메뉴 건너뛰기




Volumn 288, Issue 38, 2013, Pages 27494-27504

Complement-mediated opsonization of invasive group A Streptococcus pyogenes strain AP53 is regulated by the bacterial two-component cluster of virulence responder/sensor (covRS) system

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEINS; HUMAN NEUTROPHIL; OPSONOPHAGOCYTOSIS; PLASMA PROTEIN; REGULATORY SYSTEMS; SENSOR COMPONENTS; STREPTOCOCCUS PYOGENES; TRANSCRIPTIONAL REGULATOR;

EID: 84884571258     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.494864     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 33947287983 scopus 로고    scopus 로고
    • The two faces of Janus: Virulence gene regulation by CovR/S in group A streptococci
    • Churchward, G. (2007) The two faces of Janus: virulence gene regulation by CovR/S in group A streptococci. Mol. Microbiol. 64, 34-41
    • (2007) Mol. Microbiol. , vol.64 , pp. 34-41
    • Churchward, G.1
  • 2
    • 0028945555 scopus 로고
    • Insertional inactivation of virR in Streptococcus pyogenes M49 demonstrates that VirR functions as a positive regulator of ScpA, FcRA, OF, and M protein
    • McLandsborough, L. A., and Cleary, P. P. (1995) Insertional inactivation of virR in Streptococcus pyogenes M49 demonstrates that VirR functions as a positive regulator of ScpA, FcRA, OF, and M protein. FEMS Microbiol. Lett. 128, 45-51
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 45-51
    • McLandsborough, L.A.1    Cleary, P.P.2
  • 3
    • 0027394334 scopus 로고
    • Three different types of organization of the vir regulon in group A streptococci
    • Podbielski, A. (1993) Three different types of organization of the vir regulon in group A streptococci. Mol. Gen. Genet. 237, 287-300
    • (1993) Mol. Gen. Genet. , vol.237 , pp. 287-300
    • Podbielski, A.1
  • 4
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub, M. T., and Goulian, M. (2007) Specificity in two-component signal transduction pathways. Annu. Rev. Genet. 41, 121-145
    • (2007) Annu. Rev. Genet. , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 5
    • 0031027087 scopus 로고    scopus 로고
    • Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site
    • Kondo, H., Nakagawa, A., Nishihira, J., Nishimura, Y., Mizuno, T., and Tanaka, I. (1997) Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site. Nat. Struct. Biol. 4, 28-31
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 28-31
    • Kondo, H.1    Nakagawa, A.2    Nishihira, J.3    Nishimura, Y.4    Mizuno, T.5    Tanaka, I.6
  • 6
    • 2942511333 scopus 로고    scopus 로고
    • CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenes
    • Dalton, T. L., and Scott, J. R. (2004) CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenes. J. Bacteriol. 186, 3928-3937
    • (2004) J. Bacteriol. , vol.186 , pp. 3928-3937
    • Dalton, T.L.1    Scott, J.R.2
  • 9
    • 0018935575 scopus 로고
    • Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement
    • Pangburn, M. K., and Müller-Eberhard, H. J. (1980) Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement. J. Exp. Med. 152, 1102-1114
    • (1980) J. Exp. Med. , vol.152 , pp. 1102-1114
    • Pangburn, M.K.1    Müller-Eberhard, H.J.2
  • 10
    • 0022273901 scopus 로고
    • Membrane complement receptors specific for bound fragments of C3
    • Ross, G. D., and Medof, M. E. (1985) Membrane complement receptors specific for bound fragments of C3. Adv. Immunol. 37, 217-267
    • (1985) Adv. Immunol. , vol.37 , pp. 217-267
