메뉴 건너뛰기




Volumn 61, Issue 22, 2004, Pages 2793-2798

The staphylocoagulase family of zymogen activator and adhesion proteins

Author keywords

Blood coagulation; Endocarditis; Fibrinogen; Proteinases; Prothrombin; Staphylocoagulase; Zymogens

Indexed keywords

BACTERIAL ENZYME; BINDING PROTEIN; ENZYME PRECURSOR; FIBRIN; FIBRINOGEN; PLASMA PROTEIN; PLASMINOGEN ACTIVATOR; PRETHROMBIN 2; PROTEIN; PROTHROMBIN; SCLEROPROTEIN; STAPHYLOCOCCAL SERINE PROTEINASE; THROMBIN; UNCLASSIFIED DRUG;

EID: 11244267323     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-4285-7     Document Type: Review
Times cited : (50)

References (37)
  • 1
    • 0141929350 scopus 로고    scopus 로고
    • Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation
    • Friedrich R., Panizzi P., Fuentes-Prior P., Richter K., Verhamme I., Anderson P. J. et al. (2003) Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. Nature 425: 535-539
    • (2003) Nature , vol.425 , pp. 535-539
    • Friedrich, R.1    Panizzi, P.2    Fuentes-Prior, P.3    Richter, K.4    Verhamme, I.5    Anderson, P.J.6
  • 2
    • 0022646220 scopus 로고
    • Isolation and characterization of staphylocoagulase chymotryptic fragment. Localization of the procoagulant- and prothrombin-binding domain of this protein
    • Kawabata S., Morita T., Miyata T., Iwanaga S. and Igarashi H. (1986) Isolation and characterization of staphylocoagulase chymotryptic fragment. Localization of the procoagulant- and prothrombin-binding domain of this protein. J. Biol. Chem. 261: 1427-1433
    • (1986) J. Biol. Chem. , vol.261 , pp. 1427-1433
    • Kawabata, S.1    Morita, T.2    Miyata, T.3    Iwanaga, S.4    Igarashi, H.5
  • 3
    • 0016442564 scopus 로고
    • Activation of a pro-enzyme by a stoichiometric reaction with another protein. The reaction between prothrombin and staphylocoagulase
    • Hemker H. C., Bas B. M. and Muller A. D. (1975) Activation of a pro-enzyme by a stoichiometric reaction with another protein. The reaction between prothrombin and staphylocoagulase. Biochim. Biophys. Acta 379: 180-188
    • (1975) Biochim. Biophys. Acta , vol.379 , pp. 180-188
    • Hemker, H.C.1    Bas, B.M.2    Muller, A.D.3
  • 4
    • 0036642405 scopus 로고    scopus 로고
    • Platelet-binding domains in 2 fibrinogen-binding proteins of Staphylococcus aureus identified by phage display
    • Heilmann C., Herrmann M., Kehrel B. E. and Peters G. (2002) Platelet-binding domains in 2 fibrinogen-binding proteins of Staphylococcus aureus identified by phage display. J. Infect. Dis. 186: 32-39
    • (2002) J. Infect. Dis. , vol.186 , pp. 32-39
    • Heilmann, C.1    Herrmann, M.2    Kehrel, B.E.3    Peters, G.4
  • 5
    • 0028834487 scopus 로고
    • Role of Staphylococcus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis
    • Moreillon P., Entenza J. M., Francioli P., McDevitt D., Foster T. J., François P. et al. (1995) Role of Staphylococcus aureus coagulase and clumping factor in pathogenesis of experimental endocarditis. Infect. Immun. 63: 4738-4743
    • (1995) Infect. Immun. , vol.63 , pp. 4738-4743
    • Moreillon, P.1    Entenza, J.M.2    Francioli, P.3    McDevitt, D.4    Foster, T.J.5    François, P.6
  • 6
    • 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. and 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
  • 8
    • 0003126792 scopus 로고
    • Infective and noninfective endocarditis
    • Hurst J. W., Rackley C. E., Sonnenblick E. H. and Wenger N. K. (eds), McGraw-Hill, New York
