메뉴 건너뛰기




Volumn 195, Issue 5, 2007, Pages 684-693

The CXC chemokine MIG/CXCL9 is important in innate immunity against Streptococcus pyogenes

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CHEMOKINE; BACTERIAL PROTEIN; CXCL11 CHEMOKINE; CXCL9 CHEMOKINE; GAMMA INTERFERON INDUCIBLE PROTEIN 10;

EID: 33847009078     PISSN: 00221899     EISSN: None     Source Type: Journal    
DOI: 10.1086/510857     Document Type: Article
Times cited : (84)

References (35)
  • 1
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham MW. Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 2000; 13:470-511.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 2
    • 0029859871 scopus 로고    scopus 로고
    • Type 1 and type 2 cytokine dysregulation in human infectious, neoplastic, and inflammatory diseases
    • Lucey DR, Clerici M, Shearer GM. Type 1 and type 2 cytokine dysregulation in human infectious, neoplastic, and inflammatory diseases. Clin Microbiol Rev 1996; 9:532-62.
    • (1996) Clin Microbiol Rev , vol.9 , pp. 532-562
    • Lucey, D.R.1    Clerici, M.2    Shearer, G.M.3
  • 3
    • 10244226689 scopus 로고    scopus 로고
    • War and peace at mucosal surfaces
    • Sansonetti PJ. War and peace at mucosal surfaces. Nat Rev Immunol 2004; 4:953-64.
    • (2004) Nat Rev Immunol , vol.4 , pp. 953-964
    • Sansonetti, P.J.1
  • 4
    • 0033559522 scopus 로고    scopus 로고
    • The T cell-specific CXC chemokines IP-10, Mig, and I-TAC are expressed by activated human bronchial epithelial cells
    • Sauty A, Dziejman M, Taha RA, et al. The T cell-specific CXC chemokines IP-10, Mig, and I-TAC are expressed by activated human bronchial epithelial cells. J Immunol 1999; 162:3549-58.
    • (1999) J Immunol , vol.162 , pp. 3549-3558
    • Sauty, A.1    Dziejman, M.2    Taha, R.A.3
  • 5
    • 0036467505 scopus 로고    scopus 로고
    • The role of chemokines in linking innate and adaptive immunity
    • Luster AD. The role of chemokines in linking innate and adaptive immunity. Curr Opin Immunol 2002; 14:129-35.
    • (2002) Curr Opin Immunol , vol.14 , pp. 129-135
    • Luster, A.D.1
  • 7
    • 0023604651 scopus 로고
    • Biochemical characterization of a gamma interferon-inducible cytokine (IP-10)
    • Luster AD, Ravetch JV. Biochemical characterization of a gamma interferon-inducible cytokine (IP-10). J Exp Med 1987; 166:1084-97.
    • (1987) J Exp Med , vol.166 , pp. 1084-1097
    • Luster, A.D.1    Ravetch, J.V.2
  • 8
    • 0032526864 scopus 로고    scopus 로고
    • Interferon-inducible T cell alpha chemoattractant (I-TAC): A novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3
    • Cole KE, Strick CA, Paradis TJ, et al. Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3. J Exp Med 1998; 187:2009-21.
    • (1998) J Exp Med , vol.187 , pp. 2009-2021
    • Cole, K.E.1    Strick, C.A.2    Paradis, T.J.3
  • 9
    • 0029829106 scopus 로고    scopus 로고
    • Chemokine receptor specific for IP10 and Mig: Structure, function, and expression in activated T-lymphocytes
    • Loetscher M, Gerber B, Loetscher P, et al. Chemokine receptor specific for IP10 and Mig: structure, function, and expression in activated T-lymphocytes. J Exp Med 1996; 184:963-9.
