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Volumn 154, Issue 1-2, 2010, Pages 61-76

The PRRSV replicase: Exploring the multifunctionality of an intriguing set of nonstructural proteins

Author keywords

Diagnostic assays; Nonstructural proteins; RNA synthesis; Vaccines; Viral enzymes

Indexed keywords

HELICASE; MESSENGER RNA; NONSTRUCTURAL PROTEIN 1; NONSTRUCTURAL PROTEIN 10; NONSTRUCTURAL PROTEIN 11; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 4; NONSTRUCTURAL PROTEIN 8; NONSTRUCTURAL PROTEIN 9; RIBONUCLEASE; RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 78649322018     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2010.07.030     Document Type: Review
Times cited : (329)

References (114)
  • 1
    • 0033008414 scopus 로고    scopus 로고
    • North American and European porcine reproductive and respiratory syndrome viruses differ in non-structural protein coding regions
    • Allende R., Lewis T.L., Lu Z., Rock D.L., Kutish G.F., Ali A., Doster A.R., Osorio F.A. North American and European porcine reproductive and respiratory syndrome viruses differ in non-structural protein coding regions. J. Gen. Virol. 1999, 80:307-315.
    • (1999) J. Gen. Virol. , vol.80 , pp. 307-315
    • Allende, R.1    Lewis, T.L.2    Lu, Z.3    Rock, D.L.4    Kutish, G.F.5    Ali, A.6    Doster, A.R.7    Osorio, F.A.8
  • 3
    • 0036374953 scopus 로고    scopus 로고
    • Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus
    • Bautista E.M., Faaberg K.S., Mickelson D., McGruder E.D. Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus. Virology 2002, 298:258-270.
    • (2002) Virology , vol.298 , pp. 258-270
    • Bautista, E.M.1    Faaberg, K.S.2    Mickelson, D.3    McGruder, E.D.4
  • 5
    • 73949087536 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus nonstructural protein 1beta modulates host innate immune response by antagonizing IRF3 activation
    • Beura L.K., Sarkar S.N., Kwon B., Subramaniam S., Jones C., Pattnaik A.K., Osorio F.A. Porcine reproductive and respiratory syndrome virus nonstructural protein 1beta modulates host innate immune response by antagonizing IRF3 activation. J. Virol. 2010, 84:1574-1584.
    • (2010) J. Virol. , vol.84 , pp. 1574-1584
    • Beura, L.K.1    Sarkar, S.N.2    Kwon, B.3    Subramaniam, S.4    Jones, C.5    Pattnaik, A.K.6    Osorio, F.A.7
  • 7
    • 66849101997 scopus 로고    scopus 로고
    • Antibody response of nonstructural proteins: implication for diagnostic detection and differentiation of Type I and Type II porcine reproductive and respiratory syndrome virus
    • Brown E., Lawson S., Welbon C., Murtaugh M.P., Nelson E.A., Zimmerman J.J., Rowland R.R.R., Fang Y. Antibody response of nonstructural proteins: implication for diagnostic detection and differentiation of Type I and Type II porcine reproductive and respiratory syndrome virus. Clin. Vac. Immunol. 2009, 16:628-635.
    • (2009) Clin. Vac. Immunol. , vol.16 , pp. 628-635
    • Brown, E.1    Lawson, S.2    Welbon, C.3    Murtaugh, M.P.4    Nelson, E.A.5    Zimmerman, J.J.6    Rowland, R.R.R.7    Fang, Y.8
  • 8
    • 0037770207 scopus 로고    scopus 로고
    • Generation of a candidate live marker vaccine for equine arteritis virus by deletion of the major virus neutralization domain
    • Castillo-Olivares J., Wieringa R.T., Bakonyi A.A.F., de Vries N.J., Poyner D., Rottier P.J.M. Generation of a candidate live marker vaccine for equine arteritis virus by deletion of the major virus neutralization domain. J. Virol. 2003, 77:8470-8480.
    • (2003) J. Virol. , vol.77 , pp. 8470-8480
    • Castillo-Olivares, J.1    Wieringa, R.T.2    Bakonyi, A.A.F.3    de Vries, N.J.4    Poyner, D.5    Rottier, P.J.M.6
  • 9
    • 0030634897 scopus 로고    scopus 로고
    • Nidovirales: a new order comprising Coronaviridae and Arteriviridae
    • Cavanagh D. Nidovirales: a new order comprising Coronaviridae and Arteriviridae. Arch. Virol. 1997, 142:629-633.
    • (1997) Arch. Virol. , vol.142 , pp. 629-633
    • Cavanagh, D.1
  • 10
    • 75849149994 scopus 로고    scopus 로고
    • Identification of two auto-cleavage products of nonstructural protein 1 (nsp1) in porcine reproductive and respiratory syndrome virus infected cells: nsp1 function as interferon antagonist
    • Chen Z., Lawson S., Sun Z., Zhou X., Guan X., Christopher-Hennings J., Nelson E.A., Fang Y. Identification of two auto-cleavage products of nonstructural protein 1 (nsp1) in porcine reproductive and respiratory syndrome virus infected cells: nsp1 function as interferon antagonist. Virology 2010, 398(1):87-97.
    • (2010) Virology , vol.398 , Issue.1 , pp. 87-97
    • Chen, Z.1    Lawson, S.2    Sun, Z.3    Zhou, X.4    Guan, X.5    Christopher-Hennings, J.6    Nelson, E.A.7    Fang, Y.8
  • 11
    • 77949499693 scopus 로고    scopus 로고
    • Immunodominant epitopes in nsp2 of porcine reproductive and respiratory syndrome virus are dispensable for replication but play an important role in modulation of host immune response
    • Chen Z., Zhou X., Lunney J.K., Lawson S., Sun Z., Brown E., Christopher-Hennings J., Knudsen D., Nelson E., Fang Y. Immunodominant epitopes in nsp2 of porcine reproductive and respiratory syndrome virus are dispensable for replication but play an important role in modulation of host immune response. J. Gen. Virol. 2010, 91:1047-1057.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1047-1057
    • Chen, Z.1    Zhou, X.2    Lunney, J.K.3    Lawson, S.4    Sun, Z.5    Brown, E.6    Christopher-Hennings, J.7    Knudsen, D.8    Nelson, E.9    Fang, Y.10
  • 12
    • 0027254342 scopus 로고
    • Molecular characterization of porcine reproductive and respiratory syndrome virus, a member of the arterivirus group
    • Conzelmann K.K., Visser N., Van Woensel P., Thiel H.J. Molecular characterization of porcine reproductive and respiratory syndrome virus, a member of the arterivirus group. Virology 1993, 193:329-339.
    • (1993) Virology , vol.193 , pp. 329-339
    • Conzelmann, K.K.1    Visser, N.2    Van Woensel, P.3    Thiel, H.J.4
  • 14
    • 33748684385 scopus 로고    scopus 로고
    • Mapping of B-cell linear epitopes on Nsp2 and structural proteins of a North American strain of porcine reproductive and respiratory syndrome virus
    • de Lima M., Pattnaik A.K., Flores E.F., Osorio F.A. Mapping of B-cell linear epitopes on Nsp2 and structural proteins of a North American strain of porcine reproductive and respiratory syndrome virus. Virology 2006, 353:410-421.