    • Durack D. T. (1990) Infective and noninfective endocarditis. In: The Heart: Arteries and Veins, vol. 63, pp. 1230-1255, Hurst J. W., Rackley C. E., Sonnenblick E. H. and Wenger N. K. (eds), McGraw-Hill, New York
    • (1990) The Heart: Arteries and Veins , vol.63 , pp. 1230-1255
    • Durack, D.T.1
  • 9
    • 2442442058 scopus 로고    scopus 로고
    • The molecular basis of fibronectin-mediated bacterial adherence to host cells
    • Schwarz-Linek U., Höök M. and Potts J. R. (2004) The molecular basis of fibronectin-mediated bacterial adherence to host cells. Mol. Microbiol. 52: 631-641
    • (2004) Mol. Microbiol. , vol.52 , pp. 631-641
    • Schwarz-Linek, U.1    Höök, M.2    Potts, J.R.3
  • 11
    • 0036061581 scopus 로고    scopus 로고
    • Staphylococcus aureus extracellular adherence protein serves as anti-inflammatory factor by inhibiting the recruitment of host leukocytes
    • Chavakis T., Hussain M., Kanse S. M., Peters G., Bretzel R. G., Flock J. I. et al. (2002) Staphylococcus aureus extracellular adherence protein serves as anti-inflammatory factor by inhibiting the recruitment of host leukocytes. Nat. Med. 8: 687-693
    • (2002) Nat. Med. , vol.8 , pp. 687-693
    • Chavakis, T.1    Hussain, M.2    Kanse, S.M.3    Peters, G.4    Bretzel, R.G.5    Flock, J.I.6
  • 12
    • 0031034572 scopus 로고    scopus 로고
    • Role of coagulase in a murine model of hematogenous pulmonary infection induced by intravenous injection of Staphylococcus aureus enmeshed in agar beads
    • Sawai T., Tomono K., Yanagihara K., Yamamoto, Y., Kaku M., Hirakata Y. et al. (1997) Role of coagulase in a murine model of hematogenous pulmonary infection induced by intravenous injection of Staphylococcus aureus enmeshed in agar beads. Infect. Immun. 65: 466-471
    • (1997) Infect. Immun. , vol.65 , pp. 466-471
    • Sawai, T.1    Tomono, K.2    Yanagihara, K.3    Yamamoto, Y.4    Kaku, M.5    Hirakata, Y.6
  • 13
    • 0035522333 scopus 로고    scopus 로고
    • Infective endocarditis in adults
    • Mylonakis E. and Calderwood S. B. (2001) Infective endocarditis in adults. N. Engl. J. Med. 345: 1318-1330
    • (2001) N. Engl. J. Med. , vol.345 , pp. 1318-1330
    • Mylonakis, E.1    Calderwood, S.B.2
  • 14
    • 0032508547 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human plasmin complexed with streptokinase
    • Wang X., Lin X., Loy J. A., Tang J. and Zhang X.C. (1998) Crystal structure of the catalytic domain of human plasmin complexed with streptokinase. Science 281: 1662-1665
    • (1998) Science , vol.281 , pp. 1662-1665
    • Wang, X.1    Lin, X.2    Loy, J.A.3    Tang, J.4    Zhang, X.C.5
  • 15
    • 0034640546 scopus 로고    scopus 로고
    • Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen
    • Boxrud P. D., Fay W. P. and Bock P. E. (2000) Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen. J. Biol. Chem. 275: 14579-14589
    • (2000) J. Biol. Chem. , vol.275 , pp. 14579-14589
    • Boxrud, P.D.1    Fay, W.P.2    Bock, P.E.3
  • 16
    • 0018898952 scopus 로고
    • Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37 degrees C
    • Wohl R. C., Summaria L. and Robbins K. C. (1980) Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37 degrees C. J. Biol. Chem. 255: 2005-2013
    • (1980) J. Biol. Chem. , vol.255 , pp. 2005-2013
    • Wohl, R.C.1    Summaria, L.2    Robbins, K.C.3
  • 17
    • 0031596034 scopus 로고    scopus 로고
