메뉴 건너뛰기




Volumn 287, Issue 30, 2012, Pages 25010-25018

Streptococcal surface proteins activate the contact system and control its antibacterial activity

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-BACTERIAL ACTIVITY; ANTIBACTERIAL EFFECTS; ANTIBACTERIAL PEPTIDES; ANTIMICROBIAL PEPTIDE; BACTERIAL PATHOGENS; CONTACT SYSTEMS; HIGH MOLECULAR WEIGHT; HUMAN PLASMAS; INNATE IMMUNITY; MUTANT STRAIN; PROINFLAMMATORY; PROTEIN G; PROTEOLYTIC CASCADE; SURFACE PROTEINS;

EID: 84864085487     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.373217     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 79951557398 scopus 로고    scopus 로고
    • Invasive infection caused by Streptococcus dysgalactiae subsp. equisimilis: Characteristics of strains and clinical features
    • Takahashi, T., Ubukata, K., and Watanabe, H. (2011) Invasive infection caused by Streptococcus dysgalactiae subsp. equisimilis: characteristics of strains and clinical features. J. Infect. Chemother. 17, 1-10
    • (2011) J. Infect. Chemother. , vol.17 , pp. 1-10
    • Takahashi, T.1    Ubukata, K.2    Watanabe, H.3
  • 2
    • 0345832035 scopus 로고    scopus 로고
    • Characterization of Group C and G Streptococcal Strains That Cause Streptococcal Toxic Shock Syndrome
    • DOI 10.1128/JCM.42.1.186-192.2004
    • Hashikawa, S., Iinuma, Y., Furushita, M., Ohkura, T., Nada, T., Torii, K., Hasegawa, T., and Ohta, M. (2004) Characterization of group C and G streptococcal strains that cause streptococcal toxic shock syndrome. J. Clin. Microbiol. 42, 186-192 (Pubitemid 38082718)
    • (2004) Journal of Clinical Microbiology , vol.42 , Issue.1 , pp. 186-192
    • Hashikawa, S.1    Iinuma, Y.2    Furushita, M.3    Ohkura, T.4    Nada, T.5    Torii, K.6    Hasegawa, T.7    Ohta, M.8
  • 3
    • 76049130113 scopus 로고    scopus 로고
    • Disease burden due to Streptococcus dysgalactiae subsp. equisimilis (group G and C streptococcus) is higher than that due to Streptococcus pyogenes among Mumbai school children
    • Bramhachari, P. V., Kaul, S. Y., McMillan, D. J., Shaila, M. S., Karmarkar, M. G., and Sriprakash, K. S. (2010) Disease burden due to Streptococcus dysgalactiae subsp. equisimilis (group G and C streptococcus) is higher than that due to Streptococcus pyogenes among Mumbai school children. J. Med. Microbiol. 59, 220-223
    • (2010) J. Med. Microbiol. , vol.59 , pp. 220-223
    • Bramhachari, P.V.1    Kaul, S.Y.2    McMillan, D.J.3    Shaila, M.S.4    Karmarkar, M.G.5    Sriprakash, K.S.6
  • 4
    • 0036605915 scopus 로고    scopus 로고
    • Bacteremia due to beta-hemolytic Streptococcus group G: Increasing incidence and clinical characteristics of patients
    • DOI 10.1016/S0002-9343(02)01117-8, PII S0002934302011178
    • Sylvetsky, N., Raveh, D., Schlesinger, Y., Rudensky, B., and Yinnon, A. M. (2002) Bacteremia due to β-hemolytic Streptococcus group G: increasing incidence and clinical characteristics of patients. Am. J. Med. 112, 622-626 (Pubitemid 34597162)
    • (2002) American Journal of Medicine , vol.112 , Issue.8 , pp. 622-626
    • Sylvetsky, N.1    Raveh, D.2    Schlesinger, Y.3    Rudensky, B.4    Yinnon, A.M.5
  • 6
    • 70149091079 scopus 로고    scopus 로고
    • Human infections due to Streptococcus dysgalactiae subspecies equisimilis
    • Brandt, C. M., and Spellerberg, B. (2009) Human infections due to Streptococcus dysgalactiae subspecies equisimilis. Clin. Infect. Dis. 49, 766-772
    • (2009) Clin. Infect. Dis. , vol.49 , pp. 766-772
    • Brandt, C.M.1    Spellerberg, B.2
  • 8
    • 0030830360 scopus 로고    scopus 로고
    • Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes
    • Colman, R. W., and Schmaier, A. H. (1997) Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood 90, 3819-3843 (Pubitemid 27484034)
    • (1997) Blood , vol.90 , Issue.10 , pp. 3819-3843
    • Colman, R.W.1    Schmaier, A.H.2
  • 9
    • 13444267658 scopus 로고    scopus 로고