    • (2006) Virology , vol.353 , pp. 410-421
    • de Lima, M.1    Pattnaik, A.K.2    Flores, E.F.3    Osorio, F.A.4
  • 15
    • 45049088392 scopus 로고    scopus 로고
    • Development of a porcine reproductive and respiratory syndrome virus differentiable (DIVA) strain through deletion of specific immunodominant epitopes
    • de Lima M., Kwon B., Ansari I.H., Pattnaik A.K., Flores E.F., Osorio F.A. Development of a porcine reproductive and respiratory syndrome virus differentiable (DIVA) strain through deletion of specific immunodominant epitopes. Vaccine 2008, 26:3594-3600.
    • (2008) Vaccine , vol.26 , pp. 3594-3600
    • de Lima, M.1    Kwon, B.2    Ansari, I.H.3    Pattnaik, A.K.4    Flores, E.F.5    Osorio, F.A.6
  • 17
    • 0029074522 scopus 로고
    • Processing and evolution of the N-Terminal region of the arterivirus replicase ORF1a protein: identification of two papainlike cysteine proteases
    • den Boon J.A., Faaberg K.S., Meulenberg J.J.M., Wassenaar A.L.M., Plagemann P.G.W., Gorbelenya A.E., Snijder E.J. Processing and evolution of the N-Terminal region of the arterivirus replicase ORF1a protein: identification of two papainlike cysteine proteases. J. Virol. 1995, 69:4500-4505.
    • (1995) J. Virol. , vol.69 , pp. 4500-4505
    • den Boon, J.A.1    Faaberg, K.S.2    Meulenberg, J.J.M.3    Wassenaar, A.L.M.4    Plagemann, P.G.W.5    Gorbelenya, A.E.6    Snijder, E.J.7
  • 20
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk K., Rötzschke O., Stevanović S., Jung G., Rammensee H.G. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 1991, 351:290-296.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rötzschke, O.2    Stevanović, S.3    Jung, G.4    Rammensee, H.G.5
  • 21
    • 1442348815 scopus 로고    scopus 로고
    • Heterogeneity in Nsp2 of European-like porcine reproductive and respiratory syndrome viruses isolated in the United States
    • Fang Y., Kim D.Y., Ropp S., Steen P., Christopher-Hennings J., Nelson E.A., Rowland R.R.R. Heterogeneity in Nsp2 of European-like porcine reproductive and respiratory syndrome viruses isolated in the United States. Virus Res. 2004, 100:229-235.
    • (2004) Virus Res. , vol.100 , pp. 229-235
    • Fang, Y.1    Kim, D.Y.2    Ropp, S.3    Steen, P.4    Christopher-Hennings, J.5    Nelson, E.A.6    Rowland, R.R.R.7
  • 22
    • 33751205654 scopus 로고    scopus 로고
    • A full-length cDNA infectious clone of North American type 1 porcine reproductive and respiratory syndrome virus: expression of green fluorescent protein in the nsp2 region
    • Fang Y., Rowland R.R.R., Roof M., Lunney J.K., Christopher-Hennings J., Nelson E.A. A full-length cDNA infectious clone of North American type 1 porcine reproductive and respiratory syndrome virus: expression of green fluorescent protein in the nsp2 region. J. Virol. 2006, 80:11447-11455.
    • (2006) J. Virol. , vol.80 , pp. 11447-11455
    • Fang, Y.1    Rowland, R.R.R.2    Roof, M.3    Lunney, J.K.4    Christopher-Hennings, J.5    Nelson, E.A.6
  • 23
    • 34247464685 scopus 로고    scopus 로고
    • Diversity and evolution of a newly emerged North American Type 1 porcine arterivirus
    • Fang Y., Schneider P., Zhang W.P., Faaberg K., Nelson E.A., Rowland R.R.R. Diversity and evolution of a newly emerged North American Type 1 porcine arterivirus. Arch. Virol. 2007, 152:1009-1017.
    • (2007) Arch. Virol. , vol.152 , pp. 1009-1017
    • Fang, Y.1    Schneider, P.2    Zhang, W.P.3    Faaberg, K.4    Nelson, E.A.5    Rowland, R.R.R.6
  • 24
    • 58149378585 scopus 로고    scopus 로고
    • Development of genetic markers in the nonstructural protein 2 region of a US type 1 porcine reproductive and respiratory syndrome virus: implications for future recombinant marker vaccine development
    • Fang Y., Christopher-Hennings J., Brown E., Liu H., Chen Z., Lawson S., Breen R., Clement T., Gao X., Bao J., Knudsen D., Daly R., Nelson E.A. Development of genetic markers in the nonstructural protein 2 region of a US type 1 porcine reproductive and respiratory syndrome virus: implications for future recombinant marker vaccine development. J. Gen. Virol. 2008, 89:3086-3096.
    • (2008) J. Gen. Virol. , vol.89 , pp. 3086-3096
    • Fang, Y.1    Christopher-Hennings, J.2    Brown, E.3    Liu, H.4    Chen, Z.5    Lawson, S.6    Breen, R.7    Clement, T.8    Gao, X.9    Bao, J.10    Knudsen, D.11    Daly, R.12    Nelson, E.A.13
  • 26
    • 3142681148 scopus 로고    scopus 로고
    • Genomic characterization of two Chinese isolates of porcine respiratory and reproductive syndrome virus
    • Gao Z.Q., Guo X., Yang H.C. Genomic characterization of two Chinese isolates of porcine respiratory and reproductive syndrome virus. Arch. Virol. 2004, 149:1341-1351.
    • (2004) Arch. Virol. , vol.149 , pp. 1341-1351
    • Gao, Z.Q.1    Guo, X.2    Yang, H.C.3
  • 27
    • 0027325337 scopus 로고
    • Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (LDV)
    • Godeny E.K., Chen L., Kumar S.N., Methven S.L., Koonin E.V., Brinton M.A. Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (LDV). Virology 1993, 194:585-596.
    • (1993) Virology , vol.194 , pp. 585-596
    • Godeny, E.K.1    Chen, L.2    Kumar, S.N.3    Methven, S.L.4    Koonin, E.V.5    Brinton, M.A.6
  • 29
    • 38449090489 scopus 로고    scopus 로고
    • Pathogenic viruses: smart manipulators of the interfeon system
    • Haller O., Weber F. Pathogenic viruses: smart manipulators of the interfeon system. Curr. Top. Microbiol. Immunol. 2007, 316:315-334.
    • (2007) Curr. Top. Microbiol. Immunol. , vol.316 , pp. 315-334
    • Haller, O.1    Weber, F.2
  • 30
    • 33750417154 scopus 로고    scopus 로고
    • Complete genome analysis of RFLP 184 isolates of porcine reproductive and respiratory syndrome virus
    • Han J., Wang Y., Faaberg K.S. Complete genome analysis of RFLP 184 isolates of porcine reproductive and respiratory syndrome virus. Virus Res. 2006, 122:175-182.