    • Ross, G.D.1    Medof, M.E.2
  • 12
    • 0017704496 scopus 로고
    • Human complement C3b inactivator: Isolation, characterization, and demonstration of an absolute requirement for the serum protein β1H for cleavage of C3b and C4b in solution
    • Pangburn, M. K., Schreiber, R. D., and Müller-Eberhard, H. J. (1977) Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein β1H for cleavage of C3b and C4b in solution. J. Exp. Med. 146, 257-270
    • (1977) J. Exp. Med. , vol.146 , pp. 257-270
    • Pangburn, M.K.1    Schreiber, R.D.2    Müller-Eberhard, H.J.3
  • 13
    • 0018073707 scopus 로고
    • Human C4-binding protein. II. Role in proteolysis of C4b by C3b-inactivator
    • Fujita, T., Gigli, I., and Nussenzweig, V. (1978) Human C4-binding protein. II. Role in proteolysis of C4b by C3b-inactivator. J. Exp. Med. 148, 1044-1051
    • (1978) J. Exp. Med. , vol.148 , pp. 1044-1051
    • Fujita, T.1    Gigli, I.2    Nussenzweig, V.3
  • 14
    • 0342316481 scopus 로고    scopus 로고
    • Human complement regulators: A major target for pathogenic microorganisms
    • Lindahl, G., Sjöbring, U., and Johnsson, E. (2000) Human complement regulators: a major target for pathogenic microorganisms. Curr. Opin. Immunol. 12, 44-51
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 44-51
    • Lindahl, G.1    Sjöbring, U.2    Johnsson, E.3
  • 15
    • 0343017792 scopus 로고
    • Antiphagocytic activity of streptococcal M protein: Selective binding of complement control protein factor H
    • Horstmann, R. D., Sievertsen, H. J., Knobloch, J., and Fischetti, V. A. (1988) Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc. Natl. Acad. Sci. U. S. A. 85, 1657-1661
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 1657-1661
    • Horstmann, R.D.1    Sievertsen, H.J.2    Knobloch, J.3    Fischetti, V.A.4
  • 17
    • 0027451350 scopus 로고
    • PAM, a novel plasminogen-binding protein from Streptococcus pyogenes
    • Berge, A., and Sjöbring, U. (1993) PAM, a novel plasminogen-binding protein from Streptococcus pyogenes. J. Biol. Chem. 268, 25417-25424
    • (1993) J. Biol. Chem. , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjöbring, U.2
  • 20
    • 84874771761 scopus 로고    scopus 로고
    • A natural inactivating mutation in the CovS component of the CovRS regulatory operon in a pattern D Streptococcal pyogenes strain influences virulence-associated genes
    • Liang, Z., Zhang, Y., Agrahari, G., Chandrahas, V., Glinton, K., Donahue, D. L., Balsara, R. D., Ploplis, V. A., and Castellino, F. J. (2013) A natural inactivating mutation in the CovS component of the CovRS regulatory operon in a pattern D Streptococcal pyogenes strain influences virulence-associated genes. J. Biol. Chem. 288, 6561-6573
    • (2013) J. Biol. Chem. , vol.288 , pp. 6561-6573
    • Liang, Z.1    Zhang, Y.2    Agrahari, G.3    Chandrahas, V.4    Glinton, K.5    Donahue, D.L.6    Balsara, R.D.7    Ploplis, V.A.8    Castellino, F.J.9
  • 22
    • 65349138252 scopus 로고    scopus 로고
    • Synergy between type 1 fimbriae expression and C3 opsonisation increases internalisation of E coli by human tubular epithelial cells
    • Li, K., Zhou, W., Hong, Y., Sacks, S. H., and Sheerin, N. S. (2009) Synergy between type 1 fimbriae expression and C3 opsonisation increases internalisation of E. coli by human tubular epithelial cells. BMCMicrobiol. 9, 64
    • (2009) BMCMicrobiol. , vol.9 , pp. 64
    • Li, K.1    Zhou, W.2    Hong, Y.3    Sacks, S.H.4    Sheerin, N.S.5
  • 23
