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Volumn 79, Issue 2, 2005, Pages 1071-1083

Impairment of nuclear pores in bovine herpesvirus 1-infected MDBK cells

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; GREEN FLUORESCENT PROTEIN; VIRUS PROTEIN;

EID: 19944426290     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.2.1071-1083.2005     Document Type: Article
Times cited : (68)

References (46)
  • 1
    • 0028885225 scopus 로고
    • The herpes simplex virus 1 UL11 proteins are associated with cytoplasmic and nuclear membranes and with nuclear bodies of infected cells
    • Baines, J. D., R. J. Jacob, L. Simmerman, and B. Roizman. 1995. The herpes simplex virus 1 UL11 proteins are associated with cytoplasmic and nuclear membranes and with nuclear bodies of infected cells. J. Virol. 69:825-833.
    • (1995) J. Virol. , vol.69 , pp. 825-833
    • Baines, J.D.1    Jacob, R.J.2    Simmerman, L.3    Roizman, B.4
  • 2
    • 0027692049 scopus 로고
    • Simian agent 8 (SA8): Morphogenesis and ultrastructure
    • Borchers, K., and M. Oezel. 1993. Simian agent 8 (SA8): morphogenesis and ultrastructure. Zentralbl. Bakteriol. 279:526-536.
    • (1993) Zentralbl. Bakteriol. , vol.279 , pp. 526-536
    • Borchers, K.1    Oezel, M.2
  • 3
    • 0028624704 scopus 로고
    • ICP34.5 influences herpes simplex virus type 1 maturation and egress from infected cells in vitro
    • Brown, S. M., A. R. MacLean, J. D. Aitken, and J. Harland. 1994. ICP34.5 influences herpes simplex virus type 1 maturation and egress from infected cells in vitro. J. Gen. Virol. 75:3679-3686.
    • (1994) J. Gen. Virol. , vol.75 , pp. 3679-3686
    • Brown, S.M.1    MacLean, A.R.2    Aitken, J.D.3    Harland, J.4
  • 4
    • 0029949793 scopus 로고    scopus 로고
    • An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: Evidence for reenvelopment during egress
    • Browne, H., S. Bell, T. Minson, and D. W. Wilson. 1996. An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress. J. Virol. 70:4311-4316.
    • (1996) J. Virol. , vol.70 , pp. 4311-4316
    • Browne, H.1    Bell, S.2    Minson, T.3    Wilson, D.W.4
  • 5
    • 0026062504 scopus 로고
    • Origin of unenveloped capsids in the cytoplasm of cells infected with herpes simplex virus 1
    • Campadelli-Fiume, G., F. Farabegoli, S. Di Gaeta, and B. Roizman. 1991. Origin of unenveloped capsids in the cytoplasm of cells infected with herpes simplex virus 1. J. Virol. 65:1589-1595.
    • (1991) J. Virol. , vol.65 , pp. 1589-1595
    • Campadelli-Fiume, G.1    Farabegoli, F.2    Di Gaeta, S.3    Roizman, B.4
  • 6
    • 0027311102 scopus 로고
    • Pseudorabies virus infection of the rat central nervous system: Ultrastructural characterization of viral replication, transport, and pathogenesis
    • Card, J. P., L. Rinaman, R. B. Lynn, B. H. Lee, R. P. Meade, R. R. Miselis, and L. W. Enquist. 1993. Pseudorabies virus infection of the rat central nervous system: ultrastructural characterization of viral replication, transport, and pathogenesis. J. Neurosci. 13:2515-2539.
    • (1993) J. Neurosci. , vol.13 , pp. 2515-2539
    • Card, J.P.1    Rinaman, L.2    Lynn, R.B.3    Lee, B.H.4    Meade, R.P.5    Miselis, R.R.6    Enquist, L.W.7
  • 7
    • 0031134805 scopus 로고    scopus 로고
    • Study of herpes simplex virus maturation during a synchronous wave of assembly
    • Church, G. A., and D. W. Wilson. 1997. Study of herpes simplex virus maturation during a synchronous wave of assembly. J. Virol. 71:3603-3612.
    • (1997) J. Virol. , vol.71 , pp. 3603-3612
    • Church, G.A.1    Wilson, D.W.2
  • 8
    • 0029563335 scopus 로고
    • Intermediate forms of glycoconjugates are present in the envelope of herpes simplex virions during their transport along the exocytic pathway
    • Di Lazzaro, C., G. Campadelli-Fiume, and M. R. Torrisi. 1995. Intermediate forms of glycoconjugates are present in the envelope of herpes simplex virions during their transport along the exocytic pathway. Virology 214:619-623.
