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Volumn 84, Issue 24, 2010, Pages 12665-12674

Interaction of decay-accelerating factor with echovirus 7

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; DECAY ACCELERATING FACTOR;

EID: 78649414884     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00837-10     Document Type: Article
Times cited : (37)

References (68)
  • 1
    • 0025266637 scopus 로고
    • Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3.0 å
    • Arnold, E., and M. G. Rossmann. 1990. Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3.0 Å. J. Mol. Biol. 211:763-801.
    • (1990) J. Mol. Biol. , vol.211 , pp. 763-801
    • Arnold, E.1    Rossmann, M.G.2
  • 2
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold, K., L. Bordoli, J. Kopp, and T. Schwede. 2006. The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling. Bioinformatics 22:196-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 5
  • 6
    • 0026580865 scopus 로고
    • Identification of the integrin VLA-2 as a receptor for echovirus 1
    • Bergelson, J. M., M. P. Shepley, B. M. Chan, M. E. Hemler, and R. W. Finberg. 1992. Identification of the integrin VLA-2 as a receptor for echovirus 1. Science 255:1718-1720.
    • (1992) Science , vol.255 , pp. 1718-1720
    • Bergelson, J.M.1    Shepley, M.P.2    Chan, B.M.3    Hemler, M.E.4    Finberg, R.W.5
  • 7
    • 0029880767 scopus 로고    scopus 로고
    • Localization of classical and alternative pathway regulatory activity within the decay-accelerating factor
    • Brodbeck, W. G., D. Liu, J. Sperry, C. Mold, and M. E. Medof. 1996. Localization of classical and alternative pathway regulatory activity within the decay-accelerating factor. J. Immunol. 156:2528-2533.
    • (1996) J. Immunol. , vol.156 , pp. 2528-2533
    • Brodbeck, W.G.1    Liu, D.2    Sperry, J.3    Mold, C.4    Medof, M.E.5
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 13
    • 0024316730 scopus 로고
    • Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus
    • Filman, D. J., R. Syed, M. Chow, A. J. Macadam, P. D. MInor, and J. M. Hogle. 1989. Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus. EMBO J. 8:1567-1579.
    • (1989) EMBO J. , vol.8 , pp. 1567-1579
    • Filman, D.J.1    Syed, R.2    Chow, M.3    Macadam, A.J.4    Minor, P.D.5    Hogle, J.M.6
  • 18
    • 0037059776 scopus 로고    scopus 로고
    • Decay-accelerating factor (DAF), complement receptor 1 (CR1), and factor H dissociate the complement AP C3 convertase (C3bBb) via sites on the type a domain of Bb
    • Hourcade, D. E., L. Mitchell, L. A. Kuttner-Kondo, J. P. Atkinson, and M. E. Medof. 2002. Decay-accelerating factor (DAF), complement receptor 1 (CR1), and factor H dissociate the complement AP C3 convertase (C3bBb) via sites on the type A domain of Bb. J. Biol. Chem. 277:1107-1111.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1107-1111
    • Hourcade, D.E.1    Mitchell, L.2    Kuttner-Kondo, L.A.3    Atkinson, J.P.4    Medof, M.E.5
  • 19
    • 0022484141 scopus 로고
    • Modulation of humoral response to a 12-amino-acid site on the poliovirus virion
    • Icenogle, J. P., P. D. Minor, M. Ferguson, and J. M. Hogle. 1986. Modulation of humoral response to a 12-amino-acid site on the poliovirus virion. J. Virol. 60:297-301.
    • (1986) J. Virol. , vol.60 , pp. 297-301
    • Icenogle, J.P.1    Minor, P.D.2    Ferguson, M.3    Hogle, J.M.4
  • 21
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 22
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt, G. J., and R. J. Read. 1997. Not your average density. Structure 5:1557-1569.
    • (1997) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 23
    • 0033571522 scopus 로고    scopus 로고
    • Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor
    • Kolatkar, P. R., J. Bella, N. H. Olson, C. M. Bator, T. S. Baker, and M. G. Rossmann. 1999. Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J. 18:6249-6259.
    • (1999) EMBO J. , vol.18 , pp. 6249-6259
    • Kolatkar, P.R.1    Bella, J.2    Olson, N.H.3    Bator, C.M.4    Baker, T.S.5    Rossmann, M.G.6
  • 24
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and K. Henrick. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 25
    • 34447339808 scopus 로고    scopus 로고
    • Interaction of major group rhinoviruses with their cellular receptor, ICAM-1
    • B. L. Semler and E. Wimmer (ed.), ASM Press, Washington, DC
    • Kuhn, R. J., and M. G. Rossmann. 2002. Interaction of major group rhinoviruses with their cellular receptor, ICAM-1, p. 85-91. In B. L. Semler and E. Wimmer (ed.), Molecular biology of picornaviruses. ASM Press, Washington, DC.
