메뉴 건너뛰기




Volumn 191, Issue 15, 2009, Pages 4758-4766

The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2 ANTIPLASMIN; AMPICILLIN; ASPARTIC PROTEINASE; BACTERIAL PROTEIN; CELL SURFACE PROTEIN; GLUCOSE; PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATOR; TETRACYCLINE;

EID: 67749127374     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00489-09     Document Type: Article
Times cited : (23)

References (61)
  • 2
    • 0033598784 scopus 로고    scopus 로고
    • Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis
    • Achtman, M., K. Aurth, G. Morelli, G. Torrea, A. Guiyoule, and E. Carniel. 1999. Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis. Proc. Natl. Acad. Sci. USA 96:14043-14048.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14043-14048
    • Achtman, M.1    Aurth, K.2    Morelli, G.3    Torrea, G.4    Guiyoule, A.5    Carniel, E.6
  • 4
    • 0014109014 scopus 로고
    • Pesticins. 3. Expression of coagulase and mechanism of fibrinolysis
    • Beesley, E. D., R. R. Brubaker, W. A. Janssen, and M. J. Surgalla. 1967. Pesticins. 3. Expression of coagulase and mechanism of fibrinolysis. J. Bacteriol. 94:19-26.
    • (1967) J. Bacteriol , vol.94 , pp. 19-26
    • Beesley, E.D.1    Brubaker, R.R.2    Janssen, W.A.3    Surgalla, M.J.4
  • 5
    • 34548667697 scopus 로고    scopus 로고
    • Fibrinolysis and host response in bacterial infections
    • Bergmann, S., and S. Hammerschmidt. 2007. Fibrinolysis and host response in bacterial infections. Thromb. Haemost. 98:512-520.
    • (2007) Thromb. Haemost , vol.98 , pp. 512-520
    • Bergmann, S.1    Hammerschmidt, S.2
  • 6
    • 33744980249 scopus 로고    scopus 로고
    • Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: Evidence of gene reduction in an emerging pathogen
    • Chain, P. S. G., P. Hu, S. A. Malfatti, L. Radnedge, F. Larimer, L. M. Vergez, P. Worsham, M. C. Chu, and G. L. Andersen. 2006. Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen. J. Bacteriol. 188:4453-4463.
    • (2006) J. Bacteriol , vol.188 , pp. 4453-4463
    • Chain, P.S.G.1    Hu, P.2    Malfatti, S.A.3    Radnedge, L.4    Larimer, F.5    Vergez, L.M.6    Worsham, P.7    Chu, M.C.8    Andersen, G.L.9
  • 8
    • 34250736946 scopus 로고    scopus 로고
    • Fibrin and fibrinolysis in infection and host defense
    • Degen, J. L., T. H. Bugge, and J. D. Goguen. 2007. Fibrin and fibrinolysis in infection and host defense. J. Thromb. Haemost. 5(Suppl. 1):24-31.
    • (2007) J. Thromb. Haemost , vol.5 , Issue.SUPPL. 1 , pp. 24-31
    • Degen, J.L.1    Bugge, T.H.2    Goguen, J.D.3
  • 9
    • 0029824356 scopus 로고    scopus 로고
    • Identification of plasminogen in Matrigel and its activation by reconstitution of this basement membrane extract
    • Farina, A. R., A. Tiberio, A. Tacconelli, L. Cappabianca, A. Gulino, and A. R. Mackay. 1996. Identification of plasminogen in Matrigel and its activation by reconstitution of this basement membrane extract. BioTechniques 21:904-909.
    • (1996) BioTechniques , vol.21 , pp. 904-909
    • Farina, A.R.1    Tiberio, A.2    Tacconelli, A.3    Cappabianca, L.4    Gulino, A.5    Mackay, A.R.6
  • 10
    • 0019435820 scopus 로고
    • Plasmids in Yersinia pestis
    • Ferber, D. M., and R. R. Brubaker. 1981. Plasmids in Yersinia pestis. Infect. Immun. 31:839-841.