    • (1995) Virology , vol.214 , pp. 619-623
    • Di Lazzaro, C.1    Campadelli-Fiume, G.2    Torrisi, M.R.3
  • 9
    • 0015882203 scopus 로고
    • Ultrastructural studies of the envelopment and release of guinea pig herpes-like virus in cultured cells
    • Fong, C. K., R. B. Tenser, G. D. Hsiung, and P. A. Gross. 1973. Ultrastructural studies of the envelopment and release of guinea pig herpes-like virus in cultured cells. Virology 52:468-477.
    • (1973) Virology , vol.52 , pp. 468-477
    • Fong, C.K.1    Tenser, R.B.2    Hsiung, G.D.3    Gross, P.A.4
  • 10
    • 0027939149 scopus 로고
    • Identification of the bovine herpesvirus 1 circ protein, a myristylated and virion-associated polypeptide which is not essential for virus replication in cell culture
    • Fraefel, C., M. Ackermann, and M. Schwyzer. 1994. Identification of the bovine herpesvirus 1 circ protein, a myristylated and virion-associated polypeptide which is not essential for virus replication in cell culture. J. Virol. 68:8082-8088.
    • (1994) J. Virol. , vol.68 , pp. 8082-8088
    • Fraefel, C.1    Ackermann, M.2    Schwyzer, M.3
  • 11
    • 0015544712 scopus 로고
    • Observations on the growth of varicella-zoster virus in human diploid cells
    • Gershon, A., L. Cosio, and P. A. Brunell. 1973. Observations on the growth of varicella-zoster virus in human diploid cells. J. Gen. Virol. 18:21-31.
    • (1973) J. Gen. Virol. , vol.18 , pp. 21-31
    • Gershon, A.1    Cosio, L.2    Brunell, P.A.3
  • 12
    • 0028106296 scopus 로고
    • Intracellular transport of newly synthesized varicellazoster virus: Final envelopment in the trans-Golgi network
    • Gershon, A. A., D. L. Sherman, Z. Zhu, C. A. Gabel, R. T. Ambron, and M. D. Gershon. 1994. Intracellular transport of newly synthesized varicellazoster virus: final envelopment in the trans-Golgi network. J. Virol. 68:6372-6390.
    • (1994) J. Virol. , vol.68 , pp. 6372-6390
    • Gershon, A.A.1    Sherman, D.L.2    Zhu, Z.3    Gabel, C.A.4    Ambron, R.T.5    Gershon, M.D.6
  • 13
    • 0028293282 scopus 로고
    • Membrane anchoring domain of herpes simplex virus glycoprotein gB is sufficient for nuclear envelope localization
    • Gilbert, R., K. Ghosh, L. Rasile, and H. P. Ghosh. 1994. Membrane anchoring domain of herpes simplex virus glycoprotein gB is sufficient for nuclear envelope localization. J. Virol. 68:2272-2285.
    • (1994) J. Virol. , vol.68 , pp. 2272-2285
    • Gilbert, R.1    Ghosh, K.2    Rasile, L.3    Ghosh, H.P.4
  • 14
    • 0025218465 scopus 로고
    • Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110
    • Gong, M., and E. Kieff. 1990. Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110. J. Virol. 64:1507-1516.
    • (1990) J. Virol. , vol.64 , pp. 1507-1516
    • Gong, M.1    Kieff, E.2
  • 15
    • 0035087651 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses: Comparative ultrastructural study
    • Granzow, H. 2001. Egress of alphaherpesviruses: comparative ultrastructural study. J. Virol. 75:3675-3684.
    • (2001) J. Virol. , vol.75 , pp. 3675-3684
    • Granzow, H.1
  • 16
    • 0031048830 scopus 로고    scopus 로고
    • Ultrastructural analysis of the replication cycle of pseudorabies virus in cell culture: A reassessment
    • Granzow, H., F. Weiland, A. Jons, B. G. Klupp, A. Karger, and T. C. Mettenleiter. 1997. Ultrastructural analysis of the replication cycle of pseudorabies virus in cell culture: a reassessment. J. Virol. 71:2072-2082.
    • (1997) J. Virol. , vol.71 , pp. 2072-2082
    • Granzow, H.1    Weiland, F.2    Jons, A.3    Klupp, B.G.4    Karger, A.5    Mettenleiter, T.C.6
  • 18
    • 0037369083 scopus 로고    scopus 로고
    • Envelopment of human cytomegalovirus occurs by budding into Golgi-derived vacuole compartments positive for gB, Rab 3, trans-Golgi network 46, and mannosidase II
    • Erratum, 77:8179
    • Homman-Loudiyi, M., K. Hultenby, W. Britt, and C. Soderberg-Naucler. 2003. Envelopment of human cytomegalovirus occurs by budding into Golgi-derived vacuole compartments positive for gB, Rab 3, trans-Golgi network 46, and mannosidase II. J. Virol. 77:3191-3203. (Erratum, 77:8179.)
