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Journal of Virology
Volumn 77, Issue 10, 2003, Pages 5571-5577
African swine fever virus proteinase is essential for core maturation and infectivity
Author keywords

[No Author keywords available]
Indexed keywords

DNA BINDING PROTEIN; POLYPROTEIN; PROTEIN P10; PROTEIN PA104R; PROTEIN PP220; PROTEIN PP62; PROTEINASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;
EID: 0038033169     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.10.5571-5577.2003     Document Type: Article
Times cited : (41)
References (49)
  • 1
    • 0025291078 scopus 로고
    • The proteinase polypeptide of adenovirus serotype 2 virions
    • Anderson, C. W. 1990. The proteinase polypeptide of adenovirus serotype 2 virions. Virology 177:259-272.
    • (1990) Virology , vol.177 , pp. 259-272
    • Anderson, C.W.1
  • 2
    • 1842292789 scopus 로고    scopus 로고
    • Assembly of African swine fever virus: Role of polyprotein pp220
    • Andrés, G., C. Simón-Mateo, and E. Viñuela. 1997. Assembly of African swine fever virus: role of polyprotein pp220. J. Virol. 71:2331-2341.
    • (1997) J. Virol. , vol.71 , pp. 2331-2341
    • Andrés, G.1    Simón-Mateo, C.2    Viñuela, E.3
  • 3
    • 0031711867 scopus 로고    scopus 로고
    • African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum
    • Andrés, G., R. García-Escudero, C. Simón-Mateo, and E. Viñuela. 1998. African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum. J. Virol. 72:8988-9001.
    • (1998) J. Virol. , vol.72 , pp. 8988-9001
    • Andrés, G.1    García-Escudero, R.2    Simón-Mateo, C.3    Viñuela, E.4
  • 4
    • 0035808469 scopus 로고    scopus 로고
    • African swine fever virus protease, a new viral member of the SUMO-1-specific protease family
    • Andrés, G., A. Alejo, C. Simón-Mateo, and M. L. Salas. 2001. African swine fever virus protease, a new viral member of the SUMO-1-specific protease family. J. Biol. Chem. 276:780-787.
    • (2001) J. Biol. Chem. , vol.276 , pp. 780-787
    • Andrés, G.1    Alejo, A.2    Simón-Mateo, C.3    Salas, M.L.4
  • 5
    • 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., R. García-Escudero, E. Viñuela, M. L. Salas, and J. M. Rodríguez. 2001. 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: 6758-6768.
    • (2001) J. Virol. , vol.75 , pp. 6758-6768
    • Andrés, G.1    García-Escudero, R.2    Viñuela, E.3    Salas, M.L.4    Rodríguez, J.M.5
  • 6
    • 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., R. García-Escudero, M. L. Salas, and J. M. Rodríguez, 2002. Repression of African swine fever virus polyprotein pp220-encoding gene leads to the assembly of icosahedral core-less particles. J. Virol. 76:2654-2666.
    • (2002) J. Virol. , vol.76 , pp. 2654-2666
    • Andrés, G.1    García-Escudero, R.2    Salas, M.L.3    Rodríguez, J.M.4
  • 7
    • 0036891835 scopus 로고    scopus 로고
    • African swine fever virus polyproteins pp220 and pp62 assemble into the core shell
    • Andrés, G., A. Alejo, J. Salas, and M. L. Salas. 2002. African swine fever virus polyproteins pp220 and pp62 assemble into the core shell. J. Virol. 76:12473-12482.
    • (2002) J. Virol. , vol.76 , pp. 12473-12482
    • Andrés, G.1    Alejo, A.2    Salas, J.3    Salas, M.L.4
  • 8
    • 0019460091 scopus 로고
    • Variants of a cloned synthetic operator. I. A palindromic dimer lactose operator derived from one strand of the cloned 40-base-pair operator
    • Betz, J. L., and J. R. Sadler. 1981. Variants of a cloned synthetic operator. I. A palindromic dimer lactose operator derived from one strand of the cloned 40-base-pair operator. Gene 13:1-12.