    • (1996) J Exp Med , vol.184 , pp. 963-969
    • Loetscher, M.1    Gerber, B.2    Loetscher, P.3
  • 10
    • 0035879198 scopus 로고    scopus 로고
    • Cole AM, Ganz T, Liese AM, Burdick MD, Liu L, Strieter RM. Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity. J Immunol 2001; 167:623-7.
    • Cole AM, Ganz T, Liese AM, Burdick MD, Liu L, Strieter RM. Cutting edge: IFN-inducible ELR-CXC chemokines display defensin-like antimicrobial activity. J Immunol 2001; 167:623-7.
  • 11
    • 0142093059 scopus 로고    scopus 로고
    • Many chemokines including CCL20/MIP-3 alpha display antimicrobial activity
    • Yang D, Chen Q, Hoover DM, et al. Many chemokines including CCL20/MIP-3 alpha display antimicrobial activity. J Leukoc Biol 2003; 74:448-55.
    • (2003) J Leukoc Biol , vol.74 , pp. 448-455
    • Yang, D.1    Chen, Q.2    Hoover, D.M.3
  • 12
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti VA. Streptococcal M protein: molecular design and biological behavior. Clin Microbiol Rev 1989; 2:285-314.
    • (1989) Clin Microbiol Rev , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 13
    • 77957100477 scopus 로고    scopus 로고
    • The revival of group A streptococcal diseases with a commentary on staphylococcal toxic shock syndrome
    • Krause R, ed, New York: Academic Press
    • Musser JM, Krause RM. The revival of group A streptococcal diseases with a commentary on staphylococcal toxic shock syndrome. In: Krause R, ed. Emerging infections. New York: Academic Press, 1998:185-218.
    • (1998) Emerging infections , pp. 185-218
    • Musser, J.M.1    Krause, R.M.2
  • 14
    • 0030067110 scopus 로고    scopus 로고
    • Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function
    • Åkesson P, Sjöholm AG, Björck L. Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function. J Biol Chem 1996;271:1081-8.
    • (1996) J Biol Chem , vol.271 , pp. 1081-1088
    • Åkesson, P.1    Sjöholm, A.G.2    Björck, L.3
  • 15
    • 0032539905 scopus 로고    scopus 로고
    • Hypervariability generated by natural selection in an extracellular complement-inhibiting protein of serotype Ml strains of group A streptococcus
    • Stockbauer KE, Grigsby D, Pan X, et al. Hypervariability generated by natural selection in an extracellular complement-inhibiting protein of serotype Ml strains of group A streptococcus. Proc Natl Acad Sci USA 1998;95:3128- 33.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3128-3133
    • Stockbauer, K.E.1    Grigsby, D.2    Pan, X.3
  • 16
    • 0032812780 scopus 로고    scopus 로고
    • Rapid selection of complement-inhibiting protein variants in group A streptococcus epidemic waves
    • Hoe NP, Nakashima K, Lukomski S, et al. Rapid selection of complement-inhibiting protein variants in group A streptococcus epidemic waves. Nat Med 1999; 5:924-9.
    • (1999) Nat Med , vol.5 , pp. 924-929
    • Hoe, N.P.1    Nakashima, K.2    Lukomski, S.3
  • 17
    • 0034937066 scopus 로고    scopus 로고
    • Streptococcal inhibitor of complement (SIC) inhibits the membrane attack complex by preventing uptake of C567 onto cell membranes
    • Fernie-King BA, Seilly DJ, Willers C, Wurzner R, Davies A, Lachmann PJ. Streptococcal inhibitor of complement (SIC) inhibits the membrane attack complex by preventing uptake of C567 onto cell membranes. Immunology 2001; 103:390-8.