    • (2003) J. Virol. , vol.77 , pp. 3191-3203
    • Homman-Loudiyi, M.1    Hultenby, K.2    Britt, W.3    Soderberg-Naucler, C.4
  • 19
    • 0030965051 scopus 로고    scopus 로고
    • Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy
    • Kanaseki, T., K. Kawasaki, M. Murata, Y. Ikeuchi, and S. Ohnishi. 1997. Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy. J. Cell Biol. 137: 1041-1056.
    • (1997) J. Cell Biol. , vol.137 , pp. 1041-1056
    • Kanaseki, T.1    Kawasaki, K.2    Murata, M.3    Ikeuchi, Y.4    Ohnishi, S.5
  • 20
    • 0031935889 scopus 로고    scopus 로고
    • Pseudorabies virus glycoprotein gK is a virion structural component involved in virus release but is not required for entry
    • Klupp, B. G., J. Baumeister, P. Dietz, H. Granzow, and T. C. Mettenleiter. 1998. Pseudorabies virus glycoprotein gK is a virion structural component involved in virus release but is not required for entry. J. Virol. 72:1949-1958.
    • (1998) J. Virol. , vol.72 , pp. 1949-1958
    • Klupp, B.G.1    Baumeister, J.2    Dietz, P.3    Granzow, H.4    Mettenleiter, T.C.5
  • 21
    • 0036841175 scopus 로고    scopus 로고
    • Lipid intermediates in membrane fusion: Formation, structure, and decay of hemifusion diaphragm
    • Kozlovsky, Y., L. V. Chernomordik, and M. M. Kozlov. 2002. Lipid intermediates in membrane fusion: formation, structure, and decay of hemifusion diaphragm. Biophys. J. 83:2634-2651.
    • (2002) Biophys. J. , vol.83 , pp. 2634-2651
    • Kozlovsky, Y.1    Chernomordik, L.V.2    Kozlov, M.M.3
  • 22
    • 0015691737 scopus 로고
    • Mechanism of envelopment of herpesvirus by the nucelar envelope
    • Lecatsas, G., and G. Poste. 1973. Mechanism of envelopment of herpesvirus by the nucelar envelope. Onderstepoort J. Vet. Res. 40:71-72.
    • (1973) Onderstepoort J. Vet. Res. , vol.40 , pp. 71-72
    • Lecatsas, G.1    Poste, G.2
  • 23
    • 0024148804 scopus 로고
    • Visualization of glycoproteins after tunicamycin and monensin treatment of herpes simplex virus infected cells
    • Lopez-Iglesias, C., and F. Puvion-Dutilleul. 1988. Visualization of glycoproteins after tunicamycin and monensin treatment of herpes simplex virus infected cells. J. Ultrastruct. Mol. Struct. Res. 101:75-91.
    • (1988) J. Ultrastruct. Mol. Struct. Res. , vol.101 , pp. 75-91
    • Lopez-Iglesias, C.1    Puvion-Dutilleul, F.2
  • 24
    • 0023772685 scopus 로고
    • Herpes simplex virus infection of the human sensory neuron. An electron microscopy study
    • Lycke, E., B. Hamark, M. Johansson, A. Krotochwil, J. Lycke, and B. Svennerholm. 1988. Herpes simplex virus infection of the human sensory neuron. An electron microscopy study. Arch. Virol. 101:87-104.
    • (1988) Arch. Virol. , vol.101 , pp. 87-104
    • Lycke, E.1    Hamark, B.2    Johansson, M.3    Krotochwil, A.4    Lycke, J.5    Svennerholm, B.6
  • 25
    • 0036929660 scopus 로고    scopus 로고
    • Structure and energy of fusion stalks: The role of membrane edges
    • May, S. 2002. Structure and energy of fusion stalks: the role of membrane edges. Biophys. J. 83:2969-2980.
    • (2002) Biophys. J. , vol.83 , pp. 2969-2980
    • May, S.1
  • 26
    • 0030776258 scopus 로고    scopus 로고
    • Membrane rearrangements in fusion mediated by viral proteins
    • Melikyan, G. B., and L. V. Chernomordik. 1997. Membrane rearrangements in fusion mediated by viral proteins. Trends Microbiol. 5:349-355.