    • The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action
    • Parry M. A., Fernandez-Catalan C., Bergner A., Huber R., Hopfner K. P., Schlott B. et al. (1998) The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action. Nat. Struct. Biol. 5: 917-923
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 917-923
    • Parry, M.A.1    Fernandez-Catalan, C.2    Bergner, A.3    Huber, R.4    Hopfner, K.P.5    Schlott, B.6
  • 18
    • 0035918292 scopus 로고    scopus 로고
    • The mechanism of a bacterial plasminogen activator intermediate between streptokinase and staphylokinase
    • Sazonova I. Y., Houng A. K., Chowdhry S. A., Robinson B. R., Hedstrom L. and Reed G. L. (2001) The mechanism of a bacterial plasminogen activator intermediate between streptokinase and staphylokinase. J. Biol. Chem. 276: 12609-12613
    • (2001) J. Biol. Chem. , vol.276 , pp. 12609-12613
    • Sazonova, I.Y.1    Houng, A.K.2    Chowdhry, S.A.3    Robinson, B.R.4    Hedstrom, L.5    Reed, G.L.6
  • 19
    • 0032513149 scopus 로고    scopus 로고
    • Molecular co-operation between protein PAM and streptokinase for plasmin acquisition by Streptococcus pyogenes
    • Ringdahl U., Svensson M., Wistedt A. C., Renne T., Kellner R., Müller-Esterl W. et al. (1998) Molecular co-operation between protein PAM and streptokinase for plasmin acquisition by Streptococcus pyogenes. J. Biol. Chem. 273: 6424-6430
    • (1998) J. Biol. Chem. , vol.273 , pp. 6424-6430
    • Ringdahl, U.1    Svensson, M.2    Wistedt, A.C.3    Renne, T.4    Kellner, R.5    Müller-Esterl, W.6
  • 21
    • 0020524899 scopus 로고
    • Activation of human prothrombin by stoichiometric levels of staphylocoagulase
    • Hendrix H., Lindhout T., Mertens K., Engels W. and Hemker H. C. (1983) Activation of human prothrombin by stoichiometric levels of staphylocoagulase. J. Biol. Chem. 258: 3637-3644
    • (1983) J. Biol. Chem. , vol.258 , pp. 3637-3644
    • Hendrix, H.1    Lindhout, T.2    Mertens, K.3    Engels, W.4    Hemker, H.C.5
  • 22
  • 23
    • 0021987011 scopus 로고
    • Difference in enzymatic properties between alpha-thrombin- staphylocoagulase complex and free alpha-thrombin
    • Tokyo
    • Kawabata S., Morita T., Iwanaga S. and Igarashi H. (1985) Difference in enzymatic properties between alpha-thrombin-staphylocoagulase complex and free alpha-thrombin. J. Biochem. (Tokyo) 97: 1073-1078
    • (1985) J. Biochem. , vol.97 , pp. 1073-1078
    • Kawabata, S.1    Morita, T.2    Iwanaga, S.3    Igarashi, H.4
  • 26
    • 0033937010 scopus 로고    scopus 로고
    • Zymogen activation in the streptokinase-plasminogen complex. Ile1 is required for the formation of a functional active site
    • Wang S., Reed G. L. and Hedstrom L. (2000) Zymogen activation in the streptokinase-plasminogen complex. Ile1 is required for the formation of a functional active site. Eur. J. Biochem. 267: 3994-4001
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3994-4001
    • Wang, S.1    Reed, G.L.2    Hedstrom, L.3
  • 27
    • 0017107996 scopus 로고
    • Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin
    • Bode W. and Huber R. (1976) Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin. FEBS Lett. 68: 231-236
    • (1976) FEBS Lett. , vol.68 , pp. 231-236
    • Bode, W.1    Huber, R.2
  • 28
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution
    • Bode W., Schwager P. and Huber R. (1978) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution. J. Mol. Biol. 118: 99-112