    • (2006) Virus Res. , vol.122 , pp. 175-182
    • Han, J.1    Wang, Y.2    Faaberg, K.S.3
  • 31
    • 35348840283 scopus 로고    scopus 로고
    • Identification of nonessential regions of the nsp2 replicase protein of porcine reproductive and respiratory syndrome virus strain VR-2332 for replication in cell culture
    • Han J., Liu G., Wang Y., Faaberg K.S. Identification of nonessential regions of the nsp2 replicase protein of porcine reproductive and respiratory syndrome virus strain VR-2332 for replication in cell culture. J. Virol. 2007, 81:9878-9890.
    • (2007) J. Virol. , vol.81 , pp. 9878-9890
    • Han, J.1    Liu, G.2    Wang, Y.3    Faaberg, K.S.4
  • 32
    • 69449091717 scopus 로고    scopus 로고
    • The porcine reproductive and respiratory syndrome virus nsp2 cysteine protease domain possesses both trans- and cis-cleavage activities
    • Han J., Rutherford M.S., Faaberg K.S. The porcine reproductive and respiratory syndrome virus nsp2 cysteine protease domain possesses both trans- and cis-cleavage activities. J. Virol. 2009, 83:9449-9463.
    • (2009) J. Virol. , vol.83 , pp. 9449-9463
    • Han, J.1    Rutherford, M.S.2    Faaberg, K.S.3
  • 34
    • 2442679084 scopus 로고    scopus 로고
    • Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase
    • Ivanov K.A., Thiel V., Dobbe J.C., van der Meer Y., Snijder E.J., Ziebuhr J. Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase. J. Virol. 2004, 78:5619-5632.
    • (2004) J. Virol. , vol.78 , pp. 5619-5632
    • Ivanov, K.A.1    Thiel, V.2    Dobbe, J.C.3    van der Meer, Y.4    Snijder, E.J.5    Ziebuhr, J.6
  • 35
    • 34047123178 scopus 로고    scopus 로고
    • Cross-reactive antibody responses to nsp1 and nsp2 of porcine reproductive and respiratory syndrome virus
    • Johnson C.R., Yu W., Murtaugh M. Cross-reactive antibody responses to nsp1 and nsp2 of porcine reproductive and respiratory syndrome virus. J. Gen. Virol. 2007, 88:1184-1195.
    • (2007) J. Gen. Virol. , vol.88 , pp. 1184-1195
    • Johnson, C.R.1    Yu, W.2    Murtaugh, M.3
  • 36
    • 0028213467 scopus 로고
    • A conventionally attenuated glycoprotein E-negative strain of bovine herpesvirus type 1 is an efficacious and safe vaccine
    • Kaashoek M.J., Moerman A., Madic J., Rijsewijk F.A., Quak J., Gielkens A.L., van Oirschot J.T. A conventionally attenuated glycoprotein E-negative strain of bovine herpesvirus type 1 is an efficacious and safe vaccine. Vaccine 1994, 12:439-444.
    • (1994) Vaccine , vol.12 , pp. 439-444
    • Kaashoek, M.J.1    Moerman, A.2    Madic, J.3    Rijsewijk, F.A.4    Quak, J.5    Gielkens, A.L.6    van Oirschot, J.T.7
  • 37
    • 34547755766 scopus 로고    scopus 로고
    • Expression and stability of foreign tags inserted into nsp2 of porcine reproductive and respiratory syndrome virus (PRRSV)
    • Kim D.Y., Calvert J.G., Chang K.O., Horlen K., Kerrigan M., Rowland R.R.R. Expression and stability of foreign tags inserted into nsp2 of porcine reproductive and respiratory syndrome virus (PRRSV). Virus Res. 2007, 128:106-114.
    • (2007) Virus Res. , vol.128 , pp. 106-114
    • Kim, D.Y.1    Calvert, J.G.2    Chang, K.O.3    Horlen, K.4    Kerrigan, M.5    Rowland, R.R.R.6
  • 38
    • 58149470391 scopus 로고    scopus 로고
    • Insertion and deletion in a non-essential region of the nonstructural protein 2 (nsp2) of porcine reproductive and respiratory syndrome (PRRS) virus: effects on virulence and immunogenicity
    • Kim D.Y., Kaiser T.J., Horlen K., Keith M.L., Taylor L.P., Jolie R., Calvert J.G., Rowland R.R.R. Insertion and deletion in a non-essential region of the nonstructural protein 2 (nsp2) of porcine reproductive and respiratory syndrome (PRRS) virus: effects on virulence and immunogenicity. Virus Genes 2009, 38:118-128.
    • (2009) Virus Genes , vol.38 , pp. 118-128
    • Kim, D.Y.1    Kaiser, T.J.2    Horlen, K.3    Keith, M.L.4    Taylor, L.P.5    Jolie, R.6    Calvert, J.G.7    Rowland, R.R.R.8
  • 39
    • 77953028825 scopus 로고    scopus 로고
    • Modulation of type I interferon induction by porcine reproductive and respiratory syndrome virus and degradation of CREB-binding protein by non-structural protein 1 in MARC-145 and HeLa cells
    • Kim O., Sun Y., Lai F.W., Song C., Yoo D. Modulation of type I interferon induction by porcine reproductive and respiratory syndrome virus and degradation of CREB-binding protein by non-structural protein 1 in MARC-145 and HeLa cells. Virology 2010, 402(2):315-326.
    • (2010) Virology , vol.402 , Issue.2 , pp. 315-326
    • Kim, O.1    Sun, Y.2    Lai, F.W.3    Song, C.4    Yoo, D.5
  • 43
    • 53349166311 scopus 로고    scopus 로고
    • Identification of virulence determinants of porcine reproductive and respiratory syndrome virus through construction of chimeric clones
    • Kwon B., Ansari I.H., Pattnaik A.K., Osorio F.A. Identification of virulence determinants of porcine reproductive and respiratory syndrome virus through construction of chimeric clones. Virology 2008, 380:371-378.
    • (2008) Virology , vol.380 , pp. 371-378
    • Kwon, B.1    Ansari, I.H.2    Pattnaik, A.K.3    Osorio, F.A.4
  • 44
    • 41849125938 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus (PRRSV) suppresses interferon-β production by interfering with the RIG-I signaling pathway
    • Luo R., Xiao S., Jiang Y., Jin H., Wang D., Liu M., Chen H., Fang L. Porcine reproductive and respiratory syndrome virus (PRRSV) suppresses interferon-β production by interfering with the RIG-I signaling pathway. Mol. Immunol. 2008, 45:2839-2846.