    • (1981) Infect. Immun , vol.31 , pp. 839-841
    • Ferber, D.M.1    Brubaker, R.R.2
  • 11
    • 0014312753 scopus 로고
    • Studies on the pathogenesis of plague. Blood coagulation and tissue responses of Macaca mulatta following exposure to aerosols of Pasteurella pestis
    • Finegold, M. J., J. J. Petery, R. F. Berendt, and H. R. Adams. 1968. Studies on the pathogenesis of plague. Blood coagulation and tissue responses of Macaca mulatta following exposure to aerosols of Pasteurella pestis. Am. J. Pathol. 53:99-114.
    • (1968) Am. J. Pathol , vol.53 , pp. 99-114
    • Finegold, M.J.1    Petery, J.J.2    Berendt, R.F.3    Adams, H.R.4
  • 13
    • 0034428360 scopus 로고    scopus 로고
    • Role of the pleiotropic effects of plasminogen deficiency in infection experiments with plasminogen-deficient mice
    • Goguen, J. D., T. Bugge, and J. L. Degen. 2000. Role of the pleiotropic effects of plasminogen deficiency in infection experiments with plasminogen-deficient mice. Methods 21:179-183.
    • (2000) Methods , vol.21 , pp. 179-183
    • Goguen, J.D.1    Bugge, T.2    Degen, J.L.3
  • 14
    • 0033919460 scopus 로고    scopus 로고
    • A PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides
    • Guina, T., E. C. Yi, H. Wang, M. Hackett, and S. I. Miller. 2000. A PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides. J. Bacteriol. 182:4077-4086.
    • (2000) J. Bacteriol , vol.182 , pp. 4077-4086
    • Guina, T.1    Yi, E.C.2    Wang, H.3    Hackett, M.4    Miller, S.I.5
  • 15
    • 63349105215 scopus 로고    scopus 로고
    • Breaking barriers - attack on innate immune defences by omptin surface proteases of enterobacterial pathogens
    • Haiko, J., M. Suomalainen, T. Ojala, K. Lähteenmäki, and T. K. Korhonen. 2009. Breaking barriers - attack on innate immune defences by omptin surface proteases of enterobacterial pathogens. Innate Immun. 15:67-80.
    • (2009) Innate Immun , vol.15 , pp. 67-80
    • Haiko, J.1    Suomalainen, M.2    Ojala, T.3    Lähteenmäki, K.4    Korhonen, T.K.5
  • 16
    • 33947267107 scopus 로고    scopus 로고
    • General and specific host responses to bacterial infection in Peyer's patches: A role for stromelysin-1 (matrix metalloproteinase-3) during Salmonella enterica infection
    • Handley, S. A., and V. L. Miller. 2007. General and specific host responses to bacterial infection in Peyer's patches: a role for stromelysin-1 (matrix metalloproteinase-3) during Salmonella enterica infection. Mol. Microbiol. 64:94-110.
    • (2007) Mol. Microbiol , vol.64 , pp. 94-110
    • Handley, S.A.1    Miller, V.L.2
  • 17
    • 34548067653 scopus 로고    scopus 로고
    • Omptin proteins: An expanding family of outer membrane proteases in gram-negative Enterobacteriaceae
    • Hritonenko, V., and C. Stathopoulos. 2007. Omptin proteins: an expanding family of outer membrane proteases in gram-negative Enterobacteriaceae. Mol. Membr. Biol. 24:395-406.
    • (2007) Mol. Membr. Biol , vol.24 , pp. 395-406
    • Hritonenko, V.1    Stathopoulos, C.2
  • 19
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik, R., K. P. Locher, and P. Van Gelder. 2000. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37:239-253.
    • (2000) Mol. Microbiol , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 20
    • 0000983237 scopus 로고    scopus 로고
    • In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT
    • Kramer, R. A., D. Zandwijken, M. R. Egmond, and N. Dekker. 2000. In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT. Eur. J. Biochem. 267:885-893.