    • (1997) Trends Microbiol. , vol.5 , pp. 349-355
    • Melikyan, G.B.1    Chernomordik, L.V.2
  • 27
    • 0022653027 scopus 로고
    • Bovine herpesvirus 1: Molecular and antigenic characteristics of variant viruses isolated from calves with neurological disease
    • Metzler, A. E., A. A. Schudel, and M. Engels. 1986. Bovine herpesvirus 1: molecular and antigenic characteristics of variant viruses isolated from calves with neurological disease. Arch. Virol. 87:205-217.
    • (1986) Arch. Virol. , vol.87 , pp. 205-217
    • Metzler, A.E.1    Schudel, A.A.2    Engels, M.3
  • 28
    • 0024297309 scopus 로고
    • Nanomelic chondrocytes synthesize a glycoprotein related to chondroitin sulfate proteoglycan core protein
    • O'Donnell, C. M., K. Kaczman-Daniel, P. F. Goetinck, and B. M. Vertel. 1988. Nanomelic chondrocytes synthesize a glycoprotein related to chondroitin sulfate proteoglycan core protein. J. Biol. Chem. 263:17749-17754.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17749-17754
    • O'Donnell, C.M.1    Kaczman-Daniel, K.2    Goetinck, P.F.3    Vertel, B.M.4
  • 29
    • 0029922169 scopus 로고    scopus 로고
    • Molecular dissection of the nuclear pore complex
    • Pante, N., and U. Aebi. 1996. Molecular dissection of the nuclear pore complex. Crit. Rev. Biochem. Mol. Biol. 31:153-199.
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 153-199
    • Pante, N.1    Aebi, U.2
  • 30
    • 0025868634 scopus 로고
    • Morphogenesis of three pseudorabies virus strains in porcine nasal mucosa
    • Pol, J. M., F. Wagenaar, and A. Gielkens. 1991. Morphogenesis of three pseudorabies virus strains in porcine nasal mucosa. Intervirology 32:327-337.
    • (1991) Intervirology , vol.32 , pp. 327-337
    • Pol, J.M.1    Wagenaar, F.2    Gielkens, A.3
  • 31
    • 0029690315 scopus 로고    scopus 로고
    • Retrieval of human cytomegalovirus glycoprotein B from the infected cell surface for virus envelopment
    • Radsak, K., M. Eickmann, T. Mockenhaupt, E. Bogner, H. Kern, A. Eis-Hubinger, and M. Reschke. 1996. Retrieval of human cytomegalovirus glycoprotein B from the infected cell surface for virus envelopment. Arch. Virol. 141:557-572.
    • (1996) Arch. Virol. , vol.141 , pp. 557-572
    • Radsak, K.1    Eickmann, M.2    Mockenhaupt, T.3    Bogner, E.4    Kern, H.5    Eis-Hubinger, A.6    Reschke, M.7
  • 32
    • 0001315638 scopus 로고
    • Structure and assembly of herpesviruses
    • Rixon, F. J. 1993. Structure and assembly of herpesviruses. Semin. Virol. 4: 135-144.
    • (1993) Semin. Virol. , vol.4 , pp. 135-144
    • Rixon, F.J.1
  • 34
    • 0014515438 scopus 로고
    • Concerning the egress of herpes simplex virus from infected cells: Electron and light microscope observations
    • Schwartz, J., and B. Roizman. 1969. Concerning the egress of herpes simplex virus from infected cells: electron and light microscope observations. Virology 38:42-49.
    • (1969) Virology , vol.38 , pp. 42-49
    • Schwartz, J.1    Roizman, B.2
  • 36
    • 11144242611 scopus 로고    scopus 로고
    • Cloning of BoHV-1genome as a BAC and amplication-mediated creation of mutagenized BoHV-1
    • Cairns, Australia
    • Tobler, K., C. Fraefel, and M. Ackermann. 2002. Cloning of BoHV-1genome as a BAC and amplication-mediated creation of mutagenized BoHV-1, abstr. 5.26. 27th International Herpesvirus Workshop, Cairns, Australia.
    • (2002) 27th International Herpesvirus Workshop
    • Tobler, K.1    Fraefel, C.2    Ackermann, M.3
  • 38
    • 2642653226 scopus 로고    scopus 로고
    • Double-layer coating for field-emission cryo-scanning electron microscopy-present state and applications
    • Walther, P., and M. Müller. 1997. Double-layer coating for field-emission cryo-scanning electron microscopy-present state and applications. Scanning 19:343-348.