    • (2008) Mol. Immunol. , vol.45 , pp. 2839-2846
    • Luo, R.1    Xiao, S.2    Jiang, Y.3    Jin, H.4    Wang, D.5    Liu, M.6    Chen, H.7    Fang, L.8
  • 45
    • 0033974998 scopus 로고    scopus 로고
    • A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae
    • Makarova K.S., Aravind L., Koonin E.V. A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. Trends Biochem. Sci. 2000, 25:50-52.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 50-52
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 46
    • 0036785519 scopus 로고    scopus 로고
    • Newcastle disease virus marker vaccine: an immunodominant epitope on the nucleoprotein gene of NDV can be deleted or replaced by a foreign epitope
    • Mebatsion T., Koolen M.J.M., de Vaan L.T.C., de Haas N., Braber M., Romer-Oberdorfer A., van den Elzen P., van der Marel P. Newcastle disease virus marker vaccine: an immunodominant epitope on the nucleoprotein gene of NDV can be deleted or replaced by a foreign epitope. J. Virol. 2002, 76:10138-10146.
    • (2002) J. Virol. , vol.76 , pp. 10138-10146
    • Mebatsion, T.1    Koolen, M.J.M.2    de Vaan, L.T.C.3    de Haas, N.4    Braber, M.5    Romer-Oberdorfer, A.6    van den Elzen, P.7    van der Marel, P.8
  • 47
    • 0242500999 scopus 로고    scopus 로고
    • Gradual development of the interferon-gamma response of swine to porcine reproductive and respiratory syndrome virus infection or vaccination
    • Meier W.A., Galeota J., Osorio F.A., Husmann R.J., Schnitzlein W.M., Zuckermann F.A. Gradual development of the interferon-gamma response of swine to porcine reproductive and respiratory syndrome virus infection or vaccination. Virology 2003, 309:18-31.
    • (2003) Virology , vol.309 , pp. 18-31
    • Meier, W.A.1    Galeota, J.2    Osorio, F.A.3    Husmann, R.J.4    Schnitzlein, W.M.5    Zuckermann, F.A.6
  • 49
    • 0031985681 scopus 로고    scopus 로고
    • Infectious transcripts from cloned genome-length cDNA of porcine reproductive respiratory syndrome virus
    • Meulenberg J.J.M., Bos-de Ruijter J.N.A., Wensvoort G., Moormann R.J.M. Infectious transcripts from cloned genome-length cDNA of porcine reproductive respiratory syndrome virus. J. Virol. 1998, 72:380-387.
    • (1998) J. Virol. , vol.72 , pp. 380-387
    • Meulenberg, J.J.M.1    Bos-de Ruijter, J.N.A.2    Wensvoort, G.3    Moormann, R.J.M.4
  • 50
    • 7044286680 scopus 로고    scopus 로고
    • Interferon type I response in porcine reproductive and respiratory syndrome virus-infected MARC-145 cells
    • Miller L.C., Laegreid W.W., Bono J.L., Chitko-Mckown C.G., Fox J.M. Interferon type I response in porcine reproductive and respiratory syndrome virus-infected MARC-145 cells. Arch. Virol. 2004, 149:2453-2463.
    • (2004) Arch. Virol. , vol.149 , pp. 2453-2463
    • Miller, L.C.1    Laegreid, W.W.2    Bono, J.L.3    Chitko-Mckown, C.G.4    Fox, J.M.5
  • 51
    • 0025330428 scopus 로고
    • Inactivation of the thymidine kinase gene of a g1 deletion mutant of pseudorabies virus generates a safe but still highly immunogenic vaccine strain
    • Moormann R.J., de Rover T., Briaire J., Peeters B.P., Gielkens A.L., van Oirschot J.T. Inactivation of the thymidine kinase gene of a g1 deletion mutant of pseudorabies virus generates a safe but still highly immunogenic vaccine strain. J. Gen. Virol. 1990, 71:1591-1595.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1591-1595
    • Moormann, R.J.1    de Rover, T.2    Briaire, J.3    Peeters, B.P.4    Gielkens, A.L.5    van Oirschot, J.T.6
  • 52
    • 66149091584 scopus 로고    scopus 로고
    • Biochemical characterization of arterivirus nonstructural protein 11 reveals the nidovirus-wide conservation of a replicative endoribonuclease
    • Nedialkova D.D., Ulferts R., van den Born E., Lauber C., Gorbalenya A.E., Ziebuhr J., Snijder E.J. Biochemical characterization of arterivirus nonstructural protein 11 reveals the nidovirus-wide conservation of a replicative endoribonuclease. J. Virol. 2009, 83(11):5671-5682.
    • (2009) J. Virol. , vol.83 , Issue.11 , pp. 5671-5682
    • Nedialkova, D.D.1    Ulferts, R.2    van den Born, E.3    Lauber, C.4    Gorbalenya, A.E.5    Ziebuhr, J.6    Snijder, E.J.7
  • 53
    • 77649247357 scopus 로고    scopus 로고
    • Arterivirus Nsp1 modulates the accumulation of minus-strand templates to control the relative abundance of viral mRNAs
    • Nedialkova D.D., Gorbalenya A.E., Snijder E.J. Arterivirus Nsp1 modulates the accumulation of minus-strand templates to control the relative abundance of viral mRNAs. PLoS Pathog. 2010, 6(2):e1000772.
    • (2010) PLoS Pathog. , vol.6 , Issue.2
    • Nedialkova, D.D.1    Gorbalenya, A.E.2    Snijder, E.J.3
  • 54
    • 0032889516 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus comparison: divergent evolution on two continents
    • Nelsen C.J., Murtaugh M.P., Faaberg K.S. Porcine reproductive and respiratory syndrome virus comparison: divergent evolution on two continents. J. Virol. 1999, 73:270-280.
    • (1999) J. Virol. , vol.73 , pp. 270-280
    • Nelsen, C.J.1    Murtaugh, M.P.2    Faaberg, K.S.3
  • 55
    • 0035104619 scopus 로고    scopus 로고
    • Epitope mapping porcine reproductive and respiratory syndrome virus by phage display: the nsp2 fragment of the replicase polyprotein contains a cluster of B-cell epitopes
    • Oleksiewicz M.B., Botner A., Toft P., Normann P., Storgaard T. Epitope mapping porcine reproductive and respiratory syndrome virus by phage display: the nsp2 fragment of the replicase polyprotein contains a cluster of B-cell epitopes. J. Virol. 2001, 75:3277-3290.
    • (2001) J. Virol. , vol.75 , pp. 3277-3290
    • Oleksiewicz, M.B.1    Botner, A.2    Toft, P.3    Normann, P.4    Storgaard, T.5
  • 56
    • 0035954834 scopus 로고    scopus 로고
    • Semen from boars infected with porcine reproductive and respiratory syndrome virus (PRRSV) contains antibodies against structural as well as nonstructural viral proteins
    • Oleksiewicz M.B., Bøtner A., Normann P. Semen from boars infected with porcine reproductive and respiratory syndrome virus (PRRSV) contains antibodies against structural as well as nonstructural viral proteins. Vet. Microbiol. 2001, 81:109-125.
