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Volumn 4, Issue 2, 2012, Pages 132-140

Streptococcal ideS and its impact on immune response and inflammation

Author keywords

Cysteine protease; Immunoglobulin G; Neutrophil priming; Streptococcus pyogenes

Indexed keywords

BACTERIAL PROTEIN; CD11B ANTIGEN; CYSTATIN C; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; PROTEIN MAC 2; PROTEINASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UNCLASSIFIED DRUG;

EID: 84857782323     PISSN: 1662811X     EISSN: 16628128     Source Type: Journal    
DOI: 10.1159/000332940     Document Type: Review
Times cited : (35)

References (59)
  • 1
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group a streptococcal infections
    • DOI 10.1128/CMR.13.3.470-511.2000
    • Cunningham MW: Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 2000; 13: 470-511. (Pubitemid 30452618)
    • (2000) Clinical Microbiology Reviews , vol.13 , Issue.3 , pp. 470-511
    • Cunningham, M.W.1
  • 2
    • 27144468026 scopus 로고    scopus 로고
    • The global burden of group A streptococcal diseases
    • DOI 10.1016/S1473-3099(05)70267-X, PII S147330990570267X
    • Carapetis JR, Steer AC, Mulholl EK, Weber M: The global burden of group A streptococcal diseases. Lancet Infect Dis 2005; 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
  • 3
    • 0026501836 scopus 로고
    • The role of streptococcal infection in the initiation of guttate psoriasis
    • Telfer NR, Chalmers RJ, Whale K, Coleman G: The role of streptococcal infection in the initiation of guttate psoriasis. Arch Dermatol 1992; 128: 39-42.
    • (1992) Arch Dermatol , vol.128 , pp. 39-42
    • Telfer, N.R.1    Chalmers, R.J.2    Whale, K.3    Coleman, G.4
  • 4
    • 0036271592 scopus 로고    scopus 로고
    • Proteolysis and its regulation at the surface of Streptococcus pyogenes
    • DOI 10.1046/j.1365-2958.2002.02766.x
    • Rasmussen M, Björck L: Proteolysis and its regulation at the surface of Streptococcus pyogenes. Mol Microbiol 2002; 43: 537-544. (Pubitemid 34597251)
    • (2002) Molecular Microbiology , vol.43 , Issue.3 , pp. 537-544
    • Rasmussen, M.1    Bjorck, L.2
  • 5
    • 1542618118 scopus 로고    scopus 로고
    • Induction of protective IgA by intestinal dendritic cells carrying commensal bacteria
    • DOI 10.1126/science.1091334
    • Macpherson AJ, Uhr T: Induction of protective IgA by intestinal dendritic cells carrying commensal bacteria. Science 2004; 303: 1662-1665. (Pubitemid 38338323)
    • (2004) Science , vol.303 , Issue.5664 , pp. 1662-1665
    • Macpherson, A.J.1    Uhr, T.2
  • 8
    • 0030995890 scopus 로고    scopus 로고
    • The lysosomal/phagosomal membrane protein h-lamp-1 is a target of the IgA1 protease of Neisseria gonorrhoeae
    • DOI 10.1016/S0014-5793(97)00163-4, PII S0014579397001634
    • Hauck CR, Meyer TF: The lysosomal/phagosomal membrane protein h-LAMP-1 is a target of the IgA1 protease of Neisseria gonorrhoeae FEBS Letters 1997; 405: 86-90. (Pubitemid 27130378)
    • (1997) FEBS Letters , vol.405 , Issue.1 , pp. 86-90
    • Hauck, C.R.1    Meyer, T.F.2
  • 9
    • 0035896552 scopus 로고    scopus 로고
    • Streptococcal IgA-binding proteins bind in the C 2-C 3 interdomain region and inhibit binding of IgA to human CD89
    • Pleass RJ, Areschoug T, Lindahl G, Woof JM: Streptococcal IgA-binding proteins bind in the C 2-C 3 interdomain region and inhibit binding of IgA to human CD89. J Biol Chem 2001; 276: 8197-8204.
    • (2001) J Biol Chem , vol.276 , pp. 8197-8204
    • Pleass, R.J.1    Areschoug, T.2    Lindahl, G.3    Woof, J.M.4
  • 11
    • 77953677176 scopus 로고    scopus 로고
    • Cleavage of IgGs by proteases associated with invasive diseases: An evasion tactic against host immunity?