    • 79952159557 scopus 로고    scopus 로고
    • M protein and hyaluronic acid capsule are essential for in vivo selection of covRS mutations characteristic of invasive serotype M1T1 groupAStreptococcus
    • Cole, J. N., Pence, M. A., Von Köckritz-Blickwede, M., Hollands, A., Gallo, R. L., Walker, M. J., and Nizet, V. (2010) M protein and hyaluronic acid capsule are essential for in vivo selection of covRS mutations characteristic of invasive serotype M1T1 groupAStreptococcus. MBio 1, e00191-e00210
    • (2010) MBio , vol.1
    • Cole, J.N.1    Pence, M.A.2    Von Köckritz-Blickwede, M.3    Hollands, A.4    Gallo, R.L.5    Walker, M.J.6    Nizet, V.7
  • 24
    • 67649201006 scopus 로고    scopus 로고
    • Clinical isolates of Streptococcus pneumoniae bind the complement inhibitor C4b-binding protein in a PspC allele-dependent fashion
    • Dieudonné-Vatran, A., Krentz, S., Blom, A. M., Meri, S., Henriques-Normark, B., Riesbeck, K., and Albiger, B. (2009) Clinical isolates of Streptococcus pneumoniae bind the complement inhibitor C4b-binding protein in a PspC allele-dependent fashion. J. Immunol. 182, 7865-7877
    • (2009) J. Immunol. , vol.182 , pp. 7865-7877
    • Dieudonné-Vatran, A.1    Krentz, S.2    Blom, A.M.3    Meri, S.4    Henriques-Normark, B.5    Riesbeck, K.6    Albiger, B.7
  • 25
    • 0035151019 scopus 로고    scopus 로고
    • The SpeB virulence factor of Streptococcus pyogenes, a multifunctional secreted and cell surface molecule with strepadhesin, laminin-binding and cysteine protease activity
    • Hytönen, J., Haataja, S., Gerlach, D., Podbielski, A., and Finne, J. (2001) The SpeB virulence factor of Streptococcus pyogenes, a multifunctional secreted and cell surface molecule with strepadhesin, laminin-binding and cysteine protease activity. Mol. Microbiol. 39, 512-519
    • (2001) Mol. Microbiol. , vol.39 , pp. 512-519
    • Hytönen, J.1    Haataja, S.2    Gerlach, D.3    Podbielski, A.4    Finne, J.5
  • 26
    • 36549029160 scopus 로고    scopus 로고
    • RivR and the small RNA RivX: The missing links between the CovR regulatory cascade and the Mga regulon
    • Roberts, S. A., and Scott, J. R. (2007) RivR and the small RNA RivX: the missing links between the CovR regulatory cascade and the Mga regulon. Mol. Microbiol. 66, 1506-1522
    • (2007) Mol. Microbiol. , vol.66 , pp. 1506-1522
    • Roberts, S.A.1    Scott, J.R.2
  • 28
    • 84876475534 scopus 로고    scopus 로고
    • Functional differences between Streptococcus pyogenes cluster 1 and cluster 2b streptokinases are determined by their β-domains
    • Zhang, Y., Liang, Z., Glinton, K., Ploplis, V. A., and Castellino, F. J. (2013) Functional differences between Streptococcus pyogenes cluster 1 and cluster 2b streptokinases are determined by their β-domains. FEBS Lett. 587, 1304-1309
    • (2013) FEBS Lett. , vol.587 , pp. 1304-1309
    • Zhang, Y.1    Liang, Z.2    Glinton, K.3    Ploplis, V.A.4    Castellino, F.J.5
  • 29
    • 0021972604 scopus 로고
    • Resistance to phagocytosis by group A streptococci: Failure of deposited complement opsonins to interact with cellular receptors
    • Weis, J. J., Law, S. K., Levine, R. P., and Cleary, P. P. (1985) Resistance to phagocytosis by group A streptococci: failure of deposited complement opsonins to interact with cellular receptors. J. Immunol. 134, 500-505
    • (1985) J. Immunol. , vol.134 , pp. 500-505
    • Weis, J.J.1    Law, S.K.2    Levine, R.P.3    Cleary, P.P.4
  • 30
    • 0035920160 scopus 로고    scopus 로고