    • (2001) Vet. Microbiol. , vol.81 , pp. 109-125
    • Oleksiewicz, M.B.1    Bøtner, A.2    Normann, P.3
  • 57
    • 0037126614 scopus 로고    scopus 로고
    • Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis
    • Pasternak A.O., van den Born E., Spaan W.J., Snijder E.J. Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis. EMBO J. 2001, 20:7220-7228.
    • (2001) EMBO J. , vol.20 , pp. 7220-7228
    • Pasternak, A.O.1    van den Born, E.2    Spaan, W.J.3    Snijder, E.J.4
  • 59
    • 0033017866 scopus 로고    scopus 로고
    • Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex
    • Pedersen K.W., van der Meer Y., Roos N., Snijder E.J. Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex. J. Virol. 1999, 73:2016-2026.
    • (1999) J. Virol. , vol.73 , pp. 2016-2026
    • Pedersen, K.W.1    van der Meer, Y.2    Roos, N.3    Snijder, E.J.4
  • 60
    • 0030876795 scopus 로고    scopus 로고
    • Comparative morphogenesis of three PRRS virus strains
    • Pol J.M.A., Wagenaar F., Reus J.E.G. Comparative morphogenesis of three PRRS virus strains. Vet. Microbiol. 1997, 55:203-208.
    • (1997) Vet. Microbiol. , vol.55 , pp. 203-208
    • Pol, J.M.A.1    Wagenaar, F.2    Reus, J.E.G.3
  • 61
    • 32444450251 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the Nidovirus replicative endoribonuclease NendoU exerts pleiotropic effects on the arterivirus life cycle
    • Posthuma C.C., Nedialkova D.D., Zevenhoven-Dobbe J.C., Blokhuis J.H., Gorbalenya A.E., Snijder E.J. Site-directed mutagenesis of the Nidovirus replicative endoribonuclease NendoU exerts pleiotropic effects on the arterivirus life cycle. J. Virol. 2006, 80:1653-1661.
    • (2006) J. Virol. , vol.80 , pp. 1653-1661
    • Posthuma, C.C.1    Nedialkova, D.D.2    Zevenhoven-Dobbe, J.C.3    Blokhuis, J.H.4    Gorbalenya, A.E.5    Snijder, E.J.6
  • 62
    • 42449116994 scopus 로고    scopus 로고
    • Formation of the arterivirus replication/transcription complex: a key role for nonstructural protein 3 in the remodeling of intracellular membranes
    • Posthuma C.C., Pedersen K.W., Lu Z., Joosten R.G., Roos N., Zevenhoven-Dobbe J.C., Snijder E.J. Formation of the arterivirus replication/transcription complex: a key role for nonstructural protein 3 in the remodeling of intracellular membranes. J. Virol. 2008, 82:4480-4491.
    • (2008) J. Virol. , vol.82 , pp. 4480-4491
    • Posthuma, C.C.1    Pedersen, K.W.2    Lu, Z.3    Joosten, R.G.4    Roos, N.5    Zevenhoven-Dobbe, J.C.6    Snijder, E.J.7
  • 63
    • 36348940608 scopus 로고    scopus 로고
    • Interferons and viruses: an interplay between induction, signaling, antiviral responses and virus countermeasures
    • Randall R.E., Goodbourn S. Interferons and viruses: an interplay between induction, signaling, antiviral responses and virus countermeasures. J. Gen. Virol. 2008, 89:1-47.
    • (2008) J. Gen. Virol. , vol.89 , pp. 1-47
    • Randall, R.E.1    Goodbourn, S.2
  • 65
    • 0023779206 scopus 로고
    • A sequence pattern common to T cell epitopes
    • Rothbard J.B., Taylor W.R. A sequence pattern common to T cell epitopes. EMBO J. 1988, 7:93-100.
    • (1988) EMBO J. , vol.7 , pp. 93-100
    • Rothbard, J.B.1    Taylor, W.R.2
  • 67
    • 0022610643 scopus 로고
    • The cap structure of simian hemorrhagic fever virion RNA
    • Sagripanti J.L., Zandomeni R.O., Weinmann R. The cap structure of simian hemorrhagic fever virion RNA. Virology 1986, 151:146-150.
    • (1986) Virology , vol.151 , pp. 146-150
    • Sagripanti, J.L.1    Zandomeni, R.O.2    Weinmann, R.3
  • 68
    • 0034767753 scopus 로고    scopus 로고
    • Antiviral actions of interferons
    • Samuel C.E. Antiviral actions of interferons. Clin. Microbiol. Rev. 2001, 14:778-809.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 778-809
    • Samuel, C.E.1
  • 69
    • 0029444973 scopus 로고
    • Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands
    • Sawicki S.G., Sawicki D.L. Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands. Adv. Exp. Med. Biol. 1995, 380:499-506.
    • (1995) Adv. Exp. Med. Biol. , vol.380 , pp. 499-506
    • Sawicki, S.G.1    Sawicki, D.L.2
  • 70
    • 33845750075 scopus 로고    scopus 로고
    • A contemporary view of coronavirus transcription
    • Sawicki S.G., Sawicki D.L., Siddell S.G. A contemporary view of coronavirus transcription. J. Virol. 2007, 81:20-29.
    • (2007) J. Virol. , vol.81 , pp. 20-29
    • Sawicki, S.G.1    Sawicki, D.L.2    Siddell, S.G.3
  • 71
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I: Papain
    • Schechter I., Berger A. On the size of the active site in proteases. I: Papain. Biochem. Biophys. Res. Commun. 1967, 27(2):157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , Issue.2 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 72
  • 73
    • 0033818909 scopus 로고    scopus 로고
    • Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases
    • Seybert A., van Dinten L.C., Snijder E.J., Ziebuhr J. Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases. J. Virol. 2000, 74:9586-9593.
    • (2000) J. Virol. , vol.74 , pp. 9586-9593
    • Seybert, A.1    van Dinten, L.C.2    Snijder, E.J.3    Ziebuhr, J.4
  • 75
    • 0034128116 scopus 로고    scopus 로고
    • Determination of the complete nucleotide sequence of a vaccine strain of porcine reproductive and respiratory syndrome virus and identification of the Nsp2 gene with a unique insertion
    • Shen S., Kwang J., Liu W., Liu D.X. Determination of the complete nucleotide sequence of a vaccine strain of porcine reproductive and respiratory syndrome virus and identification of the Nsp2 gene with a unique insertion. Arch. Virol. 2000, 145:871-883.
    • (2000) Arch. Virol. , vol.145 , pp. 871-883
    • Shen, S.1    Kwang, J.2    Liu, W.3    Liu, D.X.4
  • 76
    • 0026475757 scopus 로고
    • The 5' end of the equine arteritis virus replicase gene encodes a papainlike cysteine protease
    • Snijder E.J., Wassenaar A.L.M., Spaan W.J. The 5' end of the equine arteritis virus replicase gene encodes a papainlike cysteine protease. J. Virol. 1992, 66:7040-7048.