    • (1981) Gene , vol.13 , pp. 1-12
    • Betz, J.L.1    Sadler, J.R.2
  • 9
    • 0001007022 scopus 로고
    • Electron microscope observation of African swine fever virus in tissue culture cells
    • Breese, S. S., Jr., and C. J. DeBoer. 1966. Electron microscope observation of African swine fever virus in tissue culture cells. Virology 28: 420-428.
    • (1966) Virology , vol.28 , pp. 420-428
    • Breese S.S., Jr.1    DeBoer, C.J.2
  • 10
    • 0032530497 scopus 로고    scopus 로고
    • Intracellular virus DNA distribution and the acquisition of the nucleoprotein core during African swine fever virus particle assembly: Ultrastructural in situ hybridisation and DNase-gold labelling
    • Brookes, S. M., A. D. Hyatt, T. Wise, and R. M. Parkhouse. 1998. Intracellular virus DNA distribution and the acquisition of the nucleoprotein core during African swine fever virus particle assembly: ultrastructural in situ hybridisation and DNase-gold labelling. Virology 249:175-188.
    • (1998) Virology , vol.249 , pp. 175-188
    • Brookes, S.M.1    Hyatt, A.D.2    Wise, T.3    Parkhouse, R.M.4
  • 11
    • 0036338018 scopus 로고    scopus 로고
    • The vaccinia virus 17L gene product is the core protein proteinase
    • Byrd, C. M., T. C. Bolken, and D. E. Hruby. 2002. The vaccinia virus 17L gene product is the core protein proteinase. J. Virol. 76:8973-8976.
    • (2002) J. Virol. , vol.76 , pp. 8973-8976
    • Byrd, C.M.1    Bolken, T.C.2    Hruby, D.E.3
  • 12
  • 13
    • 0024083511 scopus 로고
    • Association of African swine fever virus with the cytoskeleton
    • Carvalho, Z. G., A. P. De Matos, and C. Rodrigues-Pousada. 1988. Association of African swine fever virus with the cytoskeleton. Virus Res. 11:175-192.
    • (1988) Virus Res. , vol.11 , pp. 175-192
    • Carvalho, Z.G.1    De Matos, A.P.2    Rodrigues-Pousada, C.3
  • 14
    • 0033981656 scopus 로고    scopus 로고
    • Biochemical requirements of virus wrapping by the endoplasmic reticulum: Involvement of ATP and endoplasmic reticulum calcium store during envelopment of African swine fever virus
    • Cobbold, C., S. M. Brookes, and T. Wileman. 2000. Biochemical requirements of virus wrapping by the endoplasmic reticulum: involvement of ATP and endoplasmic reticulum calcium store during envelopment of African swine fever virus. J. Virol. 74:2151-2160.
    • (2000) J. Virol. , vol.74 , pp. 2151-2160
    • Cobbold, C.1    Brookes, S.M.2    Wileman, T.3
  • 15
    • 0019602923 scopus 로고
    • Isolation and preliminary characterization of temperature-sensitive mutants of vaccinia virus
    • Condit, R. C., and A. Motyczka. 1981. Isolation and preliminary characterization of temperature-sensitive mutants of vaccinia virus. Virology 113:224-241.
    • (1981) Virology , vol.113 , pp. 224-241
    • Condit, R.C.1    Motyczka, A.2
  • 16
    • 0020572109 scopus 로고
    • Isolation, characterization, and physical mapping of temperature-sensitive mutants of vaccinia virus
    • Condit, R. C., A. Motyczka, and G. Spizz. 1983. Isolation, characterization, and physical mapping of temperature-sensitive mutants of vaccinia virus. Virology 128: 429-443.
    • (1983) Virology , vol.128 , pp. 429-443
    • Condit, R.C.1    Motyczka, A.2    Spizz, G.3
  • 17
    • 0001672352 scopus 로고
    • African swine fever virus
    • G. Darai (ed.), Kluwer Academic Publishers, Boston, Mass
    • Costa, J. V. 1990. African swine fever virus, p. 247-270. In G. Darai (ed.), Molecular biology of iridoviruses. Kluwer Academic Publishers, Boston, Mass.