    • Structural requirements for the complement regulatory activities of C4BP
    • Blom, A. M., Kask, L., and Dahlbäck, B. (2001) Structural requirements for the complement regulatory activities of C4BP. J. Biol. Chem. 276, 27136-27144
    • (2001) J. Biol. Chem. , vol.276 , pp. 27136-27144
    • Blom, A.M.1    Kask, L.2    Dahlbäck, B.3
  • 31
    • 68749105932 scopus 로고    scopus 로고
    • Stringent regulation of complement lectin pathway C3/C5 convertase by C4b-binding protein (C4BP)
    • Rawal, N., Rajagopalan, R., and Salvi, V. P. (2009) Stringent regulation of complement lectin pathway C3/C5 convertase by C4b-binding protein (C4BP). Mol. Immunol. 46, 2902-2910
    • (2009) Mol. Immunol. , vol.46 , pp. 2902-2910
    • Rawal, N.1    Rajagopalan, R.2    Salvi, V.P.3
  • 33
    • 1242318719 scopus 로고    scopus 로고
    • Mouse skin passage of Streptococcus pyogenes results in increased streptokinase expression and activity
    • Rezcallah, M. S., Boyle, M. D., and Sledjeski, D. D. (2004) Mouse skin passage of Streptococcus pyogenes results in increased streptokinase expression and activity. Microbiology 150, 365-371
    • (2004) Microbiology , vol.150 , pp. 365-371
    • Rezcallah, M.S.1    Boyle, M.D.2    Sledjeski, D.D.3
  • 34
    • 84871325888 scopus 로고    scopus 로고
    • Characterization of streptokinases from Group A streptococci reveals a strong functional relationship that supports the coinheritance of plasminogenbinding M-protein and cluster 2b streptokinase
    • Zhang, Y., Liang, Z., Hsueh, H. T., Ploplis, V. A., and Castellino, F. J. (2012) Characterization of streptokinases from Group A streptococci reveals a strong functional relationship that supports the coinheritance of plasminogenbinding M-protein and cluster 2b streptokinase. J. Biol. Chem. 287, 42093-42103
    • (2012) J. Biol. Chem. , vol.287 , pp. 42093-42103
    • Zhang, Y.1    Liang, Z.2    Hsueh, H.T.3    Ploplis, V.A.4    Castellino, F.J.5
  • 35
    • 9144264267 scopus 로고    scopus 로고
    • Interaction between complement regulators and Streptococcus pyogenes: Binding of C4b-binding protein and factor H/factor H-like protein 1 to M18 strains involves two different cell surface molecules
    • Pérez-Caballero, D., García-Laorden, I., Cortés, G., Wessels, M. R., De Córdoba, S. R., and Albertí, S. (2004) Interaction between complement regulators and Streptococcus pyogenes: binding of C4b-binding protein and factor H/factor H-like protein 1 to M18 strains involves two different cell surface molecules. J. Immunol. 173, 6899-6904
    • (2004) J. Immunol. , vol.173 , pp. 6899-6904
    • Pérez-Caballero, D.1    García-Laorden, I.2    Cortés, G.3    Wessels, M.R.4    De Córdoba, S.R.5    Albertí, S.6
  • 36
    • 33645650398 scopus 로고    scopus 로고
    • Human C4b-binding protein, structural basis for interaction with streptococcalMprotein, a major bacterial virulence factor
    • Jenkins, H. T., Mark, L., Ball, G., Persson, J., Lindahl, G., Uhrin, D., Blom, A. M., and Barlow, P. N. (2006) Human C4b-binding protein, structural basis for interaction with streptococcalMprotein, a major bacterial virulence factor. J. Biol. Chem. 281, 3690-3697
    • (2006) J. Biol. Chem. , vol.281 , pp. 3690-3697
    • Jenkins, H.T.1    Mark, L.2    Ball, G.3    Persson, J.4    Lindahl, G.5    Uhrin, D.6    Blom, A.M.7    Barlow, P.N.8
  • 37
    • 84866554657 scopus 로고    scopus 로고
    • Enolase of Streptococcus pneumoniae binds human complement inhibitor C4b-binding protein and contributes to complement evasion
