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Volumn 189, Issue 4, 2007, Pages 1435-1440

The plasminogen-binding group A streptococcal M protein-related protein Prp binds plasminogen via arginine and histidine residues

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; BACTERIAL PROTEIN; HISTIDINE; M PROTEIN; PLASMINOGEN; PROTEIN PRP; UNCLASSIFIED DRUG;

EID: 33846929584     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01218-06     Document Type: Conference Paper
Times cited : (59)

References (35)
  • 1
    • 0031552061 scopus 로고    scopus 로고
    • The human ENO1 gene product (recombinant human alpha-enolase) displays characteristics required for a plasminogen binding protein
    • Andronicos, N. M., M. Ranson, J. Bognacki, and M. S. Baker. 1997. The human ENO1 gene product (recombinant human alpha-enolase) displays characteristics required for a plasminogen binding protein. Biochim. Biophys. Acta 1337:27-39.
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 27-39
    • Andronicos, N.M.1    Ranson, M.2    Bognacki, J.3    Baker, M.S.4
  • 2
    • 0028360283 scopus 로고
    • Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins
    • Ben Nasr, A., A. Wistedt, U. Ringdahl, and U. Sjobring. 1994. Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins. Eur. J. Biochem. 222:267-276.
    • (1994) Eur. J. Biochem , vol.222 , pp. 267-276
    • Ben Nasr, A.1    Wistedt, A.2    Ringdahl, U.3    Sjobring, U.4
  • 3
    • 0027451350 scopus 로고
    • PAM, a novel plasminogen-binding protein from Streptococcus pyogenes
    • Berge, A., and U. Sjobring. 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    Sjobring, U.2
  • 4
    • 0025757268 scopus 로고
    • Isolation of a prokaryotic plasmin receptor. Relationship to a plasminogen activator produced by the same micro-organism
    • Broder, C. C., R. Lottenberg, G. O. von Mering, K. H. Johnston, and M. D. Boyle. 1991. Isolation of a prokaryotic plasmin receptor. Relationship to a plasminogen activator produced by the same micro-organism. J. Biol. Chem. 266:4922-4928.
    • (1991) J. Biol. Chem , vol.266 , pp. 4922-4928
    • Broder, C.C.1    Lottenberg, R.2    von Mering, G.O.3    Johnston, K.H.4    Boyle, M.D.5
  • 7
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M. W. 2000. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 13:470-511.
    • (2000) Clin. Microbiol. Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 10
    • 0027146666 scopus 로고
    • Controlled formation of model homo- and heterodimer coiled coil polypeptides
    • Graddis, T. J., D. G. Myszka, and I. M. Chaiken. 1993. Controlled formation of model homo- and heterodimer coiled coil polypeptides. Biochemistry 32:12664-12671.
    • (1993) Biochemistry , vol.32 , pp. 12664-12671
    • Graddis, T.J.1    Myszka, D.G.2    Chaiken, I.M.3
  • 11
    • 0027281174 scopus 로고
    • Nucleotide substitutions and small-scale insertion produce size and antigenic variation in group A streptococcal M1 protein
    • Harbaugh, M. P., A. Podbielski, S. Hugl, and P. P. Cleary. 1993. Nucleotide substitutions and small-scale insertion produce size and antigenic variation in group A streptococcal M1 protein. Mol. Microbiol. 8:981-991.
    • (1993) Mol. Microbiol , vol.8 , pp. 981-991
    • Harbaugh, M.P.1    Podbielski, A.2    Hugl, S.3    Cleary, P.P.4
  • 12
    • 0027174042 scopus 로고
    • Structural heterogeneity of the emm gene cluster in group A streptococci
    • Hollingshead, S. K., T. L. Readdy, D. L. Yung, and D. E. Bessen. 1993. Structural heterogeneity of the emm gene cluster in group A streptococci. Mol. Microbiol. 8:707-717.
    • (1993) Mol. Microbiol , vol.8 , pp. 707-717
    • Hollingshead, S.K.1    Readdy, T.L.2    Yung, D.L.3    Bessen, D.E.4
  • 13
    • 0035861456 scopus 로고    scopus 로고
    • Bayesian inference of phylogeny and its impact on evolutionary biology
    • Huelsenbeck, J. P., F. Ronquist, R. Nielsen, and J. P. Bollback. 2001. Bayesian inference of phylogeny and its impact on evolutionary biology. Science 294:2310-2314.
    • (2001) Science , vol.294 , pp. 2310-2314
    • Huelsenbeck, J.P.1    Ronquist, F.2    Nielsen, R.3    Bollback, J.P.4
  • 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
  • 16
    • 33645070309 scopus 로고    scopus 로고
    • Domains of group A streptococcal M protein that confer resistance to phagocytosis, opsonization and protection: Implications for vaccine development
    • McArthur, J. D., and M. J. Walker. 2006. Domains of group A streptococcal M protein that confer resistance to phagocytosis, opsonization and protection: implications for vaccine development. Mol. Microbiol. 59:1-4.
    • (2006) Mol. Microbiol , vol.59 , pp. 1-4
    • McArthur, J.D.1    Walker, M.J.2
  • 18
    • 0032486286 scopus 로고    scopus 로고
    • Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V., and V. A. Fischetti. 1998. Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 273:14503-14515.