    • (2001) Immunology , vol.103 , pp. 390-398
    • Fernie-King, B.A.1    Seilly, D.J.2    Willers, C.3    Wurzner, R.4    Davies, A.5    Lachmann, P.J.6
  • 18
    • 0036716438 scopus 로고    scopus 로고
    • Streptococcal inhibitor of complement inhibits two additional components of the mucosal innate immune system: Secretory leukocyte proteinase inhibitor and lysozyme
    • Fernie-King BA, Seilly DJ, Davies A, Lachmann PJ. Streptococcal inhibitor of complement inhibits two additional components of the mucosal innate immune system: secretory leukocyte proteinase inhibitor and lysozyme. Infect Immun 2002; 70:4908-16.
    • (2002) Infect Immun , vol.70 , pp. 4908-4916
    • Fernie-King, B.A.1    Seilly, D.J.2    Davies, A.3    Lachmann, P.J.4
  • 19
    • 0037930850 scopus 로고    scopus 로고
    • Frick IM, Åkesson P, Rasmussen M, Schmidtchen A, Björck L. SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides. J Biol Chem 2003; 278:16561-6.
    • Frick IM, Åkesson P, Rasmussen M, Schmidtchen A, Björck L. SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides. J Biol Chem 2003; 278:16561-6.
  • 20
    • 0242335085 scopus 로고    scopus 로고
    • Molecular characterization of the chemokine receptor CXCR3: Evidence for the involvement of distinct extracellular domains in a multi-step model of ligand binding and receptor activation
    • Xanthou G, Williams TJ, Pease JE. Molecular characterization of the chemokine receptor CXCR3: evidence for the involvement of distinct extracellular domains in a multi-step model of ligand binding and receptor activation. Eur J Immunol 2003; 33:2927-36.
    • (2003) Eur J Immunol , vol.33 , pp. 2927-2936
    • Xanthou, G.1    Williams, T.J.2    Pease, J.E.3
  • 21
    • 0025267751 scopus 로고
    • Small colloidal gold conjugated to Fab fragments or to immunoglobulin G as high-resolution labels for electron microscopy: A technical overview
    • Baschong W, Wrigley NG. Small colloidal gold conjugated to Fab fragments or to immunoglobulin G as high-resolution labels for electron microscopy: a technical overview. J Electron Microsc Tech 1990; 14:313-23.
    • (1990) J Electron Microsc Tech , vol.14 , pp. 313-323
    • Baschong, W.1    Wrigley, N.G.2
  • 22
    • 0018082456 scopus 로고
    • Ultrastructural localization of intracellular antigens by the use of protein A-gold complex
    • Roth J, Bendayan M, Orci L. Ultrastructural localization of intracellular antigens by the use of protein A-gold complex. J Histochem Cytochem 1978; 26:1074-81.
    • (1978) J Histochem Cytochem , vol.26 , pp. 1074-1081
    • Roth, J.1    Bendayan, M.2    Orci, L.3
  • 23
    • 0042622380 scopus 로고    scopus 로고
    • Swiss-model: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC. Swiss-model: an automated protein homology-modeling server. Nucleic Acids Res 2003; 31:3381-5.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 24
    • 0033579486 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of truncated human GRO-beta [5-73] and its structural comparison with CXC-chemokine family members GRO-alpha and IL-8
    • Qian YQ, Johanson K, McDevitt P. Nuclear magnetic resonance solution structure of truncated human GRO-beta [5-73] and its structural comparison with CXC-chemokine family members GRO-alpha and IL-8. J Mol Biol 1999;294: 1065-72.
    • (1999) J Mol Biol , vol.294 , pp. 1065-1072
    • Qian, Y.Q.1    Johanson, K.2    McDevitt, P.3
  • 25
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • Kim DE, Chivian D, Baker D. Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res 2004; 32:W526-31.
    • (2004) Nucleic Acids Res , vol.32
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 27
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans as exemplified by chemokines
    • Handel TM, Johnson Z, Crown SE, Lau EK, Proudfoot AE. Regulation of protein function by glycosaminoglycans as exemplified by chemokines. Annu Rev Biochem 2005; 74:385-410.