    • (1997) Scanning , vol.19 , pp. 343-348
    • Walther, P.1    Müller, M.2
  • 39
    • 0028808195 scopus 로고
    • Double-layer coating for high-resolution low-temperature scanning electron microscopy
    • Walther, P., E. Wehrli, R. Hermann, and M. Müller. 1995. Double-layer coating for high-resolution low-temperature scanning electron microscopy. J. Microsc. 179:229-237.
    • (1995) J. Microsc. , vol.179 , pp. 229-237
    • Walther, P.1    Wehrli, E.2    Hermann, R.3    Müller, M.4
  • 40
    • 0034747789 scopus 로고    scopus 로고
    • Essential role played by the C-terminal domain of glycoprotein I in envelopment of varicella-zoster virus in the trans-Golgi network: Interactions of glycoproteins with tegument
    • Wang, Z. H., M. D. Gershon, O. Lungu, Z. L. Zhu, S. Mallory, A. M. Arvin, and A. A. Gershon. 2001. Essential role played by the C-terminal domain of glycoprotein I in envelopment of varicella-zoster virus in the trans-Golgi network: interactions of glycoproteins with tegument. J. Virol. 75:323-340.
    • (2001) J. Virol. , vol.75 , pp. 323-340
    • Wang, Z.H.1    Gershon, M.D.2    Lungu, O.3    Zhu, Z.L.4    Mallory, S.5    Arvin, A.M.6    Gershon, A.A.7
  • 41
    • 0022534222 scopus 로고
    • Extraction of proteins and membrane lipids during low temperature embedding of biological material for electron microscopy
    • Weibull, C., and A. Christiansson. 1986. Extraction of proteins and membrane lipids during low temperature embedding of biological material for electron microscopy. J. Microsc. 142:79-86.
    • (1986) J. Microsc. , vol.142 , pp. 79-86
    • Weibull, C.1    Christiansson, A.2
  • 42
    • 0026083301 scopus 로고
    • Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress
    • Whealy, M. E., J. P. Card, R. P. Meade, A. K. Robbins, and L. W. Enquist. 1991. Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress. J. Virol. 65:1066-1081.
    • (1991) J. Virol. , vol.65 , pp. 1066-1081
    • Whealy, M.E.1    Card, J.P.2    Meade, R.P.3    Robbins, A.K.4    Enquist, L.W.5
  • 43
    • 0036005952 scopus 로고    scopus 로고
    • The significance of the Golgi complex in envelopment of bovine herpesvirus 1 (BHV-1) as revealed by cryobased electron microscopy
    • Wild, P., E. M. Schraner, D. Cantieni, E. Loepfe, P. Walther, M. Muller, and M. Engels. 2002. The significance of the Golgi complex in envelopment of bovine herpesvirus 1 (BHV-1) as revealed by cryobased electron microscopy. Micron 33:327-337.
    • (2002) Micron , vol.33 , pp. 327-337
    • Wild, P.1    Schraner, E.M.2    Cantieni, D.3    Loepfe, E.4    Walther, P.5    Muller, M.6    Engels, M.7
  • 44
    • 0035873242 scopus 로고    scopus 로고
    • Enhanced resolution of membranes in cultured cells by cryoimmobilization and freeze-substitution
    • Wild, P., E. M. Schraner, H. Adler, and B. M. Humbel. 2001. Enhanced resolution of membranes in cultured cells by cryoimmobilization and freeze-substitution. Microsc. Res. Tech. 53:313-321.
    • (2001) Microsc. Res. Tech. , vol.53 , pp. 313-321
    • Wild, P.1    Schraner, E.M.2    Adler, H.3    Humbel, B.M.4
  • 45
    • 0345471494 scopus 로고    scopus 로고
    • Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions
    • Zhou, Z. H., D. H. Chen, J. Jakana, F. J. Rixon, and W. Chiu. 1999. Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions. J. Virol. 73:3210-3218.
    • (1999) J. Virol. , vol.73 , pp. 3210-3218
    • Zhou, Z.H.1    Chen, D.H.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5
  • 46
    • 0028971193 scopus 로고
    • Envelopment of varicella-zoster virus: Targeting of viral glycoproteins to the trans-Golgi network
    • Zhu, Z., M. D. Gershon, Y. Hao, R. T. Ambron, C. A. Gabel, and A. A. Gershon. 1995. Envelopment of varicella-zoster virus: targeting of viral glycoproteins to the trans-Golgi network. J. Virol. 69:7951-7959.
    • (1995) J. Virol. , vol.69 , pp. 7951-7959
    • Zhu, Z.1    Gershon, M.D.2    Hao, Y.3    Ambron, R.T.4    Gabel, C.A.5    Gershon, A.A.6


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