    • (1998) J. Biol. Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 19
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V., and V. A. Fischetti. 1992. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J Exp. Med. 176:415-426.
    • (1992) J Exp. Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 22
    • 0027260720 scopus 로고
    • Identification of an extracellular plasmin binding protein from nephritogenic streptococci
    • Poon-King, R., J. Bannan, A. Viteri, G. Cu, and J. B. Zabriskie. 1993. Identification of an extracellular plasmin binding protein from nephritogenic streptococci. J. Exp. Med. 178:759-763.
    • (1993) J. Exp. Med , vol.178 , pp. 759-763
    • Poon-King, R.1    Bannan, J.2    Viteri, A.3    Cu, G.4    Zabriskie, J.B.5
  • 23
    • 0034978793 scopus 로고    scopus 로고
    • Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A streptococcal surface protein
    • Rios-Steiner, J. L., M. Schenone, I. Mochalkin, A. Tulinsky, and F. J. Castellino. 2001. Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A streptococcal surface protein. J. Mol. Biol. 308:705-719.
    • (2001) J. Mol. Biol , vol.308 , pp. 705-719
    • Rios-Steiner, J.L.1    Schenone, M.2    Mochalkin, I.3    Tulinsky, A.4    Castellino, F.J.5
  • 24
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist, F., and J. P. Huelsenbeck. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 26
    • 33645650114 scopus 로고    scopus 로고
    • Divergence in the plasminogen-binding group A streptococcal M protein family: Functional conservation of binding site and potential role for immune selection of variants
    • Sanderson-Smith, M., M. Batzloff, K. S. Sriprakash, M. Dowton, M. Ranson, and M. J. Walker. 2006. Divergence in the plasminogen-binding group A streptococcal M protein family: functional conservation of binding site and potential role for immune selection of variants. J. Biol. Chem. 281:3217-3226.
    • (2006) J. Biol. Chem , vol.281 , pp. 3217-3226
    • Sanderson-Smith, M.1    Batzloff, M.2    Sriprakash, K.S.3    Dowton, M.4    Ranson, M.5    Walker, M.J.6
  • 27
    • 33748744172 scopus 로고    scopus 로고
    • The maintenance of high affinity plasminogen binding by group A streptococcal plasminogen-binding M-like protein is mediated by arginine and histidine residues within the a1 and a2 repeat domains
    • Sanderson-Smith, M. L., M. J. Walker, and M. Ranson. 2006. The maintenance of high affinity plasminogen binding by group A streptococcal plasminogen-binding M-like protein is mediated by arginine and histidine residues within the a1 and a2 repeat domains. J. Biol. Chem. 281:25965-25971.
    • (2006) J. Biol. Chem , vol.281 , pp. 25965-25971
    • Sanderson-Smith, M.L.1    Walker, M.J.2    Ranson, M.3
  • 28
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformational changes
    • T. E. Creighton ed, IRL Press, Oxford, United Kingdom
    • Schmid, F. X. 1989. Spectral methods of characterizing protein conformation and conformational changes, p. 251-284. In T. E. Creighton (ed.), Protein structure: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1989) Protein structure: A practical approach , pp. 251-284
    • Schmid, F.X.1
  • 29
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 21244444520 scopus 로고    scopus 로고
    • Is plasminogen deployed as a Streptococcus pyogenes virulence factor?
    • Walker, M. J., J. D. McArthur, F. McKay, and M. Ranson. 2005. Is plasminogen deployed as a Streptococcus pyogenes virulence factor? Trends Microbiol. 13:308-313.
    • (2005) Trends Microbiol , vol.13 , pp. 308-313
    • Walker, M.J.1    McArthur, J.D.2    McKay, F.3    Ranson, M.4
  • 33
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan, S., and N. Goldman. 2001. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18:691-699.
    • (2001) Mol. Biol. Evol , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 34
    • 0032544354 scopus 로고    scopus 로고
    • Kringle 2 mediates high affinity binding of plasminogen to an internal sequence in streptococcal surface protein PAM
    • Wistedt, A. C., H. Kotarsky, D. Marti, U. Ringdahl, F. J. Castellino, J. Schaller, and U. Sjobring. 1998. Kringle 2 mediates high affinity binding of plasminogen to an internal sequence in streptococcal surface protein PAM. J. Biol. Chem. 273:24420-24424.
    • (1998) J. Biol. Chem , vol.273 , pp. 24420-24424
    • Wistedt, A.C.1    Kotarsky, H.2    Marti, D.3    Ringdahl, U.4    Castellino, F.J.5    Schaller, J.6    Sjobring, U.7
  • 35
    • 0001122618 scopus 로고
    • Identification of a plasminogen-binding motif in PAM, a bacterial surface protein
    • Wistedt, A. C., U. Ringdahl, W. Muller-Esterl, and U. Sjobring. 1995. Identification of a plasminogen-binding motif in PAM, a bacterial surface protein. Mol. Microbiol. 18:569-578.
    • (1995) Mol. Microbiol , vol.18 , pp. 569-578
    • Wistedt, A.C.1    Ringdahl, U.2    Muller-Esterl, W.3    Sjobring, U.4


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