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Volumn 130, Issue 1-2, 2008, Pages 47-59

African swine fever virus p10 protein exhibits nuclear import capacity and accumulates in the nucleus during viral infection

Author keywords

African swine fever virus; Nuclear import; p10 protein

Indexed keywords

PROTEIN P10;

EID: 46549086170     PISSN: 03781135     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetmic.2007.12.010     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 1842292789 scopus 로고    scopus 로고
    • Assembly of African swine fever virus: role of polyprotein pp220
    • Andrés G., Símon-Mateo C., and Viñuela E. Assembly of African swine fever virus: role of polyprotein pp220. J. Virol. 71 (1997) 2332-2341
    • (1997) J. Virol. , vol.71 , pp. 2332-2341
    • Andrés, G.1    Símon-Mateo, C.2    Viñuela, E.3
  • 2
    • 0031711867 scopus 로고    scopus 로고
    • African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum
    • Andrés G., García-Escudero R., Simón-Mateo C., and Viñuela E. African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum. J. Virol. 72 (1998) 8988-9001
    • (1998) J. Virol. , vol.72 , pp. 8988-9001
    • Andrés, G.1    García-Escudero, R.2    Simón-Mateo, C.3    Viñuela, E.4
  • 3
    • 0034947805 scopus 로고    scopus 로고
    • African swine fever virus structural protein pE120R is essential for virus transport from assembly sites to plasma membrane but not for infectivity
    • Andrés G., García-Escudero R., Viñuela E., Salas M.L., and Rodriguez J.M. African swine fever virus structural protein pE120R is essential for virus transport from assembly sites to plasma membrane but not for infectivity. J. Virol. 75 (2001) 6758-6768
    • (2001) J. Virol. , vol.75 , pp. 6758-6768
    • Andrés, G.1    García-Escudero, R.2    Viñuela, E.3    Salas, M.L.4    Rodriguez, J.M.5
  • 4
    • 0036187961 scopus 로고    scopus 로고
    • Repression of African swine fever virus polyprotein pp220-encoding gene leads to the assembly of icosahedral core-less particles
    • Andrés G., García-Escudero R., Salas M.L., and Rodriguez J.M. Repression of African swine fever virus polyprotein pp220-encoding gene leads to the assembly of icosahedral core-less particles. J. Virol. 76 (2002) 2654-2666
    • (2002) J. Virol. , vol.76 , pp. 2654-2666
    • Andrés, G.1    García-Escudero, R.2    Salas, M.L.3    Rodriguez, J.M.4
  • 5
    • 0035050656 scopus 로고    scopus 로고
    • Characterisation of nuclear localisation signals of the four human core histones
    • Baake M., Doenecke D., and Albig W. Characterisation of nuclear localisation signals of the four human core histones. J. Cell. Biochem. 81 (2001) 333-346
    • (2001) J. Cell. Biochem. , vol.81 , pp. 333-346
    • Baake, M.1    Doenecke, D.2    Albig, W.3
  • 7
    • 0017891963 scopus 로고
    • Electron microscopic observation of African swine fever virus development in Vero cells
    • Breese Jr. S.S., and Pan I.C. Electron microscopic observation of African swine fever virus development in Vero cells. J. Gen. Virol. 40 (1978) 499-502
    • (1978) J. Gen. Virol. , vol.40 , pp. 499-502
    • Breese Jr., S.S.1    Pan, I.C.2
  • 8
    • 0033119241 scopus 로고    scopus 로고
    • Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor
    • Brock R., Hamelers I.H.L., and Jovin T.M. Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor. Cytometry 35 (1999) 353-362
    • (1999) Cytometry , vol.35 , pp. 353-362
    • Brock, R.1    Hamelers, I.H.L.2    Jovin, T.M.3
  • 11
    • 0026456803 scopus 로고
    • Expression in vivo and in vitro of the major structural protein (VP73) of African swine fever virus
    • Cistué C., and Tabarés E. Expression in vivo and in vitro of the major structural protein (VP73) of African swine fever virus. Arch. Virol. 123 (1992) 111-124
    • (1992) Arch. Virol. , vol.123 , pp. 111-124
    • Cistué, C.1    Tabarés, E.2
  • 12
    • 0028325748 scopus 로고
    • Nuclear import of Agrobacterium VirD2 and VirE2 proteins in maize and tobacco
    • Citovsky V., Warnick D., and Zambrysky P. Nuclear import of Agrobacterium VirD2 and VirE2 proteins in maize and tobacco. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 3210-3214
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 3210-3214
    • Citovsky, V.1    Warnick, D.2    Zambrysky, P.3
  • 13
    • 0024077328 scopus 로고
    • The nucleoplasmin nuclear location sequence is larger and more complex than that of SV-40 large T antigen
    • Dingwall C., Robbins J., Dilworth S.M., Roberts B., and Richardson W.D. The nucleoplasmin nuclear location sequence is larger and more complex than that of SV-40 large T antigen. J. Cell. Biol. 107 (1988) 841-849