    • (2002) Molecular Biology of Picornaviruses , pp. 85-91
    • Kuhn, R.J.1    Rossmann, M.G.2
  • 27
    • 52649176344 scopus 로고    scopus 로고
    • Locally produced C5a binds to T cell-expressed C5aR to enhance effector T-cell expansion by limiting antigen-induced apoptosis
    • Lalli, P. N., M. G. Strainic, M. Yang, F. Lin, M. E. Medof, and P. S. Heeger. 2008. Locally produced C5a binds to T cell-expressed C5aR to enhance effector T-cell expansion by limiting antigen-induced apoptosis. Blood 112:1759-1766.
    • (2008) Blood , vol.112 , pp. 1759-1766
    • Lalli, P.N.1    Strainic, M.G.2    Yang, M.3    Lin, F.4    Medof, M.E.5    Heeger, P.S.6
  • 28
    • 0032514905 scopus 로고    scopus 로고
    • Determination of the affinity and kinetic constants for the interaction between the human echovirus 11 and its cellular receptor, CD55
    • Lea, S. M., R. M. Powell, T. McKee, D. J. Evans, D. Brown, D. I. Stuart, and P. A. van der Merwe. 1998. Determination of the affinity and kinetic constants for the interaction between the human echovirus 11 and its cellular receptor, CD55. J. Biol. Chem. 273:30443-30447.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30443-30447
    • Lea, S.M.1    Powell, R.M.2    McKee, T.3    Evans, D.J.4    Brown, D.5    Stuart, D.I.6    Van Der Merwe, P.A.7
  • 29
    • 44449106678 scopus 로고    scopus 로고
    • IFN-gamma and IL-17 production in experimental autoimmune encephalomyelitis depends on local APC-T cell complement production
    • Liu, J., F. Lin, M. G. Strainic, F. An, R. H. Miller, C. Z. Altuntas, P. S. Heeger, V. K. Tuohy, and M. E. Medof. 2008. IFN-gamma and IL-17 production in experimental autoimmune encephalomyelitis depends on local APC-T cell complement production. J. Immunol. 180:5882-5889.
    • (2008) J. Immunol. , vol.180 , pp. 5882-5889
    • Liu, J.1    Lin, F.2    Strainic, M.G.3    An, F.4    Miller, R.H.5    Altuntas, C.Z.6    Heeger, P.S.7    Tuohy, V.K.8    Medof, M.E.9
  • 33
    • 0032855287 scopus 로고    scopus 로고
    • 3 (vitronectin receptor) is a candidate receptor for the virulent echovirus 9 strain Barty
    • 3 (vitronectin receptor) is a candidate receptor for the virulent echovirus 9 strain Barty. J. Gen. Virol. 80:2311-2313.
    • (1999) J. Gen. Virol. , vol.80 , pp. 2311-2313
    • Nelsen-Salaz, B.1    Eggers, H.J.2    Zimmermann, H.3
  • 34
    • 0037770209 scopus 로고    scopus 로고
    • A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid
    • Neumann, E., R. Moser, L. Snyers, D. Blaas, and E. A. Hewat. 2003. A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid. J. Virol. 77:8504-8511.
    • (2003) J. Virol. , vol.77 , pp. 8504-8511
    • Neumann, E.1    Moser, R.2    Snyers, L.3    Blaas, D.4    Hewat, E.A.5
  • 35
    • 0033020133 scopus 로고    scopus 로고
    • Molecular evolution of the human enteroviruses: Correlation of serotype with VP1 sequence and application to picornavirus classification
    • Oberste, M. S., K. Maher, D. R. Kilpatrick, and M. A. Pallansch. 1999. Molecular evolution of the human enteroviruses: correlation of serotype with VP1 sequence and application to picornavirus classification. J. Virol. 73:1941-1948.