    • (1990) Molecular Biology of Iridoviruses , pp. 247-270
    • Costa, J.V.1
  • 18
    • 0027423988 scopus 로고
    • African swine fever virus interaction with microtubules
    • de Matos, A. P., and Z. G. Carvalho. 1993. African swine fever virus interaction with microtubules. Biol. Cell 78:229-234.
    • (1993) Biol. Cell , vol.78 , pp. 229-234
    • De Matos, A.P.1    Carvalho, Z.G.2
  • 20
    • 0027138172 scopus 로고
    • Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes
    • Dougherty, W. G., and B. L. Semler. 1993. Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes. Microbiol. Rev. 57:781-822.
    • (1993) Microbiol. Rev. , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 23
    • 0022445911 scopus 로고
    • Two-dimensional analysis of African swine fever virus proteins and proteins induced in infected cells
    • Esteves, A., M. I. Marques, and J. V. Costa. 1986. Two-dimensional analysis of African swine fever virus proteins and proteins induced in infected cells. Virology 152:192-206.
    • (1986) Virology , vol.152 , pp. 192-206
    • Esteves, A.1    Marques, M.I.2    Costa, J.V.3
  • 25
    • 0040984034 scopus 로고    scopus 로고
    • Inducible gene expression from African swine fever virus recombinants: Analysis of the major capsid protein p72
    • García-Escudero, R., G. Andrés, F. Almazán, and E. Viñuela. 1998. Inducible gene expression from African swine fever virus recombinants: analysis of the major capsid protein p72. J. Virol. 72:3185-3195.
    • (1998) J. Virol. , vol.72 , pp. 3185-3195
    • García-Escudero, R.1    Andrés, G.2    Almazán, F.3    Viñuela, E.4
  • 26
    • 0033900821 scopus 로고    scopus 로고
    • Structure of African swine fever virus late promoters: Requirement of a TATA sequence at the initiation region
    • García-Escudero, R., and E. Viñuela. 2000. Structure of African swine fever virus late promoters: requirement of a TATA sequence at the initiation region. J. Virol. 74:8176-8182.
    • (2000) J. Virol. , vol.74 , pp. 8176-8182
    • García-Escudero, R.1    Viñuela, E.2
  • 28
    • 0029983628 scopus 로고    scopus 로고
    • The role of the adenovirus proteinase on virus entry into cells
    • Greber, U. F., P. Webster, J. Weber, and A. Helenius. 1996. The role of the adenovirus proteinase on virus entry into cells. EMBO J. 15:1766-1777.
    • (1996) EMBO J. , vol.15 , pp. 1766-1777
    • Greber, U.F.1    Webster, P.2    Weber, J.3    Helenius, A.4
  • 29
    • 0035972239 scopus 로고    scopus 로고
    • Aggresomes resemble sites specialized for virus assembly
    • Heath, C. M., M. Windsor, and T. Wileman. 2001. Aggresomes resemble sites specialized for virus assembly. J. Cell Biol. 153: 449-455.
    • (2001) J. Cell Biol. , vol.153 , pp. 449-455
    • Heath, C.M.1    Windsor, M.2    Wileman, T.3
  • 30
    • 1842410751 scopus 로고    scopus 로고
    • Preferential modification of nuclear proteins by a novel ubiquitin-like molecule
    • Kamitani, T., H. P. Nguyen, and E. T. Yeh. 1997. Preferential modification of nuclear proteins by a novel ubiquitin-like molecule. J. Biol. Chem. 272: 14001-14004.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14001-14004
    • Kamitani, T.1    Nguyen, H.P.2    Yeh, E.T.3
  • 31
    • 0027456320 scopus 로고
    • Vaccinia virus morphogenesis is blocked by a temperature-sensitive mutation in the 17 gene that encodes a virion component
    • Kane, E. M., and S. Shuman. 1993. Vaccinia virus morphogenesis is blocked by a temperature-sensitive mutation in the 17 gene that encodes a virion component. J. Virol. 67:2689-2698.