    • (1992) J. Virol. , vol.66 , pp. 7040-7048
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.3
  • 77
    • 0028067318 scopus 로고
    • Proteolytic processing of the replicase ORF1a protein of equine arteritis virus
    • Snijder E.J., Wassenaar A.L.M., Spaan W.J. Proteolytic processing of the replicase ORF1a protein of equine arteritis virus. J. Virol. 1994, 68:5755-5764.
    • (1994) J. Virol. , vol.68 , pp. 5755-5764
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.3
  • 78
    • 0029044301 scopus 로고
    • The arterivirus Nsp2 protease. An unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases
    • Snijder E.J., Wassenaar A.L.M., Spaan W.J., Gorbalenya A.E. The arterivirus Nsp2 protease. An unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases. J. Biol. Chem. 1995, 270:16671-16676.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16671-16676
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.3    Gorbalenya, A.E.4
  • 79
    • 0029966508 scopus 로고    scopus 로고
    • The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases
    • Snijder E.J., Wassenaar A.L.M., van Dinten L.C., Spaan W.J.M., Gorbalenya A.E. The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases. J. Biol. Chem. 1996, 271:4864-4871.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4864-4871
    • Snijder, E.J.1    Wassenaar, A.L.M.2    van Dinten, L.C.3    Spaan, W.J.M.4    Gorbalenya, A.E.5
  • 80
    • 0031925071 scopus 로고    scopus 로고
    • The molecular biology of arteriviruses
    • Snijder E.J., Meulenberg J.J. The molecular biology of arteriviruses. J. Gen. Virol. 1998, 79:961-979.
    • (1998) J. Gen. Virol. , vol.79 , pp. 961-979
    • Snijder, E.J.1    Meulenberg, J.J.2
  • 81
    • 0035008260 scopus 로고    scopus 로고
    • Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex
    • Snijder E.J., van Tol H., Roos N., Pedersen K.W. Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex. J. Gen. Virol. 2001, 82:985-994.
    • (2001) J. Gen. Virol. , vol.82 , pp. 985-994
    • Snijder, E.J.1    van Tol, H.2    Roos, N.3    Pedersen, K.W.4
  • 83
    • 49049121501 scopus 로고    scopus 로고
    • Arteriviruses. In: Knipe, D. M., and P. M. Howley, (Eds.), Fields Virology, fifth ed. Lippincott Williams & Wilkins, Philidelphia
    • Snijder, E.J., Spaan, W.J., 2006. Arteriviruses. In: Knipe, D. M., and P. M. Howley, (Eds.), Fields Virology, vol. 1, fifth ed. Lippincott Williams & Wilkins, Philidelphia, pp. 1337-1355.
    • (2006) , vol.1 , pp. 1337-1355
    • Snijder, E.J.1    Spaan, W.J.2
  • 84
    • 70350328704 scopus 로고    scopus 로고
    • Crystal structure of porcine reproductive and respiratory syndrome virus (PRRSV) leader protease Nsp1{alpha}
    • Sun Y., Xue F., Guo Y., Ma M., Hao N., Zhang X.C., Lou Z., Li X., Rao Z. Crystal structure of porcine reproductive and respiratory syndrome virus (PRRSV) leader protease Nsp1{alpha}. J. Virol. 2009, 83:10931-10940.
    • (2009) J. Virol. , vol.83 , pp. 10931-10940
    • Sun, Y.1    Xue, F.2    Guo, Y.3    Ma, M.4    Hao, N.5    Zhang, X.C.6    Lou, Z.7    Li, X.8    Rao, Z.9
  • 85
    • 78649334068 scopus 로고    scopus 로고
    • b. Inhibition of type 1 interferon signaling by nsp11 of PRRSV. In: The 2009 International PRRS Symposium, abstract no. 33, December 2009, Chicago, IL, USA.
    • Sun, Y., Chen, N., Yoo, D., 2009b. Inhibition of type 1 interferon signaling by nsp11 of PRRSV. In: The 2009 International PRRS Symposium, abstract no. 33, 4-5 December 2009, Chicago, IL, USA.
    • (2009) , Issue.4-5
    • Sun, Y.1    Chen, N.2    Yoo, D.3
  • 86
    • 77954461006 scopus 로고    scopus 로고
    • The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism function. J. Virol. [Epub ahead of print].
    • Sun, Z., Chen, Z., Lawson, S., Fang, Y., 2010. The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism function. J. Virol. [Epub ahead of print].
    • (2010)
    • Sun, Z.1    Chen, Z.2    Lawson, S.3    Fang, Y.4
  • 87
    • 34547618481 scopus 로고    scopus 로고
    • Emergence of fatal PRRSV variants: unparalleled outbreaks of atypical PRRS in China and molecular dissection of the unique hallmark
    • Tian K., Yu X., Zhao T., Feng Y., Cao Z., Wang C., et al. Emergence of fatal PRRSV variants: unparalleled outbreaks of atypical PRRS in China and molecular dissection of the unique hallmark. PLoS ONE 2007, 2:526.
    • (2007) PLoS ONE , vol.2 , pp. 526
    • Tian, K.1    Yu, X.2    Zhao, T.3    Feng, Y.4    Cao, Z.5    Wang, C.6
  • 88
    • 69749102863 scopus 로고    scopus 로고
    • Structure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of porcine reproductive and respiratory syndrome virus (PRRSV)
    • Tian X., Lu G., Gao F., Peng H., Feng Y., Ma G., Bartlam M., Tian K., Yan J., Hilgenfeld R., Gao G.F. Structure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of porcine reproductive and respiratory syndrome virus (PRRSV). J. Mol. Biol. 2009, 392:977-993.
    • (2009) J. Mol. Biol. , vol.392 , pp. 977-993
    • Tian, X.1    Lu, G.2    Gao, F.3    Peng, H.4    Feng, Y.5    Ma, G.6    Bartlam, M.7    Tian, K.8    Yan, J.9    Hilgenfeld, R.10    Gao, G.F.11
  • 89
    • 0035852649 scopus 로고    scopus 로고
    • A zinc finger-containing papain-like protease couples subgenomic mRNA synthesis to genome translation in a positive-stranded RNA virus
    • Tijms M.A., van Dinten L.C., Gorbalenya A.E., Snijder E.J. A zinc finger-containing papain-like protease couples subgenomic mRNA synthesis to genome translation in a positive-stranded RNA virus. Proc. Natl. Acad. Sci. 2001, 98:1889-1894.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 1889-1894
    • Tijms, M.A.1    van Dinten, L.C.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 90
    • 0036211003 scopus 로고    scopus 로고
    • Nuclear localization of non-structural protein 1 and nucleocapsid protein of equine arteritis virus
    • Tijms M.A., van der Meer Y., Snijder E.J. Nuclear localization of non-structural protein 1 and nucleocapsid protein of equine arteritis virus. J. Gen. Virol. 2002, 83:795-800.