    • (2000) Eur. J. Biochem , vol.267 , pp. 885-893
    • Kramer, R.A.1    Zandwijken, D.2    Egmond, M.R.3    Dekker, N.4
  • 21
    • 3142737933 scopus 로고    scopus 로고
    • The omptin family of enterobacterial surface proteases/adhesins: From housekeeping in Escherichia coli to systemic spread of Yersinia pestis
    • Kukkonen, M., and T. K. Korhonen. 2004. The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis. Int. J. Med. Microbiol. 294:7-14.
    • (2004) Int. J. Med. Microbiol , vol.294 , pp. 7-14
    • Kukkonen, M.1    Korhonen, T.K.2
  • 24
    • 0033020422 scopus 로고    scopus 로고
    • Expression of the plague plasminogen activator in Yersinia pseudotuberculosis and Escherichia coli
    • Kutyrev, V., R. J. Mehigh, V. L. Motin, M. S. Pokrovskaya, G. B. Smirnov, and R. R. Brubaker. 1999. Expression of the plague plasminogen activator in Yersinia pseudotuberculosis and Escherichia coli. Infect. Immun. 67:1359-1367.
    • (1999) Infect. Immun , vol.67 , pp. 1359-1367
    • Kutyrev, V.1    Mehigh, R.J.2    Motin, V.L.3    Pokrovskaya, M.S.4    Smirnov, G.B.5    Brubaker, R.R.6
  • 25
    • 12944325306 scopus 로고    scopus 로고
    • Bacterial metastasis: The host plasminogen system in bacterial invasion
    • Lähteenmäki, K., S. Edelman, and T. K. Korhonen. 2005. Bacterial metastasis: the host plasminogen system in bacterial invasion. Trends Microbiol. 13:79-85.
    • (2005) Trends Microbiol , vol.13 , pp. 79-85
    • Lähteenmäki, K.1    Edelman, S.2    Korhonen, T.K.3
  • 26
    • 15944400320 scopus 로고    scopus 로고
    • Antiprotease inactivation by Salmonella enterica released from infected macrophages
    • Lähteenmäki, K., P. Kyllönen, L. Partanen, and T. K. Korhonen. 2005. Antiprotease inactivation by Salmonella enterica released from infected macrophages. Cell. Microbiol. 7:529-538.
    • (2005) Cell. Microbiol , vol.7 , pp. 529-538
    • Lähteenmäki, K.1    Kyllönen, P.2    Partanen, L.3    Korhonen, T.K.4
  • 27
    • 0031771558 scopus 로고    scopus 로고
    • Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix
    • Lähteenmäki, K., R. Virkola, A. Saren, L. Emody, and T. K. Korhonen. 1998. Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix. Infect. Immun. 66:5755-5762.
    • (1998) Infect. Immun , vol.66 , pp. 5755-5762
    • Lähteenmäki, K.1    Virkola, R.2    Saren, A.3    Emody, L.4    Korhonen, T.K.5
  • 28
    • 33846645905 scopus 로고    scopus 로고
    • A plasminogen-activating protease specifically controls the development of primary pneumonic plague
    • Lathem, W. W., P. A. Price, V. L. Miller, and W. E. Goldman. 2007. A plasminogen-activating protease specifically controls the development of primary pneumonic plague. Science 315:509-513.
    • (2007) Science , vol.315 , pp. 509-513
    • Lathem, W.W.1    Price, P.A.2    Miller, V.L.3    Goldman, W.E.4
  • 29
    • 0029064587 scopus 로고
    • Mechanisms of physiological fibrinolysis
    • Lijnen, H. R., and D. Collen. 1995. Mechanisms of physiological fibrinolysis. Baillieres Clin. Haematol. 8:277-290.