    • (1988) J. Cell. Biol. , vol.107 , pp. 841-849
    • Dingwall, C.1    Robbins, J.2    Dilworth, S.M.3    Roberts, B.4    Richardson, W.D.5
  • 14
    • 0025949412 scopus 로고
    • Nuclear targeting sequences-a consensus?
    • Dingwall C., and Laskey R.A. Nuclear targeting sequences-a consensus?. Trends Biochem. Sci. 16 (1991) 478-481
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 16
    • 4444281591 scopus 로고    scopus 로고
    • Two African swine fever virus proteins derived from a common precursor exhibit different nucleo-cytoplasmic transport activities
    • Eulálio A., Nunes-Correia I., Carvalho A.L., Faro C., Citovsky V., Simões S., and Pedroso de Lima M.C. Two African swine fever virus proteins derived from a common precursor exhibit different nucleo-cytoplasmic transport activities. J. Virol. 78 (2004) 9731-9739
    • (2004) J. Virol. , vol.78 , pp. 9731-9739
    • Eulálio, A.1    Nunes-Correia, I.2    Carvalho, A.L.3    Faro, C.4    Citovsky, V.5    Simões, S.6    Pedroso de Lima, M.C.7
  • 17
    • 0026708727 scopus 로고
    • Role of the host cell nucleus in the replication of African swine fever virus DNA
    • García-Beato R., Salas M.L., Viñuela E., and Salas J. Role of the host cell nucleus in the replication of African swine fever virus DNA. Virology 188 (1992) 637-649
    • (1992) Virology , vol.188 , pp. 637-649
    • García-Beato, R.1    Salas, M.L.2    Viñuela, E.3    Salas, J.4
  • 19
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Görlich D., and Kutay U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15 (1999) 607-660
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 20
    • 0030099238 scopus 로고    scopus 로고
    • Transport of DNA into the nuclei of Xenopus oocytes by a modified VirE2 protein of Agrobacterium
    • Guralnick B., Thomsen G., and Citovsky V. Transport of DNA into the nuclei of Xenopus oocytes by a modified VirE2 protein of Agrobacterium. Plant Cell 8 (1996) 363-373
    • (1996) Plant Cell , vol.8 , pp. 363-373
    • Guralnick, B.1    Thomsen, G.2    Citovsky, V.3
  • 22
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • Hollenberg S.M., Sternglanz R., Cheng P.F., and Weintraub H. Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15 (1995) 3813-3822
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 24
    • 0021269089 scopus 로고
    • Sequence requirements for nuclear location of simian virus 40 large-T antigen
    • Kalderón D., Richardson W.D., Markham A.F., and Smith A.E. Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature 311 (1984) 33-38
    • (1984) Nature , vol.311 , pp. 33-38
    • Kalderón, D.1    Richardson, W.D.2    Markham, A.F.3    Smith, A.E.4
  • 25
    • 0035115758 scopus 로고    scopus 로고
    • The non-haemadsorbing African swine fever virus isolate ASFV/NH/P68 provides a model for defining the protective anti-virus immune response
    • Leitão A., Cartaxeiro C., Coelho R., Cruz B., Parkhouse R.M.E., Portugal F.C., Vigário J.D., and Martins C.L.V. The non-haemadsorbing African swine fever virus isolate ASFV/NH/P68 provides a model for defining the protective anti-virus immune response. J. Gen. Virol. 82 (2001) 513-523
    • (2001) J. Gen. Virol. , vol.82 , pp. 513-523
    • Leitão, A.1    Cartaxeiro, C.2    Coelho, R.3    Cruz, B.4    Parkhouse, R.M.E.5    Portugal, F.C.6    Vigário, J.D.7    Martins, C.L.V.8
  • 26
    • 0023376779 scopus 로고
    • Pentapeptide nuclear localization signal in adenovirus E1a
    • Lyons R.H., Ferguson B.Q., and Rosenberg M. Pentapeptide nuclear localization signal in adenovirus E1a. Mol. Cell. Biol. 7 (1987) 2451-2456
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2451-2456
    • Lyons, R.H.1    Ferguson, B.Q.2    Rosenberg, M.3
  • 27
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara I.G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65 (2001) 570-594
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 28
    • 0030221192 scopus 로고    scopus 로고
    • Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids
    • Makkerh J.P., Dingwall C., and Laskey R.A. Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids. Curr. Biol. 6 (1996) 1025-1027
    • (1996) Curr. Biol. , vol.6 , pp. 1025-1027
    • Makkerh, J.P.1    Dingwall, C.2    Laskey, R.A.3
  • 29
    • 0030978415 scopus 로고    scopus 로고
    • The K nuclear shuttling doma: a novel signal for nuclear import nuclear export in the hnRNP K protein
    • Michael W.M., Eder P.S., and Dreyfuss G. The K nuclear shuttling doma: a novel signal for nuclear import nuclear export in the hnRNP K protein. EMBO J. 16 (1997) 3587-3598