    • Brezski RJ, Jordan RE: Cleavage of IgGs by proteases associated with invasive diseases: An evasion tactic against host immunity? MAbs 2010; 2: 212-220.
    • (2010) MAbs , vol.2 , pp. 212-220
    • Brezski, R.J.1    Jordan, R.E.2
  • 12
    • 0001322321 scopus 로고
    • A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen
    • Elliott SD: A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen. J Exp Med 1945; 81: 573-592.
    • (1945) J Exp Med , vol.81 , pp. 573-592
    • Elliott, S.D.1
  • 13
    • 0035875889 scopus 로고    scopus 로고
    • EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
    • DOI 10.1093/emboj/20.12.3046
    • Collin M, Olsén A: EndoS, novel secreted enzyme from Streptococcus pyogenes with endoglycosidase activity on human IgG. EMBO J 2001; 20: 3046-3055. (Pubitemid 32611992)
    • (2001) EMBO Journal , vol.20 , Issue.12 , pp. 3046-3055
    • Collin, M.1    Olsen, A.2
  • 14
    • 0037223045 scopus 로고    scopus 로고
    • Cleavage of antigen-bound immunoglobulin G by SpeB contributes to streptococcal persistence in opsonizing blood
    • DOI 10.1128/IAI.71.1.211-217.2003
    • Eriksson A, Norgren M: Cleavage of antigenbound immunoglobulin G by SpeB contributes to streptococcal persistence in opsonizing blood. Infect Immun 2003; 71: 211-217. (Pubitemid 36026022)
    • (2003) Infection and Immunity , vol.71 , Issue.1 , pp. 211-217
    • Eriksson, A.1    Norgren, M.2
  • 15
    • 0037330259 scopus 로고    scopus 로고
    • IdeS and SpeB: Immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes
    • DOI 10.1016/S1369-5274(03)00003-1
    • von Pawel-Rammingen U, Björck L: IdeS and SpeB: Immunoglobulin- degrading cysteine proteases of Streptococcus pyogenes Curr Opin Microbiol 2003; 6: 50-55. (Pubitemid 36258536)
    • (2003) Current Opinion in Microbiology , vol.6 , Issue.1 , pp. 50-55
    • Von Pawel-Rammingen, U.1    Bjorck, L.2
  • 16
    • 0037007214 scopus 로고    scopus 로고
    • IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
    • DOI 10.1093/emboj/21.7.1607
    • von Pawel-Rammingen U, Johansson BP, Björck L: IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. EMBO J 2002; 21: 1607-1615. (Pubitemid 34614617)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1607-1615
    • Von Pawel-Rammingen, U.1    Johansson, B.P.2    Bjorck, L.3
  • 17
    • 0034442652 scopus 로고    scopus 로고
    • Identification and immunogenicity of group A Streptococcus culture supernatant proteins
    • DOI 10.1128/IAI.68.12.6807-6818.2000
    • Lei B, Mackie S, Lukomski S, Musser JM: Identification and immunogenicity of group A streptococcus culture supernatant proteins. Infect Immun 2000; 68: 6807-6818. (Pubitemid 32463388)
    • (2000) Infection and Immunity , vol.68 , Issue.12 , pp. 6807-6818
    • Lei, B.1    Mackie, S.2    Lukomski, S.3    Musser, J.M.4
  • 19
    • 42949106144 scopus 로고    scopus 로고
    • The intrinsic immunoglobulin G endopeptidase activity of streptococcal Mac-2 proteins implies a unique role for the enzymatically impaired Mac-2 protein of M28 serotype strains
    • DOI 10.1128/IAI.01422-07
    • Johansson Söderberg J, Engström P, von Pawel-Rammingen U: The intrinsic IgG endopeptidase activity of streptococcal Mac-2 proteins implies a unique role for the enzymatically impaired Mac-2 protein of M28 serotype strains. Infect Immun 2008; 76: 2183-2188. (Pubitemid 351656154)
    • (2008) Infection and Immunity , vol.76 , Issue.5 , pp. 2183-2188
    • Soderberg, J.J.1    Engstrom, P.2    Von Pawel-Rammingen, U.3
  • 21
    • 29644438454 scopus 로고    scopus 로고
    • IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection
    • DOI 10.1128/IAI.74.1.497-503.2006
    • Akesson P, Moritz L, Truedsson M, Christensson B, von Pawel-Rammingen U: IdeS, a highly specific IgG-cleaving enzyme from Streptococcus pyogenes , is inhibited by specific IgG antibodies generated during infection. Infect Immun 2006; 74: 497-503. (Pubitemid 43023105)
    • (2006) Infection and Immunity , vol.74 , Issue.1 , pp. 497-503
    • Akesson, P.1    Moritz, L.2    Truedsson, M.3    Christensson, B.4    Von Pawel-Rammingen, U.5
  • 23
    • 33747696575 scopus 로고    scopus 로고
    • IdeE, an IgG endopeptidase of Streptococcus equi ssp equi
    • Lannergard J, Guss B: IdeE, an IgG endopeptidase of Streptococcus equi ssp equi FEMS Microbiol Lett 2006; 262: 230-235.