    • Formation of bradykinin: A major contributor to the innate inflammatory response
    • DOI 10.1016/S0065-2776(04)86005-X
    • Joseph, K., and Kaplan, A. P. (2005) Formation of bradykinin: a major contributor to the innate inflammatory response. Adv. Immunol. 86, 159-208 (Pubitemid 40215693)
    • (2005) Advances in Immunology , vol.86 , pp. 159-208
    • Joseph, K.1    Kaplan, A.P.2
  • 10
    • 34548665723 scopus 로고    scopus 로고
    • The dual role of the contact system in bacterial infectious disease
    • DOI 10.1160/TH07-01-0051
    • Frick, I. M., Björck, L., and Herwald, H. (2007) The dual role of the contact system in bacterial infectious disease. Thromb. Haemost. 98, 497-502 (Pubitemid 47412875)
    • (2007) Thrombosis and Haemostasis , vol.98 , Issue.3 , pp. 497-502
    • Frick, I.-M.1    Bjorck, L.2    Herwald, H.3
  • 11
    • 0037318946 scopus 로고    scopus 로고
    • Bench-to-bedside review: Functional relationships between coagulation and the innate immune response and their respective roles in the pathogenesis of sepsis
    • DOI 10.1186/cc1854
    • Opal, S. M., and Esmon, C. T. (2003) Bench-to-bedside review: functional relationships between coagulation and the innate immune response and their respective roles in the pathogenesis of sepsis. Crit. Care 7, 23-38 (Pubitemid 36204267)
    • (2003) Critical Care , vol.7 , Issue.1 , pp. 23-38
    • Opal, S.M.1    Esmon, C.T.2
  • 12
    • 77957592168 scopus 로고    scopus 로고
    • Activation of the plasma kallikrein-kinin system on human lung epithelial cells
    • Vergiliana, J. F., Asokananthan, N., and Stewart, G. A. (2010) Activation of the plasma kallikrein-kinin system on human lung epithelial cells. Biol. Chem. 391, 1067-1077
    • (2010) Biol. Chem. , vol.391 , pp. 1067-1077
    • Vergiliana, J.F.1    Asokananthan, N.2    Stewart, G.A.3
  • 13
    • 34447519008 scopus 로고    scopus 로고
    • Fifty years or research on the plasma kallikrein-kinin system: From protein structure and function to cell biology and in-vivo pathophysiology
    • DOI 10.1160/TH07-04-0250
    • Sainz, I. M., Pixley, R. A., and Colman, R. W. (2007) Fifty years of research on the plasma kallikrein-kinin system: from protein structure and function to cell biology and in vivo pathophysiology. Thromb. Haemost. 98, 77-83 (Pubitemid 47074181)
    • (2007) Thrombosis and Haemostasis , vol.98 , Issue.1 , pp. 77-83
    • Saints, I.M.1    Pixley, R.A.2    Colman, R.W.3
  • 14
    • 77951205291 scopus 로고    scopus 로고
    • Contact system activation in severe infectious diseases
    • Oehmcke, S., and Herwald, H. (2010) Contact system activation in severe infectious diseases. J. Mol. Med. 88, 121-126
    • (2010) J. Mol. Med. , vol.88 , pp. 121-126
    • Oehmcke, S.1    Herwald, H.2
  • 15
    • 34250860681 scopus 로고    scopus 로고
    • Understanding how leading bacterial pathogens subvert innate immunity to reveal novel therapeutic targets
    • Nizet, V. (2007) Understanding how leading bacterial pathogens subvert innate immunity to reveal novel therapeutic targets. J. Allergy Clin. Immunol. 120, 13-22
    • (2007) J. Allergy Clin. Immunol. , vol.120 , pp. 13-22
    • Nizet, V.1
  • 16
    • 79952353786 scopus 로고    scopus 로고
    • Streptococcus mitis: Walking the line between commensalism and pathogenesis
    • Mitchell, J. (2011) Streptococcus mitis: walking the line between commensalism and pathogenesis. Mol. Oral. Microbiol. 26, 89-98
    • (2011) Mol. Oral. Microbiol. , vol.26 , pp. 89-98
    • Mitchell, J.1
  • 17
    • 0030067110 scopus 로고    scopus 로고
    • Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function
    • Åkesson, P., Sjöholm, A. G., and Björck, L. (1996) Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function. J. Biol. Chem. 271, 1081-1088
    • (1996) J. Biol. Chem. , vol.271 , pp. 1081-1088
    • Åkesson, P.1    Sjöholm, A.G.2    Björck, L.3
  • 18
    • 78651407006 scopus 로고    scopus 로고