    • (2002) J. Gen. Virol. , vol.83 , pp. 795-800
    • Tijms, M.A.1    van der Meer, Y.2    Snijder, E.J.3
  • 91
    • 0041852685 scopus 로고    scopus 로고
    • Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100
    • Tijms M.A., Snijder E.J. Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100. J. Gen. Virol. 2003, 84:2317-2322.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2317-2322
    • Tijms, M.A.1    Snijder, E.J.2
  • 92
    • 34648833261 scopus 로고    scopus 로고
    • Arterivirus subgenomic mRNA synthesis and virion biogenesis depend on the multifunctional nsp1 autoprotease
    • Tijms M.A., Nedialkova D.D., Zevenhoven-Dobbe J.C., Gorbalenya A.E., Snijder E.J. Arterivirus subgenomic mRNA synthesis and virion biogenesis depend on the multifunctional nsp1 autoprotease. J. Virol. 2007, 81:10496-10505.
    • (2007) J. Virol. , vol.81 , pp. 10496-10505
    • Tijms, M.A.1    Nedialkova, D.D.2    Zevenhoven-Dobbe, J.C.3    Gorbalenya, A.E.4    Snijder, E.J.5
  • 93
    • 3142562527 scopus 로고    scopus 로고
    • A highly pathogenic porcine reproductive and respiratory syndrome virus generated from an infectious cDNA clone retains the in vivo virulence and transmissibility properties of the parental virus
    • Truong H.M., Lu Z., Kutish G.F., Galeota J., Osorio F.A., Pattnaik A.K. A highly pathogenic porcine reproductive and respiratory syndrome virus generated from an infectious cDNA clone retains the in vivo virulence and transmissibility properties of the parental virus. Virology 2004, 325:308-319.
    • (2004) Virology , vol.325 , pp. 308-319
    • Truong, H.M.1    Lu, Z.2    Kutish, G.F.3    Galeota, J.4    Osorio, F.A.5    Pattnaik, A.K.6
  • 94
    • 33751405956 scopus 로고    scopus 로고
    • Proteolytic maturation of replicase polyprotein pp1a by the nsp4 main proteinase is essential for equine arteritis virus replication and includes internal cleavage of nsp7
    • van Aken D., Zevenhoven-Dobbe J.C., Gorbalenya A.E., Snijder E.J. Proteolytic maturation of replicase polyprotein pp1a by the nsp4 main proteinase is essential for equine arteritis virus replication and includes internal cleavage of nsp7. J. Gen. Virol. 2006, 87:3473-3482.
    • (2006) J. Gen. Virol. , vol.87 , pp. 3473-3482
    • van Aken, D.1    Zevenhoven-Dobbe, J.C.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 95
    • 33645220757 scopus 로고    scopus 로고
    • Mutagenesis analysis of the nsp4 main proteinase reveals determinants of arterivirus replicase polyprotein autoprocessing
    • van Aken D., Snijder E.J., Gorbalenya A.E. Mutagenesis analysis of the nsp4 main proteinase reveals determinants of arterivirus replicase polyprotein autoprocessing. J. Virol. 2006, 80:3428-3437.
    • (2006) J. Virol. , vol.80 , pp. 3428-3437
    • van Aken, D.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 96
    • 0031879009 scopus 로고    scopus 로고
    • ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex
    • van der Meer Y., van Tol H., Locker J.K., Snijder E.J. ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex. J. Virol. 1998, 72:6689-6698.
    • (1998) J. Virol. , vol.72 , pp. 6689-6698
    • van der Meer, Y.1    van Tol, H.2    Locker, J.K.3    Snijder, E.J.4
  • 97
    • 0029844841 scopus 로고    scopus 로고
    • Processing of the equine arteritis virus replicase ORF1b protein: identification of cleavage products containing the putative viral polymerase and helicase domains
    • van Dinten L.C., Wassenaar A.L., Gorbalenya A.E., Spaan W.J., Snijder E.J. Processing of the equine arteritis virus replicase ORF1b protein: identification of cleavage products containing the putative viral polymerase and helicase domains. J. Virol. 1996, 70:6625-6633.
    • (1996) J. Virol. , vol.70 , pp. 6625-6633
    • van Dinten, L.C.1    Wassenaar, A.L.2    Gorbalenya, A.E.3    Spaan, W.J.4    Snijder, E.J.5
  • 98
    • 0031017109 scopus 로고    scopus 로고
    • An infectious arterivirus cDNA clone: identification of a replicase point mutation that abolishes discontinuous mRNA transcription
    • van Dinten L.C., den Boon J.A., Wassenaar A.L., Spaan W.J., Snijder E.J. An infectious arterivirus cDNA clone: identification of a replicase point mutation that abolishes discontinuous mRNA transcription. Proc. Natl. Acad. Sci. 1997, 94:991-996.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 991-996
    • van Dinten, L.C.1    den Boon, J.A.2    Wassenaar, A.L.3    Spaan, W.J.4    Snijder, E.J.5
  • 99
    • 0034105481 scopus 로고    scopus 로고
    • The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis
    • van Dinten L.C., van Tol H., Gorbalenya A.E., Snijder E.J. The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis. J. Virol. 2000, 74:5213-5223.
    • (2000) J. Virol. , vol.74 , pp. 5213-5223
    • van Dinten, L.C.1    van Tol, H.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 100
    • 47749135896 scopus 로고    scopus 로고
    • The in vitro RNA synthesizing activity of the isolated arterivirus replication/transcription complex is dependent on a host factor
    • van Hemert M.J., de Wilde A.H., Gorbalenya A.E., Snijder E.J. The in vitro RNA synthesizing activity of the isolated arterivirus replication/transcription complex is dependent on a host factor. J. Biol. Chem. 2008, 283:16525-16536.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16525-16536
    • van Hemert, M.J.1    de Wilde, A.H.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 101
    • 0032718485 scopus 로고    scopus 로고
    • Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences
    • van Marle G., Dobbe J.C., Gultyaev A.P., Luytjes W., Spaan W.J., Snijder E.J. Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences. Proc. Natl. Acad. Sci. 1999, 96:12056-12061.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 12056-12061
    • van Marle, G.1    Dobbe, J.C.2    Gultyaev, A.P.3    Luytjes, W.4    Spaan, W.J.5    Snijder, E.J.6
  • 102
    • 0033031789 scopus 로고    scopus 로고
    • Characterization of an equine arteritis virus replicase mutant defective in subgenomic mRNA synthesis
    • van Marle G., van Dinten L.C., Spaan W.J., Luytjes W., Snijder E.J. Characterization of an equine arteritis virus replicase mutant defective in subgenomic mRNA synthesis. J. Virol. 1999, 73:5274-5281.
    • (1999) J. Virol. , vol.73 , pp. 5274-5281
    • van Marle, G.1    van Dinten, L.C.2    Spaan, W.J.3    Luytjes, W.4    Snijder, E.J.5
  • 104
    • 0033976119 scopus 로고    scopus 로고
    • Development of a genetically marked recombinant rinderpest vaccine expressing green fluorescent protein
    • Walsh E.P., Baron M.D., Rennie L.F., Anderson J., Barrett T. Development of a genetically marked recombinant rinderpest vaccine expressing green fluorescent protein. J. Gen. Virol. 2000, 81:709-718.