    • (1978) J. Mol. Biol. , vol.118 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 29
    • 0018781771 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen
    • Bode W. (1979) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen. J. Mol. Biol. 127: 357-374
    • (1979) J. Mol. Biol. , vol.127 , pp. 357-374
    • Bode, W.1
  • 30
    • 0035854772 scopus 로고    scopus 로고
    • Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation
    • Boxrud P. D., Verhamme I. M., Fay W. P. and Bock P. E. (2001) Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation. J. Biol. Chem. 276: 26084-26089
    • (2001) J. Biol. Chem. , vol.276 , pp. 26084-26089
    • Boxrud, P.D.1    Verhamme, I.M.2    Fay, W.P.3    Bock, P.E.4
  • 31
    • 2342471807 scopus 로고    scopus 로고
    • The von Willebrand factor-binding protein (vWbp) of Staphylococcus aureus is a coagulase
    • Bjerketorp J., Jacobsson K. and Frykberg L. (2004) The von Willebrand factor-binding protein (vWbp) of Staphylococcus aureus is a coagulase. FEMS Microbiol. Lett. 234: 309-314
    • (2004) FEMS Microbiol. Lett. , vol.234 , pp. 309-314
    • Bjerketorp, J.1    Jacobsson, K.2    Frykberg, L.3
  • 33
    • 0037125989 scopus 로고    scopus 로고
    • Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae
    • Tettelin H., Masignani V., Cieslewicz M. J., Eisen J. A., Peterson S., Wessels M. R. et al. (2002) Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae. Proc. Natl. Acad. Sci. USA 99: 12391-12396
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12391-12396
    • Tettelin, H.1    Masignani, V.2    Cieslewicz, M.J.3    Eisen, J.A.4    Peterson, S.5    Wessels, M.R.6
  • 34
    • 18644378733 scopus 로고    scopus 로고
    • Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease
    • Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek, T. et al. (2002) Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease. Mol. Microbiol. 45: 1499-1513
    • (2002) Mol. Microbiol. , vol.45 , pp. 1499-1513
    • Glaser, P.1    Rusniok, C.2    Buchrieser, C.3    Chevalier, F.4    Frangeul, L.5    Msadek, T.6
  • 35
    • 0141678980 scopus 로고    scopus 로고
    • A novel family of fibrinogen-binding proteins in Streptococcus agalactiae
    • Jacobsson K. (2003) A novel family of fibrinogen-binding proteins in Streptococcus agalactiae. Vet. Microbiol. 96: 103-113
    • (2003) Vet. Microbiol. , vol.96 , pp. 103-113
    • Jacobsson, K.1
  • 36
    • 0037111574 scopus 로고    scopus 로고
    • Distinct and concerted functions of von Willebrand factor and fibrinogen in mural thrombus growth under high shear flow
    • Matsui H., Sugimoto M., Mizuno T., Tsuji S., Miyata S., Matsuda M. et al. (2002) Distinct and concerted functions of von Willebrand factor and fibrinogen in mural thrombus growth under high shear flow. Blood 100: 3604-3610
    • (2002) Blood , vol.100 , pp. 3604-3610
    • Matsui, H.1    Sugimoto, M.2    Mizuno, T.3    Tsuji, S.4    Miyata, S.5    Matsuda, M.6
  • 37
    • 0037315055 scopus 로고    scopus 로고
    • Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX
    • Jeng A., Sakota V., Li Z., Datta V., Beall B. and Nizet V. (2003) Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX. J. Bacteriol. 185: 1208-1217
    • (2003) J. Bacteriol. , vol.185 , pp. 1208-1217
    • Jeng, A.1    Sakota, V.2    Li, Z.3    Datta, V.4    Beall, B.5    Nizet, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.