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Volumn 80, Issue 14, 2006, Pages 6895-6905

The 2.6-angstrom structure of infectious bursal disease virus-derived t=1 particles reveals new stabilizing elements of the virus capsid

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; HISTIDINE; PROTEIN VP2; THREONINE;

EID: 33745797693     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00368-06     Document Type: Article
Times cited : (60)

References (44)
  • 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
  • 3
    • 0035202793 scopus 로고    scopus 로고
    • Molecular determinants of virulence, cell tropism, and pathogenic phenotype of infectious bursal disease virus
    • Brandt, M., K. Yao, M. Liu, R. A. Heckert, and V. N. Vakharia. 2001. Molecular determinants of virulence, cell tropism, and pathogenic phenotype of infectious bursal disease virus. J. Virol. 75:11974-11982.
    • (2001) J. Virol. , vol.75 , pp. 11974-11982
    • Brandt, M.1    Yao, K.2    Liu, M.3    Heckert, R.A.4    Vakharia, V.N.5
  • 4
    • 0023178609 scopus 로고
    • Susceptibility of chicken blood lymphoblasts and monocytes to infectious bursal disease virus (IBDV)
    • Burkhardt, E., and H. Muller. 1987. Susceptibility of chicken blood lymphoblasts and monocytes to infectious bursal disease virus (IBDV). Arch. Virol. 94:297-303.
    • (1987) Arch. Virol. , vol.94 , pp. 297-303
    • Burkhardt, E.1    Muller, H.2
  • 5
    • 0034755358 scopus 로고    scopus 로고
    • C terminus of infectious bursal disease virus major capsid protein VP2 is involved in definition of the T number for capsid assembly
    • Caston, J. R., J. L. Martinez-Torrecuadrada, A. Maraver, E. Lombardo, J. F. Rodriguez, J. I. Casal, and J. L. Carrascosa. 2001. C terminus of infectious bursal disease virus major capsid protein VP2 is involved in definition of the T number for capsid assembly. J. Virol. 75:10815-10828.
    • (2001) J. Virol. , vol.75 , pp. 10815-10828
    • Caston, J.R.1    Martinez-Torrecuadrada, J.L.2    Maraver, A.3    Lombardo, E.4    Rodriguez, J.F.5    Casal, J.I.6    Carrascosa, J.L.7
  • 6
    • 0036168067 scopus 로고    scopus 로고
    • The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids
    • Chevalier, C., J. Lepault, I. Erk, B. Da Costa, and B. Delmas. 2002. The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids. J. Virol. 76:2384-2392.
    • (2002) J. Virol. , vol.76 , pp. 2384-2392
    • Chevalier, C.1    Lepault, J.2    Erk, I.3    Da Costa, B.4    Delmas, B.5
  • 11
    • 0025727426 scopus 로고
    • Sequence analysis of infectious pancreatic necrosis virus genome segment B and its encoded VP1 protein: A putative RNA-dependent RNA polymerase lacking the Gly-Asp-Asp motif
    • Duncan, R., C. L. Mason, E. Nagy, J. A. Leong, and P. Dobos. 1991. Sequence analysis of infectious pancreatic necrosis virus genome segment B and its encoded VP1 protein: a putative RNA-dependent RNA polymerase lacking the Gly-Asp-Asp motif. Virology 181:541-552.
    • (1991) Virology , vol.181 , pp. 541-552
    • Duncan, R.1    Mason, C.L.2    Nagy, E.3    Leong, J.A.4    Dobos, P.5
  • 12
    • 0016908379 scopus 로고
    • The epizootiology of infectious bursal disease and prevention of it by immunization
    • Edgar, S. A., and Y. Cho. 1976. The epizootiology of infectious bursal disease and prevention of it by immunization. Dev. Biol. Stand. 33:349-356.