    • (1999) J. Virol. , vol.73 , pp. 1941-1948
    • Oberste, M.S.1    Maher, K.2    Kilpatrick, D.R.3    Pallansch, M.A.4
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 33646167688 scopus 로고    scopus 로고
    • Structural and functional insights into the interaction of echoviruses and decay-accelerating factor
    • Pettigrew, D. M., D. T. Williams, D. Kerrigan, D. J. Evans, S. M. Lea, and D. Bhella. 2006. Structural and functional insights into the interaction of echoviruses and decay-accelerating factor. J. Biol. Chem. 281:5169-5177.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5169-5177
    • Pettigrew, D.M.1    Williams, D.T.2    Kerrigan, D.3    Evans, D.J.4    Lea, S.M.5    Bhella, D.6
  • 40
    • 0031850010 scopus 로고    scopus 로고
    • Characterization of echoviruses that bind decay accelerating factor (CD55): Evidence that some haemagglutinating strains use more than one cellular receptor
    • Powell, R. M., V. Schmitt, T. Ward, I. Goodfellow, D. J. Evans, and J. W. Almond. 1998. Characterization of echoviruses that bind decay accelerating factor (CD55): evidence that some haemagglutinating strains use more than one cellular receptor. J. Gen. Virol. 79:1707-1713.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1707-1713
    • Powell, R.M.1    Schmitt, V.2    Ward, T.3    Goodfellow, I.4    Evans, D.J.5    Almond, J.W.6
  • 41
    • 0030785478 scopus 로고    scopus 로고
    • Interaction between echovirus 7 and its receptor, decay-accelerating factor (CD55): Evidence for a secondary cellular factor in a-particle formation
    • Powell, R. M., T. Ward, D. J. Evans, and J. W. Almond. 1997. Interaction between echovirus 7 and its receptor, decay-accelerating factor (CD55): evidence for a secondary cellular factor in A-particle formation. J. Virol. 71:9306-9312.
    • (1997) J. Virol. , vol.71 , pp. 9306-9312
    • Powell, R.M.1    Ward, T.2    Evans, D.J.3    Almond, J.W.4
  • 42
    • 0032747586 scopus 로고    scopus 로고
    • Mapping the binding domains on decay-accelerating factor (DAF) for haemagglutinating enteroviruses: Implications for evolution of a DAF-binding phenotype
    • Powell, R. M., T. Ward, I. Goodfellow, J. W. Almond, and D. J. Evans. 1999. Mapping the binding domains on decay-accelerating factor (DAF) for haemagglutinating enteroviruses: implications for evolution of a DAF-binding phenotype. J. Gen. Virol. 80:3145-3152.
    • (1999) J. Gen. Virol. , vol.80 , pp. 3145-3152
    • Powell, R.M.1    Ward, T.2    Goodfellow, I.3    Almond, J.W.4    Evans, D.J.5
  • 44
    • 0033780164 scopus 로고    scopus 로고
    • Fitting atomic models into electron microscopy maps
    • Rossmann, M. G. 2000. Fitting atomic models into electron microscopy maps. Acta Crystallogr. D Biol. Crystallogr. 56:1341-1349.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1341-1349
    • Rossmann, M.G.1
  • 45
    • 0028032395 scopus 로고
    • Viral cell recognition and entry
    • Rossmann, M. G. 1994. Viral cell recognition and entry. Protein Sci. 3:1712-1725.
    • (1994) Protein Sci. , vol.3 , pp. 1712-1725
    • Rossmann, M.G.1
  • 48
    • 0035783056 scopus 로고    scopus 로고
    • Combining electron microscopic with X-ray crystallographic structures
    • Rossmann, M. G., R. Bernal, and S. V. Pletnev. 2001. Combining electron microscopic with X-ray crystallographic structures. J. Struct. Biol. 136:190-200.
    • (2001) J. Struct. Biol. , vol.136 , pp. 190-200
    • Rossmann, M.G.1    Bernal, R.2    Pletnev, S.V.3
  • 49
  • 50
    • 0001952393 scopus 로고
    • Picornaviridae and their replication
    • B. N. Fields et al. (ed.), 2nd ed., Raven Press, New York, NY
    • Rueckert, R. R. 1990. Picornaviridae and their replication, p. 507-548. In B. N. Fields et al. (ed.), Fields virology, 2nd ed., vol. 1. Raven Press, New York, NY.
    • (1990) Fields Virology , vol.1 , pp. 507-548
    • Rueckert, R.R.1
  • 52
    • 0031008583 scopus 로고    scopus 로고
    • Coxsackievirus A21 binds to decay-accelerating factor but requires intercellular adhesion molecule 1 for cell entry
    • Shafren, D. R., D. J. Dorahy, R. A. Ingham, G. F. Burns, and R. D. Barry. 1997. Coxsackievirus A21 binds to decay-accelerating factor but requires intercellular adhesion molecule 1 for cell entry. J. Virol. 71:4736-4743.
    • (1997) J. Virol. , vol.71 , pp. 4736-4743
    • Shafren, D.R.1    Dorahy, D.J.2    Ingham, R.A.3    Burns, G.F.4    Barry, R.D.5
  • 53
    • 0022644644 scopus 로고
    • Use of monoclonal antibodies to identify four neutralization immunogens on a common cold picornavirus, human rhinovirus 14
    • Sherry, B., A. G. Mosser, R. J. Colonno, and R. R. Rueckert. 1986. Use of monoclonal antibodies to identify four neutralization immunogens on a common cold picornavirus, human rhinovirus 14. J. Virol. 57:246-257.