    • Agarwal, V., Hammerschmidt, S., Malm, S., Bergmann, S., Riesbeck, K., and Blom, A. M. (2012) Enolase of Streptococcus pneumoniae binds human complement inhibitor C4b-binding protein and contributes to complement evasion. J. Immunol. 189, 3575-3584
    • (2012) J. Immunol. , vol.189 , pp. 3575-3584
    • Agarwal, V.1    Hammerschmidt, S.2    Malm, S.3    Bergmann, S.4    Riesbeck, K.5    Blom, A.M.6
  • 38
    • 0036841294 scopus 로고    scopus 로고
    • Acquisition of regulators of complement activation by Streptococcus pyogenes serotype M1
    • Pandiripally, V., Gregory, E., and Cue, D. (2002) Acquisition of regulators of complement activation by Streptococcus pyogenes serotype M1. Infect. Immun. 70, 6206-6214
    • (2002) Infect. Immun. , vol.70 , pp. 6206-6214
    • Pandiripally, V.1    Gregory, E.2    Cue, D.3
  • 39
    • 4644303454 scopus 로고    scopus 로고
    • The emerging pathogen Moraxella catarrhalis interacts with complement inhibitor C4b binding protein through ubiquitous surface proteins A1 and A2
    • Nordström, T., Blom, A. M., Forsgren, A., and Riesbeck, K. (2004) The emerging pathogen Moraxella catarrhalis interacts with complement inhibitor C4b binding protein through ubiquitous surface proteins A1 and A2. J. Immunol. 173, 4598-4606
    • (2004) J. Immunol. , vol.173 , pp. 4598-4606
    • Nordström, T.1    Blom, A.M.2    Forsgren, A.3    Riesbeck, K.4
  • 40
    • 84865199168 scopus 로고    scopus 로고
    • Lsa30, a novel adhesin of Leptospira interrogans binds human plasminogen and the complement regulator C4bp
    • Souza, N. M., Vieira, M. L., Alves, I. J., De Morais, Z. M., Vasconcellos, S. A., and Nascimento, A. L. (2012) Lsa30, a novel adhesin of Leptospira interrogans binds human plasminogen and the complement regulator C4bp. Microb. Pathog. 53, 125-134
    • (2012) Microb. Pathog. , vol.53 , pp. 125-134
    • Souza, N.M.1    Vieira, M.L.2    Alves, I.J.3    De Morais, Z.M.4    Vasconcellos, S.A.5    Nascimento, A.L.6
  • 41
    • 77149129877 scopus 로고    scopus 로고
    • Binding of the complement inhibitor C4b-binding protein to Lyme disease Borreliae
    • Pietikäinen, J., Meri, T., Blom, A. M., and Meri, S. (2010) Binding of the complement inhibitor C4b-binding protein to Lyme disease Borreliae. Mol. Immunol. 47, 1299-1305
    • (2010) Mol. Immunol. , vol.47 , pp. 1299-1305
    • Pietikäinen, J.1    Meri, T.2    Blom, A.M.3    Meri, S.4
  • 42
    • 0032856769 scopus 로고    scopus 로고
    • A twocomponent regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B
    • Heath, A., DiRita, V. J., Barg, N. L., and Engleberg, N. C. (1999) A twocomponent regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B. Infect. Immun. 67, 5298-5305
    • (1999) Infect. Immun. , vol.67 , pp. 5298-5305
    • Heath, A.1    Di Rita, V.J.2    Barg, N.L.3    Engleberg, N.C.4
  • 43
    • 67651230633 scopus 로고    scopus 로고
    • CovS simultaneously activates and inhibits the CovR-mediated repression of distinct subsets of group A Streptococcus virulence factor-encoding genes
    • Treviño, J., Perez, N., Ramirez-Peña, E., Liu, Z., Shelburne, S. A., 3rd, Musser, J. M., and Sumby, P. (2009) CovS simultaneously activates and inhibits the CovR-mediated repression of distinct subsets of group A Streptococcus virulence factor-encoding genes. Infect. Immun. 77, 3141-3149
    • (2009) Infect. Immun. , vol.77 , pp. 3141-3149
    • Treviño, J.1    Perez, N.2    Ramirez-Peña, E.3    Liu, Z.4    Shelburne III, S.A.5    Musser, J.M.6    Sumby, P.7