    • (1976) Dev. Biol. Stand. , vol.33 , pp. 349-356
    • Edgar, S.A.1    Cho, Y.2
  • 13
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R. M. 1997. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15: 132-134, 112-113.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 14
    • 0000625192 scopus 로고
    • Proceedings of the CCP4 study weekend. Data collection and processing
    • Evans, P. 1994. Proceedings of the CCP4 study weekend. Data collection and processing. Acta Crystallogr. Sect. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.50 , pp. 760-763
    • Evans, P.1
  • 15
    • 1842339336 scopus 로고    scopus 로고
    • The major antigenic protein of infectious bursal disease virus, VP2, is an apoptotic inducer
    • Fernandez-Arias, A., S. Martinez, and J. F. Rodriguez. 1997. The major antigenic protein of infectious bursal disease virus, VP2, is an apoptotic inducer. J. Virol. 71:8014-8018.
    • (1997) J. Virol. , vol.71 , pp. 8014-8018
    • Fernandez-Arias, A.1    Martinez, S.2    Rodriguez, J.F.3
  • 17
    • 0036301072 scopus 로고    scopus 로고
    • Detailed architecture of a DNA translocating machine: The high-resolution structure of the bacteriophage phi29 connector particle
    • Guasch, A., J. Pous, B. Ibarra, F. X. Gomis-Ruth, J. M. Valpuesta, N. Sousa, J. L. Carrascosa, and M. Coll. 2002. Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle. J. Mol. Biol. 315:663-676.
    • (2002) J. Mol. Biol. , vol.315 , pp. 663-676
    • Guasch, A.1    Pous, J.2    Ibarra, B.3    Gomis-Ruth, F.X.4    Valpuesta, J.M.5    Sousa, N.6    Carrascosa, J.L.7    Coll, M.8
  • 18
    • 0031569393 scopus 로고    scopus 로고
    • The refined structure of human rhinovitus 16 at 2.15 a resolution: Implications for the viral life cycle
    • Hadfield, A. T., W. Lee, R. Zhao, M. A. Oliveira, I. Minor, R. R. Rueckert, and M. G. Rossmann. 1997. The refined structure of human rhinovitus 16 at 2.15 A resolution: implications for the viral life cycle. Structure 5:427-441.
    • (1997) Structure , vol.5 , pp. 427-441
    • Hadfield, A.T.1    Lee, W.2    Zhao, R.3    Oliveira, M.A.4    Minor, I.5    Rueckert, R.R.6    Rossmann, M.G.7
  • 20
    • 0032979159 scopus 로고    scopus 로고
    • Lipofectin increases the specific activity of cypovirus particles for cultured insect cells
    • Hill, C. L., T. F. Booth, D. I. Stuart, and P. P. Mertens. 1999. Lipofectin increases the specific activity of cypovirus particles for cultured insect cells. J. Virol. Methods 78:177-189.
    • (1999) J. Virol. Methods , vol.78 , pp. 177-189
    • Hill, C.L.1    Booth, T.F.2    Stuart, D.I.3    Mertens, P.P.4
  • 21
    • 0030026807 scopus 로고    scopus 로고
    • Functional implications of protein-protein interactions in icosahedral viruses
    • Johnson, J. E. 1996. Functional implications of protein-protein interactions in icosahedral viruses. Proc. Natl. Acad. Sci. USA 93:27-33.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 27-33
    • Johnson, J.E.1
  • 22
    • 0030841587 scopus 로고    scopus 로고
    • Electron density map interpretation
    • C. Carter and R. Sweet (ed.). Academic Press, London, United Kingdom
    • Jones, T., and M. Kjeldgaard. 1997. Electron density map interpretation, p. 173-208. In C. Carter and R. Sweet (ed.), Macromolecular crystallography, vol. B. Academic Press, London, United Kingdom.
    • (1997) Macromolecular Crystallography , vol.B , pp. 173-208
    • Jones, T.1    Kjeldgaard, M.2
  • 23
    • 0024058731 scopus 로고
    • Biochemistry and immunology of infectious bursal disease virus
    • Kibenge, F. S., A. S. Dhillon, and R. G. Russell. 1988. Biochemistry and immunology of infectious bursal disease virus. J. Gen. Virol. 69:1757-1775.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1757-1775
    • Kibenge, F.S.1    Dhillon, A.S.2    Russell, R.G.3
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 0031031329 scopus 로고    scopus 로고
    • Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles
    • Lawton, J. A., M. K. Estes, and B. V. Prasad. 1997. Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat. Struct. Biol. 4:118-121.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 118-121
    • Lawton, J.A.1    Estes, M.K.2    Prasad, B.V.3
  • 26
    • 0002414103 scopus 로고
    • Macromolecular data processing
    • D. Moras, A. Podjarny, and J. Thiery (ed.). Oxford University Press, Oxford, United Kingdom
    • Leslie, A. 1991. Macromolecular data processing, p. 27-38. In D. Moras, A. Podjarny, and J. Thiery (ed.), Crystallographic computing, vol. 5. Oxford University Press, Oxford, United Kingdom.