    • (1986) J. Virol. , vol.57 , pp. 246-257
    • Sherry, B.1    Mosser, A.G.2    Colonno, R.J.3    Rueckert, R.R.4
  • 54
    • 0037708648 scopus 로고    scopus 로고
    • Identification of the pocket factors in a picornavirus
    • Smyth, M., T. Pettitt, A. Symonds, and J. Martin. 2003. Identification of the pocket factors in a picornavirus. Arch. Virol. 148:1225-1233.
    • (2003) Arch. Virol. , vol.148 , pp. 1225-1233
    • Smyth, M.1    Pettitt, T.2    Symonds, A.3    Martin, J.4
  • 55
    • 0033621704 scopus 로고    scopus 로고
    • Human parechoviruses - Biology and clinical significance
    • Stanway, G., P. Joki-Korpela, and T. Hyypiä. 2000. Human parechoviruses - biology and clinical significance. Rev. Med. Virol. 10:57-69.
    • (2000) Rev. Med. Virol. , vol.10 , pp. 57-69
    • Stanway, G.1    Joki-Korpela, P.2    Hyypiä, T.3
  • 57
    • 0036721021 scopus 로고    scopus 로고
    • A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts
    • Stuart, A. D., H. E. Eustace, T. A. McKee, and T. D. K. Brown. 2002. A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts. J. Virol. 76:9307-9322.
    • (2002) J. Virol. , vol.76 , pp. 9307-9322
    • Stuart, A.D.1    Eustace, H.E.2    McKee, T.A.3    Brown, T.D.K.4
  • 58
    • 33745903422 scopus 로고    scopus 로고
    • Coxsackievirus myocarditis: Interplay between virus and host in the pathogenesis of heart disease
    • Tam, P. E. 2006. Coxsackievirus myocarditis: interplay between virus and host in the pathogenesis of heart disease. Viral Immunol. 19:133-146.
    • (2006) Viral Immunol. , vol.19 , pp. 133-146
    • Tam, P.E.1
  • 59
    • 0031058884 scopus 로고    scopus 로고
    • Rotation function calculations with GLRF program
    • Tong, L., and M. G. Rossmann. 1997. Rotation function calculations with GLRF program. Methods Enzymol. 276:594-611.
    • (1997) Methods Enzymol. , vol.276 , pp. 594-611
    • Tong, L.1    Rossmann, M.G.2
  • 61
    • 0025957484 scopus 로고
    • The major and minor group receptor families contain all but one human rhinovirus serotype
    • Uncapher, C. R., C. M. DeWitt, and R. J. Colonno. 1991. The major and minor group receptor families contain all but one human rhinovirus serotype. Virology 180:814-817.
    • (1991) Virology , vol.180 , pp. 814-817
    • Uncapher, C.R.1    DeWitt, C.M.2    Colonno, R.J.3
  • 62
    • 2342648870 scopus 로고    scopus 로고
    • X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein
    • Verdaguer, N., I. Fita, M. Reithmayer, R. Moser, and D. Blaas. 2004. X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein. Nat. Struct. Mol. Biol. 11:429-434.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 429-434
    • Verdaguer, N.1    Fita, I.2    Reithmayer, M.3    Moser, R.4    Blaas, D.5
  • 63
    • 27244434501 scopus 로고    scopus 로고
    • Host and virus determinants of picornavirus pathogenesis and tropism
    • Whitton, J. L., C. T. Cornell, and R. Feuer. 2005. Host and virus determinants of picornavirus pathogenesis and tropism. Nat. Rev. Microbiol. 3:765-776.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 765-776
    • Whitton, J.L.1    Cornell, C.T.2    Feuer, R.3
  • 64
    • 1642364117 scopus 로고    scopus 로고
    • Interactions of decay-accelerating factor (DAF) with haemagglutinating human enteroviruses: Utilizing variation in primate DAF to map virus binding sites
    • Williams, D. T., Y. Chaudhry, I. G. Goodfellow, S. Lea, and D. J. Evans. 2004. Interactions of decay-accelerating factor (DAF) with haemagglutinating human enteroviruses: utilizing variation in primate DAF to map virus binding sites. J. Gen. Virol. 85:731-738.
    • (2004) J. Gen. Virol. , vol.85 , pp. 731-738
    • Williams, D.T.1    Chaudhry, Y.2    Goodfellow, I.G.3    Lea, S.4    Evans, D.J.5
  • 67
    • 33845338800 scopus 로고    scopus 로고
    • AUTO3DEM - An automated and high throughput program for image reconstruction of icosahedral particles
    • Yan, X., R. S. Sinkovits, and T. S. Baker. 2007. AUTO3DEM - an automated and high throughput program for image reconstruction of icosahedral particles. J. Struct. Biol. 157:73-82.
    • (2007) J. Struct. Biol. , vol.157 , pp. 73-82
    • Yan, X.1    Sinkovits, R.S.2    Baker, T.S.3


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