    • (1993) J. Virol. , vol.67 , pp. 2689-2698
    • Kane, E.M.1    Shuman, S.2
  • 32
    • 0031980211 scopus 로고    scopus 로고
    • Role of matrix in an early postentry step in the human immunodeficiency virus type 1 life cycle
    • Kiernan, R. E., A. Ono, G. Englund, and E. O. Freed. 1998. Role of matrix in an early postentry step in the human immunodeficiency virus type 1 life cycle. J. Virol. 72:4116-4126.
    • (1998) J. Virol. , vol.72 , pp. 4116-4126
    • Kiernan, R.E.1    Ono, A.2    Englund, G.3    Freed, E.O.4
  • 34
    • 0033965481 scopus 로고    scopus 로고
    • An African swine fever virus ERV1-ALR homologue, 9GL, affects virion maturation and viral growth in macrophages and viral virulence in swine
    • Lewis, T., L. Zsak, T. G. Burrage, Z. Lu, G. F. Kutish, J. G. Neilan, and D. L. Rock. 2000. An African swine fever virus ERV1-ALR homologue, 9GL, affects virion maturation and viral growth in macrophages and viral virulence in swine. J. Virol. 74: 1275-1285.
    • (2000) J. Virol. , vol.74 , pp. 1275-1285
    • Lewis, T.1    Zsak, L.2    Burrage, T.G.3    Lu, Z.4    Kutish, G.F.5    Neilan, J.G.6    Rock, D.L.7
  • 35
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell cycle progression in yeast
    • Li, S.-J., and M. Hochstrasser. 1999. A new protease required for cell cycle progression in yeast. Nature 398:246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 36
    • 0026544596 scopus 로고
    • Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast
    • Lisowski, T. 1992. Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast. Mol. Gen. Genet. 232:58-64.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 58-64
    • Lisowski, T.1
  • 37
    • 0024383385 scopus 로고
    • Gly-Gly-X, a novel consensus sequence for the proteolytic processing of viral and cellular proteins
    • López-Otín, C., C. Simón-Mateo, L. Martínez, and E. Viñuela. 1989. Gly-Gly-X, a novel consensus sequence for the proteolytic processing of viral and cellular proteins. J. Biol. Chem. 264:9107-9110.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9107-9110
    • López-Otín, C.1    Simón-Mateo, C.2    Martínez, L.3    Viñuela, E.4
  • 38
    • 0026642465 scopus 로고
    • Genetic manipulation of African swine fever virus: Construction of recombinant viruses expressing the β-galactosidase gene
    • Rodríguez, J. M., F. Almazán, E. Viñuela, and J. F. Rodríguez. 1992. Genetic manipulation of African swine fever virus: construction of recombinant viruses expressing the β-galactosidase gene. Virology 188:67-76.
    • (1992) Virology , vol.188 , pp. 67-76
    • Rodríguez, J.M.1    Almazán, F.2    Viñuela, E.3    Rodríguez, J.F.4
  • 39
    • 0031816806 scopus 로고    scopus 로고
    • Migration of mitochondria to viral assembly sites in African swine fever virus-infected cells
    • Rojo, G., M. Chamorro, M. L. Salas, E. Viñuela, J. M. Cuezva, and J. Salas. 1998. Migration of mitochondria to viral assembly sites in African swine fever virus-infected cells. J. Virol. 72:7583-7588.
    • (1998) J. Virol. , vol.72 , pp. 7583-7588
    • Rojo, G.1    Chamorro, M.2    Salas, M.L.3    Viñuela, E.4    Cuezva, J.M.5    Salas, J.6
  • 40
    • 0031937630 scopus 로고    scopus 로고
    • African swine fever virus is wrapped by the endoplasmic reticulum
    • Rouiller, I., S. M. Brookes, A. D. Hyatt, M. Windsor, and T. Wileman. 1998. African swine fever virus is wrapped by the endoplasmic reticulum. J. Virol. 72:2373-2387.
    • (1998) J. Virol. , vol.72 , pp. 2373-2387
    • Rouiller, I.1    Brookes, S.M.2    Hyatt, A.D.3    Windsor, M.4    Wileman, T.5
  • 41
    • 0002300485 scopus 로고    scopus 로고
    • African swine fever virus: A missing link between poxviruses and iridoviruses?