    • (1991) Crystallographic Computing , vol.5 , pp. 27-38
    • Leslie, A.1
  • 27
    • 0033044128 scopus 로고    scopus 로고
    • Adaptation of very virulent infectious bursal disease virus to chicken embryonic fibroblasts by site-directed mutagenesis of residues 279 and 284 of viral coat protein VP2
    • Lim, B. L., Y. Cao, T. Yu, and C. W. Mo. 1999. Adaptation of very virulent infectious bursal disease virus to chicken embryonic fibroblasts by site-directed mutagenesis of residues 279 and 284 of viral coat protein VP2. J. Virol. 73:2854-2862.
    • (1999) J. Virol. , vol.73 , pp. 2854-2862
    • Lim, B.L.1    Cao, Y.2    Yu, T.3    Mo, C.W.4
  • 28
    • 0032786536 scopus 로고    scopus 로고
    • VP1, the putative RNA-dependent RNA polymerase of infectious bursal disease virus, forms complexes with the capsid protein VP3, leading to efficient encapsidation into virus-like particles
    • Lombardo, E., A. Maraver, J. R. Castón, J. Rivera, A. Fernández-Arias, A. Serrano, J. L. Carrascosa, and J. F. Rodriguez. 1999. VP1, the putative RNA-dependent RNA polymerase of infectious bursal disease virus, forms complexes with the capsid protein VP3, leading to efficient encapsidation into virus-like particles. J. Virol. 73:6973-6983.
    • (1999) J. Virol. , vol.73 , pp. 6973-6983
    • Lombardo, E.1    Maraver, A.2    Castón, J.R.3    Rivera, J.4    Fernández- Arias, A.5    Serrano, A.6    Carrascosa, J.L.7    Rodriguez, J.F.8
  • 29
    • 0015372467 scopus 로고
    • Avian infectious bursal agent. 1. In vivo viral morphogenesis
    • Lunger, P., and T. Maddux. 1972. Avian infectious bursal agent. 1. In vivo viral morphogenesis. Avian Dis. 16:874-893.
    • (1972) Avian Dis. , vol.16 , pp. 874-893
    • Lunger, P.1    Maddux, T.2
  • 30
    • 0037688319 scopus 로고    scopus 로고
    • The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly
    • Maraver, A., A. Ona, F. Abaitua, D. Gonzalez, R. Clemente, J. A. Ruiz-Diaz, J. R. Caston, F. Pazos, and J. F. Rodriguez. 2003. The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly. J. Virol. 77:6438-6449.
    • (2003) J. Virol. , vol.77 , pp. 6438-6449
    • Maraver, A.1    Ona, A.2    Abaitua, F.3    Gonzalez, D.4    Clemente, R.5    Ruiz-Diaz, J.A.6    Caston, J.R.7    Pazos, F.8    Rodriguez, J.F.9
  • 31
    • 0034533673 scopus 로고    scopus 로고
    • Different architectures in the assembly of infectious bursal disease virus capsid proteins expressed in insect cells
    • Martinez-Torrecuadrada, J. L., J. R. Caston, M. Castro, J. L. Carrascosa, J. F. Rodriguez, and J. I. Casal. 2000. Different architectures in the assembly of infectious bursal disease virus capsid proteins expressed in insect cells. Virology 278:322-331.