    • Antibacterial activity of the contact and complement systems is blocked by SIC, a protein secreted by Streptococcus pyogenes
    • Frick, I. M., Shannon, O., Åkesson, P., Mörgelin, M., Collin, M., Schmidtchen, A., and Björck, L. (2011) Antibacterial activity of the contact and complement systems is blocked by SIC, a protein secreted by Streptococcus pyogenes. J. Biol. Chem. 286, 1331-1340
    • (2011) J. Biol. Chem. , vol.286 , pp. 1331-1340
    • Frick, I.M.1    Shannon, O.2    Åkesson, P.3    Mörgelin, M.4    Collin, M.5    Schmidtchen, A.6    Björck, L.7
  • 20
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A novel virulence mechanism
    • Herwald, H., Collin, M., Müller-Esterl, W., and Björck, L. (1996) Streptococcal cysteine proteinase releases kinins: a virulence mechanism. J. Exp. Med. 184, 665-673 (Pubitemid 26324120)
    • (1996) Journal of Experimental Medicine , vol.184 , Issue.2 , pp. 665-673
    • Herwald, H.1    Collin, M.2    Muller-Esterl, W.3    Bjorck, L.4
  • 21
    • 11044234357 scopus 로고    scopus 로고
    • Protein FOG - A streptococcal inhibitor of neutrophil function
    • DOI 10.1099/mic.0.27269-0
    • Johansson, H. M., Mörgelin, M., and Frick, I. M. (2004) Protein FOG-a streptococcal inhibitor of neutrophil function. Microbiology 150, 4211-4221 (Pubitemid 40045349)
    • (2004) Microbiology , vol.150 , Issue.12 , pp. 4211-4221
    • Johansson, H.M.1    Morgelin, M.2    Frick, I.-M.3
  • 22
    • 0021276488 scopus 로고
    • Purification and some properties of streptococcal protein G, a novel IgG-binding reagent
    • Björck, L., and Kronvall, G. (1984) Purification and some properties of streptococcal protein G, a novel IgG-binding reagent. J. Immunol. 133, 969-974 (Pubitemid 14093496)
    • (1984) Journal of Immunology , vol.133 , Issue.2 , pp. 969-974
    • Bjorck, L.1    Kronvall, G.2
  • 23
    • 0021259051 scopus 로고
    • Streptococcal Fc receptors. I. Isolation and partial characterization of the receptor from a group C streptococcus
    • Reis, K. J., Ayoub, E. M., and Boyle, M. D. (1984) Streptococcal Fc receptors. I. Isolation and partial characterization of the receptor from a group C streptococcus. J. Immunol. 132, 3091-3097 (Pubitemid 14104275)
    • (1984) Journal of Immunology , vol.132 , Issue.6 , pp. 3091-3097
    • Reis, K.J.1    Ayoub, E.M.2    Boyle, M.D.P.3
  • 24
  • 26
  • 27
    • 0026479070 scopus 로고
    • A nonradioactive biochemical characterization of membrane proteins using enhanced chemiluminescence
    • Nesbitt, S. A., and Horton, M. A. (1992) A nonradioactive biochemical characterization of membrane proteins using enhanced chemiluminescence. Anal. Biochem. 206, 267-272
    • (1992) Anal. Biochem. , vol.206 , pp. 267-272
    • Nesbitt, S.A.1    Horton, M.A.2
  • 28
    • 79959993374 scopus 로고    scopus 로고
    • Interaction of Bacteroides fragilis and Bacteroides thetaiotaomicron with the kallikrein-kinin system
    • Murphy, E. C., Mörgelin, M., Cooney, J. C., and Frick, I. M. (2011) Interaction of Bacteroides fragilis and Bacteroides thetaiotaomicron with the kallikrein-kinin system. Microbiology 157, 2094-2105
    • (2011) Microbiology , vol.157 , pp. 2094-2105
    • Murphy, E.C.1    Mörgelin, M.2    Cooney, J.C.3    Frick, I.M.4
  • 29
    • 77953459012 scopus 로고    scopus 로고
    • Collagen VI is a subepithelial adhesive target for human respiratory tract pathogens
    • Bober, M., Enochsson, C., Collin, M., and Mörgelin, M. (2010) Collagen VI is a subepithelial adhesive target for human respiratory tract pathogens. J. Innate Immun. 2, 160-166
    • (2010) J. Innate Immun. , vol.2 , pp. 160-166
    • Bober, M.1    Enochsson, C.2    Collin, M.3    Mörgelin, M.4
  • 30
    • 0023259024 scopus 로고
    • Streptococcal protein G, expressed by streptococci or by Escherichia coli, has separate binding sites for human albumin and IgG