  • 44
    • 77954082501 scopus 로고    scopus 로고
    • Highly frequent mutations in negative regulators of multiple virulence genes in group A streptococcal toxic shock syndrome isolates
    • Ikebe, T., Ato, M., Matsumura, T., Hasegawa, H., Sata, T., Kobayashi, K., and Watanabe, H. (2010) Highly frequent mutations in negative regulators of multiple virulence genes in group A streptococcal toxic shock syndrome isolates. PLoS Pathog. 6, e1000832
    • (2010) PLoS Pathog. , vol.6
    • Ikebe, T.1    Ato, M.2    Matsumura, T.3    Hasegawa, H.4    Sata, T.5    Kobayashi, K.6    Watanabe, H.7
  • 46
    • 54949129776 scopus 로고    scopus 로고
    • Incompetence of neutrophils to invasive group A Streptococcus is attributed to induction of plural virulence factors by dysfunction of a regulator
    • Ato, M., Ikebe, T., Kawabata, H., Takemori, T., and Watanabe, H. (2008) Incompetence of neutrophils to invasive group A Streptococcus is attributed to induction of plural virulence factors by dysfunction of a regulator. PLoS One 3, e3455
    • (2008) PLoS One , vol.3
    • Ato, M.1    Ikebe, T.2    Kawabata, H.3    Takemori, T.4    Watanabe, H.5
  • 47
    • 0032038665 scopus 로고    scopus 로고
    • M protein of the group A Streptococcus binds to the seventh short consensus repeat of human complement factor H
    • Blackmore, T. K., Fischetti, V. A., Sadlon, T. A., Ward, H. M., and Gordon, D. L. (1998) M protein of the group A Streptococcus binds to the seventh short consensus repeat of human complement factor H. Infect. Immun. 66, 1427-1431
    • (1998) Infect. Immun. , vol.66 , pp. 1427-1431
    • Blackmore, T.K.1    Fischetti, V.A.2    Sadlon, T.A.3    Ward, H.M.4    Gordon, D.L.5
  • 48
    • 0035724292 scopus 로고    scopus 로고
    • Fba, a novel fibronectin-binding protein from Streptococcus pyogenes, promotes bacterial entry into epithelial cells, and the fba gene is positively transcribed under the Mga regulator
    • Terao, Y., Kawabata, S., Kunitomo, E., Murakami, J., Nakagawa, I., and Hamada, S. (2001) Fba, a novel fibronectin-binding protein from Streptococcus pyogenes, promotes bacterial entry into epithelial cells, and the fba gene is positively transcribed under the Mga regulator. Mol. Microbiol. 42, 75-86
    • (2001) Mol. Microbiol. , vol.42 , pp. 75-86
    • Terao, Y.1    Kawabata, S.2    Kunitomo, E.3    Murakami, J.4    Nakagawa, I.5    Hamada, S.6
  • 49
    • 84861566815 scopus 로고    scopus 로고
    • Plasminogen is a complement inhibitor
    • Barthel, D., Schindler, S., and Zipfel, P. F. (2012) Plasminogen is a complement inhibitor. J. Biol. Chem. 287, 18831-18842
    • (2012) J. Biol. Chem. , vol.287 , pp. 18831-18842
    • Barthel, D.1    Schindler, S.2    Zipfel, P.F.3
  • 50
    • 84869060662 scopus 로고    scopus 로고
    • Plasminogen binding proteins and plasmin generation on the surface of Leptospira spp.: The contribution to the bacteria-host interactions
    • Vieira, M. L., Atzingen, M. V., Oliveira, R., Mendes, R. S., Domingos, R. F., Vasconcellos, S. A., and Nascimento, A. L. (2012) Plasminogen binding proteins and plasmin generation on the surface of Leptospira spp.: the contribution to the bacteria-host interactions. J. Biomed. Biotechnol. 2012, 758513
    • (2012) J. Biomed. Biotechnol. , vol.2012 , pp. 758513
    • Vieira, M.L.1    Atzingen, M.V.2    Oliveira, R.3    Mendes, R.S.4    Domingos, R.F.5    Vasconcellos, S.A.6    Nascimento, A.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.