    • (2006) FEMS Microbiol Lett , vol.262 , pp. 230-235
    • Lannergard, J.1    Guss, B.2
  • 26
    • 77957574501 scopus 로고    scopus 로고
    • Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola
    • Ishihara K, Wawrzonek K, Shaw LN, Inagaki S, Miyamoto M, Potempa J: Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola Biol Chem 2010; 391: 1047-1055.
    • (2010) Biol Chem , vol.391 , pp. 1047-1055
    • Ishihara, K.1    Wawrzonek, K.2    Shaw, L.N.3    Inagaki, S.4    Miyamoto, M.5    Potempa, J.6
  • 27
    • 0036010538 scopus 로고    scopus 로고
    • Recognition of immunoglobulins by Fc gamma receptors
    • Radaev S, Sun P: Recognition of immunoglobulins by Fc gamma receptors. Mol Immunol 2002; 38: 1073-1083.
    • (2002) Mol Immunol , vol.38 , pp. 1073-1083
    • Radaev, S.1    Sun, P.2
  • 28
    • 0023897194 scopus 로고
    • The binding site for C1q on IgG
    • Duncan AR, Winter G: The binding site for C1q on IgG. Nature 1988; 332: 738-740.
    • (1988) Nature , vol.332 , pp. 738-740
    • Duncan, A.R.1    Winter, G.2
  • 29
    • 10644276295 scopus 로고    scopus 로고
    • Biochemical characterization of IdeS, an IgG-specific endopeptidase from Streptococcus pyogenes
    • Vincents B, von Pawel-Rammingen U, Björck L, Abrahamson M: Biochemical characterization of IdeS, an IgG-specific endopeptidase from Streptococcus pyogenes Biochemistry 2004; 43: 15540-15549.
    • (2004) Biochemistry , vol.43 , pp. 15540-15549
    • Vincents, B.1    Von Pawel-Rammingen, U.2    Björck, L.3    Abrahamson, M.4
  • 30
    • 39149138479 scopus 로고    scopus 로고
    • Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid
    • Ryan MH, Petrone D, Nemeth JF, Barnathan E, Björck L, Jordan RE: Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid. Mol Immunol 2008; 45: 1837-1846.
    • (2008) Mol Immunol , vol.45 , pp. 1837-1846
    • Ryan, M.H.1    Petrone, D.2    Nemeth, J.F.3    Barnathan, E.4    Björck, L.5    Jordan, R.E.6
  • 32
    • 51649097889 scopus 로고    scopus 로고
    • Acceleration of cysteine protease activity by the human protease inhibitor cystatin C
    • Vincents B, Vindebro R, Abrahamsson M, von Pawel-Rammingen U: Acceleration of cysteine protease activity by the human protease inhibitor cystatin C. Chem Biol 2008; 15: 960-968.