    • E. Domingo, R. G. Webster, and J. J. Holland (ed.), Academic Press, Ltd., London, United Kingdom
    • Salas, J., M. L. Salas, and E. Viñuela. 1999. African swine fever virus: a missing link between poxviruses and iridoviruses?, p. 467-480. In E. Domingo, R. G. Webster, and J. J. Holland (ed.), Origin and evolution of viruses. Academic Press, Ltd., London, United Kingdom.
    • (1999) Origin and Evolution of Viruses , pp. 467-480
    • Salas, J.1    Salas, M.L.2    Viñuela, E.3
  • 42
    • 0027227704 scopus 로고
    • Polyprotein processing in African swine fever virus: A novel gene expression strategy for a DNA virus
    • Simón-Mateo, C., G. Andrés, and E. Viñuela. 1993. Polyprotein processing in African swine fever virus: a novel gene expression strategy for a DNA virus. EMBO J. 12:2977-2987.
    • (1993) EMBO J. , vol.12 , pp. 2977-2987
    • Simón-Mateo, C.1    Andrés, G.2    Viñuela, E.3
  • 43
    • 0030610715 scopus 로고    scopus 로고
    • Proteolytic processing in African swine fever virus: Evidence for a new structural polyprotein, pp62
    • Simón-Mateo, C., G. Andrés, F. Almazán, and E. Viñuela. 1997. Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62. J. Virol. 71:5799-5804.
    • (1997) J. Virol. , vol.71 , pp. 5799-5804
    • Simón-Mateo, C.1    Andrés, G.2    Almazán, F.3    Viñuela, E.4
  • 44
    • 0025769401 scopus 로고
    • The multistep proteolytic maturation pathway utilized by vaccinia virus P4a protein: A degenerate conserved cleavage motif within core proteins
    • Vanslyke, J. K., S. S. Whitehead, E. M. Wilson, and D. E. Hruby. 1991. The multistep proteolytic maturation pathway utilized by vaccinia virus P4a protein: a degenerate conserved cleavage motif within core proteins. Virology 183:467-478.
    • (1991) Virology , vol.183 , pp. 467-478
    • Vanslyke, J.K.1    Whitehead, S.S.2    Wilson, E.M.3    Hruby, D.E.4
  • 45
    • 0002647013 scopus 로고
    • Molecular biology of African swine fever virus
    • Y. Becker (ed.), Nijhoff, Boston, Mass
    • Viñuela, E. 1987. Molecular biology of African swine fever virus, p. 31-49. In Y. Becker (ed.), African swine fever. Nijhoff, Boston, Mass.
    • (1987) African Swine Fever , pp. 31-49
    • Viñuela, E.1
  • 46
    • 0024831007 scopus 로고
    • Characterization of the adenovirus proteinase: Development and use of a specific peptide assay
    • Webster, A., W. C. Russell, and G. D. Kemp. 1989. Characterization of the adenovirus proteinase: development and use of a specific peptide assay. J. Gen. Virol. 70:3215-3223.
    • (1989) J. Gen. Virol. , vol.70 , pp. 3215-3223
    • Webster, A.1    Russell, W.C.2    Kemp, G.D.3
  • 47
    • 0024817679 scopus 로고
    • Characterization of the adenovirus proteinase: Substrate specificity
    • Webster, A., S. Russell, P. Talbot, W. C. Russell, and G. D. Kemp. 1989. Characterization of the adenovirus proteinase: substrate specificity. J. Gen. Virol. 70:3225-3234.
    • (1989) J. Gen. Virol. , vol.70 , pp. 3225-3234
    • Webster, A.1    Russell, S.2    Talbot, P.3    Russell, W.C.4    Kemp, G.D.5
  • 49
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou, W., and M. D. Resh. 1996. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70: 8540-8548.
    • (1996) J. Virol. , vol.70 , pp. 8540-8548
    • Zhou, W.1    Resh, M.D.2

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