sci. 485:1986;124-133.
    • (1986) Ann. N Y Acad. Sci. , vol.485 , pp. 124-133
    • Scheraga, H.A.1
  • 36
    • 0022534483 scopus 로고
    • Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B
    • Senior R.M., Skogen W.F., Griffin G.L., Wilner G.D. Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B. J. Clin. Invest. 77:1986;1014-1019.
    • (1986) J. Clin. Invest. , vol.77 , pp. 1014-1019
    • Senior, R.M.1    Skogen, W.F.2    Griffin, G.L.3    Wilner, G.D.4
  • 37
    • 0023934344 scopus 로고
    • Fibrinogen-derived peptide Bβ 1-42 is a multidomained neutrophil chemoattractant
    • Skogen W.F., Senior R.M., Griffin G.L., Wilner G.D. Fibrinogen-derived peptide Bβ 1-42 is a multidomained neutrophil chemoattractant. Blood. 71:1988;1475-1479.
    • (1988) Blood , vol.71 , pp. 1475-1479
    • Skogen, W.F.1    Senior, R.M.2    Griffin, G.L.3    Wilner, G.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.