    • (2008) Chem Biol , vol.15 , pp. 960-968
    • Vincents, B.1    Vindebro, R.2    Abrahamsson, M.3    Von Pawel-Rammingen, U.4
  • 33
    • 32044433064 scopus 로고    scopus 로고
    • Crystal structure of group A Streptococcus Mac-1: Insight into dimer-mediated specificity for recognition of human IgG
    • DOI 10.1016/j.str.2005.10.012, PII S0969212606000487
    • Agniswamy J, Nagiec MJ, Liu M, Schuck P, Musser JM, Sun PD: Crystal structure of group A streptococcus Mac-1: Insight into dimer-mediated specificity for recognition of human IgG. Structure 2006; 14: 225-235. (Pubitemid 43202012)
    • (2006) Structure , vol.14 , Issue.2 , pp. 225-235
    • Agniswamy, J.1    Nagiec, M.J.2    Liu, M.3    Schuck, P.4    Musser, J.M.5    Sun, P.D.6
  • 34
    • 70349783818 scopus 로고    scopus 로고
    • Structure of the mature streptococcal cysteine protease exotoxin mSpeB in its active dimeric form
    • Olsen JG, Dagil R, Niclasen LM, Sørensen OE, Kragelund BB: Structure of the mature streptococcal cysteine protease exotoxin mSpeB in its active dimeric form. J Mol Biol 2009; 393: 693-703.
    • (2009) J Mol Biol , vol.393 , pp. 693-703
    • Olsen, J.G.1    Dagil, R.2    Niclasen, L.M.3    Sørensen, O.E.4    Kragelund, B.B.5
  • 36
    • 0037406711 scopus 로고    scopus 로고
    • Histidine and aspartic acid residues important for immunoglobulin G endopeptidase activity of the group A Streptococcus opsonophagocytosis- inhibiting Mac protein
    • DOI 10.1128/IAI.71.5.2881-2884.2003
    • Lei B, Liu M, Meyers EG, Manning HM, Nagiec MJ, Musser JM: Histidine and aspartic acid residues important for immunoglobulin G endopeptidase activity of the group A streptococcus opsonophagocytosis-inhibiting Mac protein. Infect Immun 2003; 5: 2881-2884. (Pubitemid 36519902)
    • (2003) Infection and Immunity , vol.71 , Issue.5 , pp. 2881-2884
    • Lei, B.1    Liu, M.2    Meyers, E.G.3    Manning, H.M.4    Nagiec, M.J.5    Musser, J.M.6
  • 38
    • 0035986219 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators
    • DOI 10.2174/1381612023394124
    • Turk B, Turk D, Salvesen GS: Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators. Curr Pharm Des 2002; 8: 1623-1637. (Pubitemid 34752830)
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.18 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 39
    • 31444456321 scopus 로고    scopus 로고
    • Parasite cysteine proteinase interactions with α2-macroglobulin or kininogens: Differential pathways modulating inflammation and innate immunity in infection by pathogenic trypanosomatids
    • DOI 10.1016/j.imbio.2005.10.014, PII S0171298505001762
    • Scharfstein J: Parasite cysteine protease interactions with alpha2-macroglobulin or kininogens: Differential pathways modulating inflammation and innate immunity in infection by pathogenic trypanosomatids. Immunobiology 2006; 211: 117-125. (Pubitemid 43150113)
    • (2006) Immunobiology , vol.211 , Issue.1-2 , pp. 117-125
    • Scharfstein, J.1
  • 40
    • 0025177313 scopus 로고
    • Cystatin C, a human proteinase inhibitor, blocks replication of herpes simplex virus
    • Björck L, Grubb A, Kjellén L: Cystatin C, a human protease inhibitor, blocks replication of Herpes simplex virus. J Virol 1990; 64: 941-943. (Pubitemid 20032717)
    • (1990) Journal of Virology , vol.64 , Issue.2 , pp. 941-943
    • Bjorck, L.1    Grubb, A.2    Kjellen, L.3
  • 42
    • 0035896552 scopus 로고    scopus 로고
    • Streptococcal IgA-binding proteins bind in the Calpha 2-Calpha 3 interdomain region and inhibit binding of IgA to human CD89
    • Pleass RJ, Areschoug T, Lindahl G, Woof JM: Streptococcal IgA-binding proteins bind in the Calpha 2-Calpha 3 interdomain region and inhibit binding of IgA to human CD89. J Biol Chem 2001; 276: 8197-8204.