    • Björck, L., Kastern, W., Lindahl, G., and Widebäck, K. (1987) Streptococcal protein G, expressed by streptococci or by Escherichia coli, has separate binding sites for human albumin and IgG. Mol. Immunol. 24, 1113-1122
    • (1987) Mol. Immunol. , vol.24 , pp. 1113-1122
    • Björck, L.1    Kastern, W.2    Lindahl, G.3    Widebäck, K.4
  • 31
    • 0017700478 scopus 로고
    • Association of factor XI and high molecular weight kininogen in human plasma
    • Thompson, R. E., Mandle, R., Jr., and Kaplan, A. P. (1977) Association of factor XI and high molecular weight kininogen in human plasma. J. Clin. Invest. 60, 1376-1380 (Pubitemid 8238653)
    • (1977) Journal of Clinical Investigation , vol.60 , Issue.6 , pp. 1376-1380
    • Thompson, R.E.1    Mandle Jr., R.2    Kaplan, A.P.3
  • 32
    • 0017149563 scopus 로고
    • Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma
    • Mandle, R. J., Colman, R. W., and Kaplan, A. P. (1976) Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma. Proc. Natl. Acad. Sci. U.S.A. 73, 4179-4183
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 4179-4183
    • Mandle, R.J.1    Colman, R.W.2    Kaplan, A.P.3
  • 33
    • 79961125621 scopus 로고    scopus 로고
    • Activation of the contact system at the surface of Fusobacterium necrophorum represents a possible virulence mechanism in Lemièrre syndrome
    • Holm, K., Frick, I. M., Björck, L., and Rasmussen, M. (2011) Activation of the contact system at the surface of Fusobacterium necrophorum represents a possible virulence mechanism in Lemièrre syndrome. Infect. Immun. 79, 3284-3290
    • (2011) Infect. Immun. , vol.79 , pp. 3284-3290
    • Holm, K.1    Frick, I.M.2    Björck, L.3    Rasmussen, M.4
  • 34
    • 0020529790 scopus 로고
    • Mechanisms of activation of the classical pathway of complement by Hageman factor fragment
    • Ghebrehiwet, B., Randazzo, B. P., Dunn, J. T., Silverberg, M., and Kaplan, A. P. (1983) Mechanisms of activation of the classical pathway of complement by Hageman factor fragment. J. Clin. Invest. 71, 1450-1456 (Pubitemid 13098935)
    • (1983) Journal of Clinical Investigation , vol.71 , Issue.5 , pp. 1450-1456
    • Ghebrehiwet, B.1    Randazzo, B.P.2    Dunn, J.T.3
  • 36
    • 36448955371 scopus 로고    scopus 로고
    • Protein FOG is a moderate inducer of MIG/CXCL9, and group G streptococci are more tolerant than group A streptococci to this chemokine's antibacterial effect
    • DOI 10.1099/mic.0.2007/009647-0
    • Linge, H. M., Sastalla, I., Nitsche-Schmitz, D. P., Egesten, A., and Frick, I. M. (2007) Protein FOG is a moderate inducer of MIG/CXCL9, and group G streptococci are more tolerant than group A streptococci to this chemokine's antibacterial effect. Microbiology 153, 3800-3808 (Pubitemid 350168259)
    • (2007) Microbiology , vol.153 , Issue.11 , pp. 3800-3808
    • Linge, H.M.1    Sastalla, I.2    Nitsche-Schmitz, D.P.3    Egesten, A.4    Frick, I.-M.5
  • 39
    • 27144468026 scopus 로고    scopus 로고
    • The global burden of group A streptococcal diseases
    • DOI 10.1016/S1473-3099(05)70267-X, PII S147330990570267X
    • Carapetis, J. R., Steer, A. C., Mulholland, E. K., and Weber, M. (2005) The global burden of group A streptococcal diseases. Lancet Infect. Dis. 5, 685-694 (Pubitemid 41505357)
    • (2005) Lancet Infectious Diseases , vol.5 , Issue.11 , pp. 685-694
    • Carapetis, J.R.1    Steer, A.C.2    Mulholland, E.K.3    Weber, M.4
  • 40
    • 0019917301 scopus 로고
    • Studies of components of the coagulation systems in normal individuals and septic shock patients
    • Smith-Erichsen, N., Aasen, A. O., Gallimore, M. J., and Amundsen, E. (1982) Studies of components of the coagulation systems in normal individuals and septic shock patients. Circ. Shock 9, 491-497 (Pubitemid 12001327)
    • (1982) Circulatory Shock , vol.9 , Issue.5 , pp. 491-497
    • Smith-Erichsen, N.1    Assen, A.O.2    Gallimore, M.J.3    Amundsen, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.