    • (2005) Annu Rev Biochem , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 28
    • 24144501128 scopus 로고    scopus 로고
    • The physiology of saliva and transfer of drugs into saliva
    • Aps JK, Martens LC. The physiology of saliva and transfer of drugs into saliva. Forensic Sci Int 2005; 150:119-31.
    • (2005) Forensic Sci Int , vol.150 , pp. 119-131
    • Aps, J.K.1    Martens, L.C.2
  • 29
    • 0038242202 scopus 로고    scopus 로고
    • Crystal structures of oligomeric forms of the IP-10/CXCL10 chemokine
    • Swaminathan GJ, Holloway DE, Colvin RA, et al. Crystal structures of oligomeric forms of the IP-10/CXCL10 chemokine. Structure 2003; 11:521-32.
    • (2003) Structure , vol.11 , pp. 521-532
    • Swaminathan, G.J.1    Holloway, D.E.2    Colvin, R.A.3
  • 30
    • 3342901589 scopus 로고    scopus 로고
    • NMR structure of CXCR3 binding chemokine CXCL11 (ITAC)
    • Booth V, Clark-Lewis I, Sykes BD. NMR structure of CXCR3 binding chemokine CXCL11 (ITAC). Protein Sci 2004; 13:2022-8.
    • (2004) Protein Sci , vol.13 , pp. 2022-2028
    • Booth, V.1    Clark-Lewis, I.2    Sykes, B.D.3
  • 31
    • 0033955513 scopus 로고    scopus 로고
    • Nonpolar inactivation of the hypervariable Streptococcal inhibitor of complement gene (sic) in serotype M1 Streptococcus pyogenes significantly decreases mouse mucosal colonization
    • Lukomski S, Hoe NP, Abdi I, et al. Nonpolar inactivation of the hypervariable Streptococcal inhibitor of complement gene (sic) in serotype M1 Streptococcus pyogenes significantly decreases mouse mucosal colonization. Infect Immun 2000; 68:535-42.
    • (2000) Infect Immun , vol.68 , pp. 535-542
    • Lukomski, S.1    Hoe, N.P.2    Abdi, I.3
  • 32
    • 0037188512 scopus 로고    scopus 로고
    • Insight into the molecular basis of pathogen abundance: Group A Streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells
    • Hoe NP, Ireland RM, DeLeo FR, et al. Insight into the molecular basis of pathogen abundance: group A Streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells. Proc Natl Acad Sci USA 2002; 99:7646-51.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7646-7651
    • Hoe, N.P.1    Ireland, R.M.2    DeLeo, F.R.3
  • 33
    • 0037143532 scopus 로고    scopus 로고
    • The CXCR3 binding chemokine IP-10/CXCL10: Structure and receptor interactions
    • Booth V, Keizer DW, Kamphuis MB, Clark-Lewis I, Sykes BD. The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions. Biochemistry 2002; 41:10418-25.
    • (2002) Biochemistry , vol.41 , pp. 10418-10425
    • Booth, V.1    Keizer, D.W.2    Kamphuis, M.B.3    Clark-Lewis, I.4    Sykes, B.D.5
  • 34
    • 0038608022 scopus 로고    scopus 로고
    • CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10)
    • Campanella GS, Lee EM, Sun J, Luster AD. CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10). J Biol Chem 2003;278:17066-74.
    • (2003) J Biol Chem , vol.278 , pp. 17066-17074
    • Campanella, G.S.1    Lee, E.M.2    Sun, J.3    Luster, A.D.4
  • 35
    • 0028046519 scopus 로고
    • Group A streptococci efficiently invade human respiratory epithelial cells
    • LaPenta D, Rubens C, Chi E, Cleary PP. Group A streptococci efficiently invade human respiratory epithelial cells. Proc Natl Acad Sci USA 1994; 91:12115-9.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12115-12119
    • LaPenta, D.1    Rubens, C.2    Chi, E.3    Cleary, P.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.