    • (2001) J Biol Chem , vol.276 , pp. 8197-8204
    • Pleass, R.J.1    Areschoug, T.2    Lindahl, G.3    Woof, J.M.4
  • 43
    • 0030878839 scopus 로고    scopus 로고
    • Streptococcal protein H forms soluble complement-activating complexes with IgG, but inhibits complement activation by IgG-coated targets
    • DOI 10.1074/jbc.272.33.20774
    • Berge A, Kihlberg BM, Sjöholm AG, Björck L: Streptococcal protein H forms soluble complement-activating complexes with IgG, but inhibits complement activation by IgGcoated targets. J Biol Chem 1997; 272: 20774-20781. (Pubitemid 27355644)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20774-20781
    • Berge, A.1    Kihlberg, B.-M.2    Sjoholm, A.G.3    Bjorck, L.4
  • 44
    • 44749094643 scopus 로고    scopus 로고
    • The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytes
    • Johansson Söderberg J, von Pawel-Rammingen U: The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytes. Mol Immunol 2008; 45: 3347-3353.
    • (2008) Mol Immunol , vol.45 , pp. 3347-3353
    • Johansson Söderberg, J.1    Von Pawel-Rammingen, U.2
  • 45
    • 0021360476 scopus 로고
    • The NADPH oxidase of human polymorphonuclear leukocytes. Evidence for regulation by multiple signals
    • McPhail LC, Clayton CC, Snyderman R: The NADPH oxidase of human polymorphonuclear leukocytes: Evidence for regulation by multiple signals. J Biol Chem 1984; 259: 5768-5775. (Pubitemid 14145044)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.9 , pp. 5768-5775
    • McPhail, L.C.1    Clayton, C.C.2    Snyderman, R.3
  • 46
    • 27644514297 scopus 로고    scopus 로고
    • Structural organization of the neutrophil NADPH oxidase: Phosphorylation and translocation during priming and activation
    • DOI 10.1189/jlb.0804442
    • Sheppard FR, Kelher MR, Moore EE, McLaughlin NJ, Banerjee A, Silliman CC: Structural organization of the neutro -phil NADPH oxidase: Phosphorylation and translocation during priming and activation. J Leukoc Biol 2005; 78: 1025-1042. (Pubitemid 41572466)
    • (2005) Journal of Leukocyte Biology , vol.78 , Issue.5 , pp. 1025-1042
    • Sheppard, F.R.1    Kelher, M.R.2    Moore, E.E.3    McLaughlin, N.J.D.4    Banerjee, A.5    Silliman, C.C.6
  • 47
    • 0036200993 scopus 로고    scopus 로고
    • Neutrophil priming in host defense: Role of oxidants as priming agents
    • Swain SD, Rohn TT, Quinn MT: Neutrophil priming in host defense: Role of oxidants as priming agents. Antioxid Redox Signal 2002; 4: 69-83. (Pubitemid 34260688)
    • (2002) Antioxidants and Redox Signaling , vol.4 , Issue.1 , pp. 69-83
    • Swain, S.D.1    Rohn, T.T.2    Quinn, M.T.3
  • 48
    • 24144501079 scopus 로고    scopus 로고
    • Systemic immunization with streptococcal immunoglobulin-binding protein Sib35 induces protective immunity against group a Streptococcus challenge in mice
    • DOI 10.1016/j.vaccine.2005.02.035, PII S0264410X05005293
    • Okamoto S, Tamura Y, Terao Y, Hamada S, Kawabata S: Systemic immunization with streptococcal immunoglobulin-binding protein Sib35 induces protective immunity against group A streptococcus challenge in mice. Vaccine 2005; 23: 4852-4859. (Pubitemid 41242879)
    • (2005) Vaccine , vol.23 , Issue.40 , pp. 4852-4859
    • Okamoto, S.1    Tamura, Y.2    Terao, Y.3    Hamada, S.4    Kawabata, S.5
  • 49
    • 0028021477 scopus 로고
    • Relation between low capacity of human sera to inhibit streptococcal mitogens and serious manifestation of disease
    • Norrby-Teglund A, Pauksens K, Holm SE, Norgren M: Relation between low capacity of human serum to inhibit streptococcal mitogens and serious manifestation of disease. J Infect Dis 1994; 170: 585-591. (Pubitemid 24262259)
    • (1994) Journal of Infectious Diseases , vol.170 , Issue.3 , pp. 585-591
    • Norrby-Teglund, A.1    Pauksens, K.2    Holm, S.E.3    Norgren, M.4