    • (2000) Virology , vol.278 , pp. 322-331
    • Martinez-Torrecuadrada, J.L.1    Caston, J.R.2    Castro, M.3    Carrascosa, J.L.4    Rodriguez, J.F.5    Casal, J.I.6
  • 32
    • 0035794638 scopus 로고    scopus 로고
    • Atomic structure of the major capsid protein of rotavirus: Implications for the architecture of the virion
    • Mathieu, M., I. Petitpas, J. Navaza, J. Lepault, E. Kohli, P. Pothier, B. V. Prasad, J. Cohen, and F. A. Rey. 2001. Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion. EMBO J. 20:1485-1497.
    • (2001) EMBO J. , vol.20 , pp. 1485-1497
    • Mathieu, M.1    Petitpas, I.2    Navaza, J.3    Lepault, J.4    Kohli, E.5    Pothier, P.6    Prasad, B.V.7    Cohen, J.8    Rey, F.A.9
  • 33
  • 34
    • 0032771585 scopus 로고    scopus 로고
    • Tissue culture infectivity of different strains of infectious bursal disease virus is determined by distinct amino acids in VP2
    • Mundt, E. 1999. Tissue culture infectivity of different strains of infectious bursal disease virus is determined by distinct amino acids in VP2. J. Gen. Virol. 80:2067-2076.
    • (1999) J. Gen. Virol. , vol.80 , pp. 2067-2076
    • Mundt, E.1
  • 36
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. 1994. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50:157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 37
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface proteins
    • Nicholls, A., R. Bharadwaj, and B. Honig. 1993. GRASP: graphical representation and analysis of surface proteins. Biophys. J. 64:A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 38
    • 0021112807 scopus 로고
    • Structure of tomato busy stunt virus IV. The virus particle at 2.9 A resolution
    • Olson, A. J., G. Bricogne, and S. C. Harrison. 1983. Structure of tomato busy stunt virus IV. The virus particle at 2.9 A resolution. J. Mol. Biol. 171:61-93.
    • (1983) J. Mol. Biol. , vol.171 , pp. 61-93
    • Olson, A.J.1    Bricogne, G.2    Harrison, S.C.3
  • 40
    • 21744450430 scopus 로고    scopus 로고
    • Structural polymorphism of the major capsid protein of a double-stranded RNA virus: An amphipathic alpha helix as a molecular switch
    • Saugar, I., D. Luque, A. Ona, J. F. Rodriguez, J. L. Carrascosa, B. L. Trus, and J. R. Caston. 2005. Structural polymorphism of the major capsid protein of a double-stranded RNA virus: an amphipathic alpha helix as a molecular switch. Structure 13:1007-1017.
    • (2005) Structure , vol.13 , pp. 1007-1017
    • Saugar, I.1    Luque, D.2    Ona, A.3    Rodriguez, J.F.4    Carrascosa, J.L.5    Trus, B.L.6    Caston, J.R.7
  • 41
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic motile virus determined by X-ray crystallography and cryo-electron microscopy
    • Speir, J. A., S. Munshi, G. Wang, T. S. Baker, and J. E. Johnson. 1995. Structures of the native and swollen forms of cowpea chlorotic motile virus determined by X-ray crystallography and cryo-electron microscopy. Structure 3:63-78.
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Munshi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 43
    • 0036136631 scopus 로고    scopus 로고
    • Alteration of amino acids in VP2 of very virulent infectious bursal disease virus results in tissue culture adaptation and attenuation in chickens
    • van Loon, A. A., N. de Haas, I. Zeyda, and E. Mundt. 2002. Alteration of amino acids in VP2 of very virulent infectious bursal disease virus results in tissue culture adaptation and attenuation in chickens. J. Gen. Virol. 83:121-129.
    • (2002) J. Gen. Virol. , vol.83 , pp. 121-129
    • Van Loon, A.A.1    De Haas, N.2    Zeyda, I.3    Mundt, E.4
  • 44
    • 0035918982 scopus 로고    scopus 로고
    • Induction of apoptosis in vitro by the 17-kDa nonstructural protein of infectious bursal disease virus: Possible role in viral pathogenesis
    • Yao, K., and V. N. Vakharia. 2001. Induction of apoptosis in vitro by the 17-kDa nonstructural protein of infectious bursal disease virus: possible role in viral pathogenesis. Virology 285:50-58.
    • (2001) Virology , vol.285 , pp. 50-58
    • Yao, K.1    Vakharia, V.N.2


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