    • (1995) Baillieres Clin. Haematol , vol.8 , pp. 277-290
    • Lijnen, H.R.1    Collen, D.2
  • 31
    • 0024412413 scopus 로고
    • A Yersinia pestis-specific DNA fragment encodes temperature-dependent coagulase and fibrinolysin-associated phenotypes
    • McDonough, K. A., and S. Falkow. 1989. A Yersinia pestis-specific DNA fragment encodes temperature-dependent coagulase and fibrinolysin-associated phenotypes. Mol. Microbiol. 3:767-775.
    • (1989) Mol. Microbiol , vol.3 , pp. 767-775
    • McDonough, K.A.1    Falkow, S.2
  • 32
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti, P., and D. B. Rifkin. 1993. Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev. 73:161-195.
    • (1993) Physiol. Rev , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 33
    • 0017037714 scopus 로고
    • Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12
    • Nakamura, K., and S. Mizushima. 1976. Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12. J. Biochem. 80:1411-1422.
    • (1976) J. Biochem , vol.80 , pp. 1411-1422
    • Nakamura, K.1    Mizushima, S.2
  • 36
    • 0031029062 scopus 로고    scopus 로고
    • Yersinia pestis - etiologic agent of plague
    • Perry, R. D., and J. D. Fetherston. 1997. Yersinia pestis - etiologic agent of plague. Clin. Microbiol. Rev. 10:35-66.
    • (1997) Clin. Microbiol. Rev , vol.10 , pp. 35-66
    • Perry, R.D.1    Fetherston, J.D.2
  • 39
    • 34247182998 scopus 로고    scopus 로고
    • The surface protease PgtE of Salmonella enterica affects complement activity by proteolytically cleaving C3b, C4b and C5
    • Ramu, P., R. Tanskanen, M. Holmberg, K. Lähteenmäki, T. K. Korhonen, and S. Meri. 2007. The surface protease PgtE of Salmonella enterica affects complement activity by proteolytically cleaving C3b, C4b and C5. FEBS Lett. 581:1716-1720.
    • (2007) FEBS Lett , vol.581 , pp. 1716-1720
    • Ramu, P.1    Tanskanen, R.2    Holmberg, M.3    Lähteenmäki, K.4    Korhonen, T.K.5    Meri, S.6
  • 42
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European Molecular Biology Open Software Suite
    • Rice, P., I. Longden, and A. Bleasby. 2000. EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet. 16:276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 43
    • 33645788354 scopus 로고    scopus 로고
    • Role of the Yersinia pestis plasminogen activator in the incidence of distinct septicemic and bubonic forms of flea-borne plague
    • Sebbane, F., C. O. Jarrett, D. Gardner, D. Long, and B. J. Hinnebusch. 2006. Role of the Yersinia pestis plasminogen activator in the incidence of distinct septicemic and bubonic forms of flea-borne plague. Proc. Natl. Acad. Sci. USA 103:5526-5530.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5526-5530
    • Sebbane, F.1    Jarrett, C.O.2    Gardner, D.3    Long, D.4    Hinnebusch, B.J.5
  • 44
    • 17844375136 scopus 로고    scopus 로고
    • Kinetics of disease progression and host response in a rat model of bubonic plague
    • Sebbane, F., D. Gardner, D. Long, B. B. Gowen, and B. J. Hinnebusch. 2005. Kinetics of disease progression and host response in a rat model of bubonic plague. Am. J. Pathol. 166:1427-1439.
    • (2005) Am. J. Pathol , vol.166 , pp. 1427-1439
    • Sebbane, F.1    Gardner, D.2    Long, D.3    Gowen, B.B.4    Hinnebusch, B.J.5
  • 46
    • 0033925196 scopus 로고    scopus 로고
    • Characterization of the O-antigen gene clusters of Yersinia pseudotuberculosis and the cryptic O-antigen gene cluster of Yersinia pestis shows that the plague bacillus is most closely related to and has evolved from Y. pseudotuberculosis serotype O:1b
    • Skurnik, M., A. Peippo, and E. Ervela. 2000. Characterization of the O-antigen gene clusters of Yersinia pseudotuberculosis and the cryptic O-antigen gene cluster of Yersinia pestis shows that the plague bacillus is most closely related to and has evolved from Y. pseudotuberculosis serotype O:1b. Mol. Microbiol. 37:316-330.