  • 50
    • 0029846421 scopus 로고    scopus 로고
    • Evidence for the presence of streptococcal-superantigen-neutralizing antibodies in normal polyspecific immunoglobulin G
    • Norrby-Teglund A, Kaul R, Low DE, McGeer A, Andersson J, Andersson U, Kotb M: Evidence for the presence of streptococcal-superantigen-neutralizing antibodies in normal polyspecific immunoglobulin G. Infect Immun 1996; 64: 5395-5398. (Pubitemid 26404008)
    • (1996) Infection and Immunity , vol.64 , Issue.12 , pp. 5395-5398
    • Norrby-Teglund, A.1    Kaul, R.2    Low, D.E.3    McGeer, A.4    Andersson, J.5    Andersson, U.6    Kotb, M.7
  • 51
    • 10644284599 scopus 로고    scopus 로고
    • Insight of host immune evasion mediated by two variants of group A Streptococcus Mac protein
    • DOI 10.1074/jbc.M410698200
    • Agniswamy J, Lei B, Musser JM, Sun PD: Insight of host immune evasion mediated by two variants of group A streptococcus Mac protein. J Biol Chem 2004; 279: 52789-52796. (Pubitemid 39656655)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52789-52796
    • Agniswamy, J.1    Lei, B.2    Musser, J.M.3    Sun, P.D.4
  • 53
    • 40349087551 scopus 로고    scopus 로고
    • Streptococcal immunoglobulin-binding protein Sib35 exerts stimulatory and mitogenic effects toward mouse B lymphocytes
    • DOI 10.1111/j.1574-6968.2008.01078.x
    • Okamoto S, Terao Y, Tamura Y, Hamada S, Kawabata S: Streptococcal immunoglobulin-binding protein Sib35 exerts stimulatory and mitogenic effects towards mouse B lymphocytes. FEMS Microbiol Lett 2008; 281: 73-80. (Pubitemid 351342051)
    • (2008) FEMS Microbiology Letters , vol.281 , Issue.1 , pp. 73-80
    • Okamoto, S.1    Terao, Y.2    Tamura, Y.3    Hamada, S.4    Kawabata, S.5
  • 54
    • 34547559233 scopus 로고    scopus 로고
    • Immunoglobulin cleavage by the streptococcal cysteine protease IdeS can be detected using protein G capture and mass spectrometry
    • DOI 10.1016/j.mimet.2007.04.017, PII S0167701207001686
    • Hess JL, Porsch EA, Shertz CA, Boyle MD: Immunoglobulin cleavage by the streptococcal cysteine protease IdeS can be detected using protein G capture and mass spectrometry. J Microbiol Meth 2007; 70: 284-291. (Pubitemid 47198134)
    • (2007) Journal of Microbiological Methods , vol.70 , Issue.2 , pp. 284-291
    • Hess, J.L.1    Porsch, E.A.2    Shertz, C.A.3    Boyle, M.D.P.4
  • 55
    • 65349158258 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of reversible inhibitors of IdeS, a bacterial cysteine protease and virulence determinant
    • Berggren K, Johansson B, Fex T, Kihlberg J, Björck L, Luthman K: Synthesis and biological evaluation of reversible inhibitors of IdeS, a bacterial cysteine protease and virulence determinant. Bioorg Med Chem 2009; 17: 3463-3470.
    • (2009) Bioorg Med Chem , vol.17 , pp. 3463-3470
    • Berggren, K.1    Johansson, B.2    Fex, T.3    Kihlberg, J.4    Björck, L.5    Luthman, K.6
  • 57
    • 44449121775 scopus 로고    scopus 로고
    • IdeS: A bacterial proteolytic enzyme with therapeutic potential
    • Johansson BP, Shannon O, Björck L: IdeS: A bacterial proteolytic enzyme with therapeutic potential. PLoS One 2008; 3:e1692.
    • (2008) PLoS One , vol.3
    • Johansson, B.P.1    Shannon, O.2    Björck, L.3
  • 58
    • 35348848012 scopus 로고    scopus 로고
    • Blocking of experimental arthritis by cleavage of IgG antibodies in vivo
    • DOI 10.1002/art.22930
    • Nandakumar KS, Johansson BP, Björck L, Holmdahl R: Blocking of experimental arthritis by cleavage of IgG antibodies in vivo. Arthritis Rheum 2007; 56: 3253-3260. (Pubitemid 47585420)
    • (2007) Arthritis and Rheumatism , vol.56 , Issue.10 , pp. 3253-3260
    • Nandakumar, K.S.1    Johansson, B.P.2    Bjorck, L.3    Holmdahl, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.