    • (1997) EMBO J. , vol.16 , pp. 3587-3598
    • Michael, W.M.1    Eder, P.S.2    Dreyfuss, G.3
  • 30
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller J.H. Experiments in Molecular Genetics (1972), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 32
    • 0027357948 scopus 로고
    • Structure and expression in E. coli of the gene coding for protein p10 of African swine fever virus
    • Muñoz M., Freije J.M., Salas M.L., Viñuela E., and López-Otin C. Structure and expression in E. coli of the gene coding for protein p10 of African swine fever virus. Arch. Virol. 130 (1993) 93-107
    • (1993) Arch. Virol. , vol.130 , pp. 93-107
    • Muñoz, M.1    Freije, J.M.2    Salas, M.L.3    Viñuela, E.4    López-Otin, C.5
  • 33
    • 0017357099 scopus 로고
    • Requirement of cell nucleus for African swine fever virus replication in Vero cells
    • Ortin J., and Viñuela E. Requirement of cell nucleus for African swine fever virus replication in Vero cells. J. Virol. 21 (1977) 902-905
    • (1977) J. Virol. , vol.21 , pp. 902-905
    • Ortin, J.1    Viñuela, E.2
  • 34
    • 0026582064 scopus 로고
    • Sequential paraformaldehyde and methanol fixation for simultaneous flow cytometric analysis of DNA, cell surface proteins, and intracellular proteins
    • Pollice A., McCoy J., Shackney S., Smith C., Agarwal J., Burholt D., Janocko L., Hornicek F., Singh S., and Hartsock R. Sequential paraformaldehyde and methanol fixation for simultaneous flow cytometric analysis of DNA, cell surface proteins, and intracellular proteins. Cytometry 13 (1992) 432-444
    • (1992) Cytometry , vol.13 , pp. 432-444
    • Pollice, A.1    McCoy, J.2    Shackney, S.3    Smith, C.4    Agarwal, J.5    Burholt, D.6    Janocko, L.7    Hornicek, F.8    Singh, S.9    Hartsock, R.10
  • 35
    • 0034005718 scopus 로고    scopus 로고
    • A genetic system for detection of protein nuclear import and export
    • Rhee Y., Gurel F., Gafni Y., Dingwall C., and Citovsky V. A genetic system for detection of protein nuclear import and export. Nat. Biotechnol. 18 (2000) 433-437
    • (2000) Nat. Biotechnol. , vol.18 , pp. 433-437
    • Rhee, Y.1    Gurel, F.2    Gafni, Y.3    Dingwall, C.4    Citovsky, V.5
  • 36
    • 0345062265 scopus 로고    scopus 로고
    • Replication of African swine fever virus DNA in infected cells
    • Rojo G., Garcia-Beato R., Viñuela E., Salas M.L., and Salas J. Replication of African swine fever virus DNA in infected cells. Virology 257 (1999) 524-536
    • (1999) Virology , vol.257 , pp. 524-536
    • Rojo, G.1    Garcia-Beato, R.2    Viñuela, E.3    Salas, M.L.4    Salas, J.5
  • 37
    • 0002300485 scopus 로고    scopus 로고
    • African swine fever virus: a missing link between poxviruses and iridoviruses
    • Domingo E., Webster R., and Holland J. (Eds), Academic Press, Inc., New York
    • Salas J., Salas M.L., and Viñuela E. African swine fever virus: a missing link between poxviruses and iridoviruses. In: Domingo E., Webster R., and Holland J. (Eds). Origin and Evolution of Viruses (1999), Academic Press, Inc., New York 467-480
    • (1999) Origin and Evolution of Viruses , pp. 467-480
    • Salas, J.1    Salas, M.L.2    Viñuela, E.3
  • 38
  • 39
    • 0022054094 scopus 로고
    • A Tn3 lacZ transposon for the random generation of β-galactosidase gene fusions: application to the analysis of gene expression in Agrobacterium
    • Stachel S.E., An G., Flores C., and Nester E.W. A Tn3 lacZ transposon for the random generation of β-galactosidase gene fusions: application to the analysis of gene expression in Agrobacterium. EMBO J. 4 (1985) 891-898
    • (1985) EMBO J. , vol.4 , pp. 891-898
    • Stachel, S.E.1    An, G.2    Flores, C.3    Nester, E.W.4
  • 40
    • 1542350594 scopus 로고    scopus 로고
    • Immuno-localization of Fas and FasL in rat hepatic endothelial cells: influence of different fixation protocols
    • Vekemans K., Rosseel L., Wisse E., and Braet F. Immuno-localization of Fas and FasL in rat hepatic endothelial cells: influence of different fixation protocols. Micron 35 (2004) 303-306
    • (2004) Micron , vol.35 , pp. 303-306
    • Vekemans, K.1    Rosseel, L.2    Wisse, E.3    Braet, F.4
  • 41
    • 0032551236 scopus 로고    scopus 로고
    • Nuclear import and export of viruses and virus genomes
    • Whittaker G.R., and Helenius A. Nuclear import and export of viruses and virus genomes. Virology 246 (1998) 1-23
    • (1998) Virology , vol.246 , pp. 1-23
    • Whittaker, G.R.1    Helenius, A.2


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