    • (2000) J. Gen. Virol. , vol.81 , pp. 709-718
    • Walsh, E.P.1    Baron, M.D.2    Rennie, L.F.3    Anderson, J.4    Barrett, T.5
  • 105
    • 0033780321 scopus 로고    scopus 로고
    • Recombinant rinderpest vaccines expressing membrane-anchored proteins as genetic markers: evidence of exclusion of marker protein from the virus envelope
    • Walsh E.P., Baron M.D., Rennie L.F., Monaghan P., Anderson J., Barrett T. Recombinant rinderpest vaccines expressing membrane-anchored proteins as genetic markers: evidence of exclusion of marker protein from the virus envelope. J. Virol. 2000, 74:10165-10175.
    • (2000) J. Virol. , vol.74 , pp. 10165-10175
    • Walsh, E.P.1    Baron, M.D.2    Rennie, L.F.3    Monaghan, P.4    Anderson, J.5    Barrett, T.6
  • 106
    • 38649113555 scopus 로고    scopus 로고
    • Attenuation of porcine reproductive and respiratory syndrome virus strain MN184 using chimeric construction with vaccine sequence
    • Wang Y., Liang Y., Han J., Burkhart K.M., Vaughn E.M., Roof M.B., Faaberg K.S. Attenuation of porcine reproductive and respiratory syndrome virus strain MN184 using chimeric construction with vaccine sequence. Virology 2008, 371(2):418-429.
    • (2008) Virology , vol.371 , Issue.2 , pp. 418-429
    • Wang, Y.1    Liang, Y.2    Han, J.3    Burkhart, K.M.4    Vaughn, E.M.5    Roof, M.B.6    Faaberg, K.S.7
  • 107
    • 0030856299 scopus 로고    scopus 로고
    • Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that Nsp2 acts as a cofactor for the Nsp4 serine protease
    • Wassenaar A.L., Spaan W.J., Gorbalenya A.E., Snijder E.J. Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that Nsp2 acts as a cofactor for the Nsp4 serine protease. J. Virol. 1997, 71:9313-9322.
    • (1997) J. Virol. , vol.71 , pp. 9313-9322
    • Wassenaar, A.L.1    Spaan, W.J.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 108
    • 78649316091 scopus 로고
    • Electron microscopic studies on the morphogenesis of PRRSV in infected cells-comparative studies. In: Schwyzer, M., Ackermann, M., Bertoni, G., Kocherhans, R., McCullough, K., Engels, M., Wittek, R., Zanoni, R. (Eds.), Immunobiology of Viral Infections. Proceedings of the 3rd Congress of the European Society of
    • Weiland, F., Granzow, H., Wieczorek-Krohmer, M., Weiland, E., 1995. Electron microscopic studies on the morphogenesis of PRRSV in infected cells-comparative studies. In: Schwyzer, M., Ackermann, M., Bertoni, G., Kocherhans, R., McCullough, K., Engels, M., Wittek, R., Zanoni, R. (Eds.), Immunobiology of Viral Infections. Proceedings of the 3rd Congress of the European Society of Veterinary Virology, pp. 499-502.
    • (1995)
    • Weiland, F.1    Granzow, H.2    ieczorek-Krohmer, M.3    Weiland, E.4
  • 109
    • 0034011266 scopus 로고    scopus 로고
    • Classical swine fever virus E(rns) deletion mutants: trans-complementation and potential use as non transmissible, modified, live-attenuated marker vaccines
    • Widjojoatmodjo M.N., van Gennip H.G., Bouma A., van Rijn P.A., Moormann R.J. Classical swine fever virus E(rns) deletion mutants: trans-complementation and potential use as non transmissible, modified, live-attenuated marker vaccines. J. Virol. 2000, 74:2973-2980.
    • (2000) J. Virol. , vol.74 , pp. 2973-2980
    • Widjojoatmodjo, M.N.1    van Gennip, H.G.2    Bouma, A.3    van Rijn, P.A.4    Moormann, R.J.5
  • 110
    • 34248207613 scopus 로고    scopus 로고
    • Monoclonal antibody and porcine antisera recognized B-cell epitopes of Nsp2 protein of a Chinese strain of porcine reproductive and respiratory syndrome virus
    • Yan Y., Guo X., Ge X., Chen Y., Cha Z., Yang H. Monoclonal antibody and porcine antisera recognized B-cell epitopes of Nsp2 protein of a Chinese strain of porcine reproductive and respiratory syndrome virus. Virus Res. 2007, 126:207-215.
    • (2007) Virus Res. , vol.126 , pp. 207-215
    • Yan, Y.1    Guo, X.2    Ge, X.3    Chen, Y.4    Cha, Z.5    Yang, H.6
  • 111
    • 78649316417 scopus 로고    scopus 로고
    • Modulation of type 1 interferon production and evasion strategies of PRRSV from the host defense. In: The 2009 International PRRS Symposium, 4-5 December 2009, Chicago, IL, USA (abstract no. 9).
    • Yoo, D., Kim, O., Song, C., Sun, Y., Du, Y., Liu, H.C., 2009. Modulation of type 1 interferon production and evasion strategies of PRRSV from the host defense. In: The 2009 International PRRS Symposium, 4-5 December 2009, Chicago, IL, USA (abstract no. 9).
    • (2009)
    • Yoo, D.1    Kim, O.2    Song, C.3    Sun, Y.4    Du, Y.5    Liu, H.C.6
  • 112
    • 45849089115 scopus 로고    scopus 로고
    • Genetic polymorphism of the nsp2 gene in North American type porcine reproductive and respiratory syndrome virus
    • Yoshii M., Okinaga T., Miyazaki A., Kato K., Ikeda H., Tsunemitsu H. Genetic polymorphism of the nsp2 gene in North American type porcine reproductive and respiratory syndrome virus. Arch. Virol. 2008, 153(7):1323-1334.
    • (2008) Arch. Virol. , vol.153 , Issue.7 , pp. 1323-1334
    • Yoshii, M.1    Okinaga, T.2    Miyazaki, A.3    Kato, K.4    Ikeda, H.5    Tsunemitsu, H.6
  • 113
    • 65349102181 scopus 로고    scopus 로고
    • The 30 amino acids deletion in Nsp2 of highly pathogenic porcine reproductive and respiratory syndrome virus emerging in China is not related to its virulence
    • Zhou L., Zhang J., Zeng J., Yin S., Li Y., Zheng L., Guo X., Ge X., Yang H. The 30 amino acids deletion in Nsp2 of highly pathogenic porcine reproductive and respiratory syndrome virus emerging in China is not related to its virulence. J. Virol. 2009, 83:5156-5167.
    • (2009) J. Virol. , vol.83 , pp. 5156-5167
    • Zhou, L.1    Zhang, J.2    Zeng, J.3    Yin, S.4    Li, Y.5    Zheng, L.6    Guo, X.7    Ge, X.8    Yang, H.9
  • 114
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr J., Snijder E.J., Gorbalenya A.E. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 2000, 81:853-879.
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3


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