    • (2000) Mol. Microbiol , vol.37 , pp. 316-330
    • Skurnik, M.1    Peippo, A.2    Ervela, E.3
  • 47
    • 0024563389 scopus 로고
    • Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: Relationship to ompT of Escherichia coli and gene E of Salmonella typhimurium
    • Sodeinde, O. A., and J. D. Goguen. 1989. Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: relationship to ompT of Escherichia coli and gene E of Salmonella typhimurium. Infect. Immun. 57:1517-1523.
    • (1989) Infect. Immun , vol.57 , pp. 1517-1523
    • Sodeinde, O.A.1    Goguen, J.D.2
  • 48
    • 0023715723 scopus 로고
    • Genetic analysis of the 9.5-kilobase virulence plasmid of Yersinia pestis
    • Sodeinde, O. A., and J. D. Goguen. 1988. Genetic analysis of the 9.5-kilobase virulence plasmid of Yersinia pestis. Infect. Immun. 56:2743-2748.
    • (1988) Infect. Immun , vol.56 , pp. 2743-2748
    • Sodeinde, O.A.1    Goguen, J.D.2
  • 51
    • 0014199226 scopus 로고
    • The isolation and characterization of the S-carboxymethyl β (light) chain derivative of human plasmin. The localization of the active site on the β (light) chain
    • Summaria, L., B. Hsieh, W. R. Groskopf, and K. C. Robbins. 1967. The isolation and characterization of the S-carboxymethyl β (light) chain derivative of human plasmin. The localization of the active site on the β (light) chain. J. Biol. Chem. 242:5046-5052.
    • (1967) J. Biol. Chem , vol.242 , pp. 5046-5052
    • Summaria, L.1    Hsieh, B.2    Groskopf, W.R.3    Robbins, K.C.4
  • 53
    • 65249177164 scopus 로고    scopus 로고
    • Directed enzyme evolution: Climbing fitness peaks one amino acid at a time
    • Tracewell, C. A., and F. H. Arnold. 2009. Directed enzyme evolution: climbing fitness peaks one amino acid at a time. Curr. Opin. Chem. Biol. 13:3-9.
    • (2009) Curr. Opin. Chem. Biol , vol.13 , pp. 3-9
    • Tracewell, C.A.1    Arnold, F.H.2
  • 55
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • Vandeputte-Rutten, L., R. A. Kramer, J. Kroon, N. Dekker, M. R. Egmond, and P. Gros. 2001. Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J. 20:5033-5039.
    • (2001) EMBO J , vol.20 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 56
    • 18744388856 scopus 로고    scopus 로고
    • Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
    • Varadarajan, N., J. Gam, M. J. Olsen, G. Georgiou, and B. L. Iverson. 2005. Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity. Proc. Natl. Acad. Sci. USA 102:6855-6860.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6855-6860
    • Varadarajan, N.1    Gam, J.2    Olsen, M.J.3    Georgiou, G.4    Iverson, B.L.5
  • 57
    • 1342292545 scopus 로고    scopus 로고
    • The yersiniae - a model genus to study the rapid evolution of bacterial pathogens
    • Wren, B. W. 2003. The yersiniae - a model genus to study the rapid evolution of bacterial pathogens. Nat. Rev. Microbiol. 1:55-64.
    • (2003) Nat. Rev. Microbiol , vol.1 , pp. 55-64
    • Wren, B.W.1
  • 59
    • 5644235022 scopus 로고    scopus 로고
    • Comparative and evolutionary genomics of Yersinia pestis
    • Zhou, D., Y. Han, Y. Song, P. Huang, and R. Yang. 2004. Comparative and evolutionary genomics of Yersinia pestis. Microbes Infect. 6:1226-1234.
    • (2004) Microbes Infect , vol.6 , pp. 1226-1234
    • Zhou, D.1    Han, Y.2    Song, Y.3    Huang, P.4    Yang, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.