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Volumn 37, Issue 7, 2005, Pages 701-709

Trans-dominant inhibition of RNA viral replication can slow growth of drug-resistant viruses

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEIN VIRAL PROTEINASE 2A; PROTEINASE; RNA POLYMERASE; UNCLASSIFIED DRUG; ANTIVIRUS AGENT; CAPSID PROTEIN; CYSTEINE PROTEINASE; DISOXARIL; ISOXAZOLE DERIVATIVE; PICORNAIN 2A, PICORNAVIRUS; VIRUS PROTEIN;

EID: 22844440540     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1583     Document Type: Article
Times cited : (113)

References (48)
  • 1
    • 0030747157 scopus 로고    scopus 로고
    • RNA virus mutations and fitness for survival
    • Domingo, E. & Holland, J.J. RNA virus mutations and fitness for survival. Annu. Rev. Microbiol. 51, 151-178 (1997).
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 151-178
    • Domingo, E.1    Holland, J.J.2
  • 2
    • 0343881333 scopus 로고
    • Mixed infection of HeLa cells with polioviruses types 1 and 2
    • Ledinko, N. & Hirst, G.K. Mixed infection of HeLa cells with polioviruses types 1 and 2. Virology 14, 207-219 (1961).
    • (1961) Virology , vol.14 , pp. 207-219
    • Ledinko, N.1    Hirst, G.K.2
  • 3
    • 2442673461 scopus 로고
    • Maturation of poliovirus RNA with capsid protein coded by heterologous enteroviruses
    • Holland, J.J. & Cords, C.E. Maturation of poliovirus RNA with capsid protein coded by heterologous enteroviruses. Proc. Natl. Acad. Sci. USA 51, 1082-1085 (1964).
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 1082-1085
    • Holland, J.J.1    Cords, C.E.2
  • 4
    • 1842340370 scopus 로고
    • Rescue of drug-requiring and drug-inhibited enteroviruses
    • Ikegami, N., Eggers, H.J. & Tamm, I. Rescue of drug-requiring and drug-inhibited enteroviruses. Proc. Natl. Acad. Sci. USA 52, 1419-1426 (1964).
    • (1964) Proc. Natl. Acad. Sci. USA , vol.52 , pp. 1419-1426
    • Ikegami, N.1    Eggers, H.J.2    Tamm, I.3
  • 5
    • 0024431579 scopus 로고
    • Virus mutation frequencies can be greatly underestimated by monoclonal antibody neutralization of virions
    • Holland, J.J. et al. Virus mutation frequencies can be greatly underestimated by monoclonal antibody neutralization of virions. J. Virol. 63, 5030-5036 (1989).
    • (1989) J. Virol. , vol.63 , pp. 5030-5036
    • Holland, J.J.1
  • 6
    • 0001856730 scopus 로고    scopus 로고
    • Possible unifying mechanism of picornavirus genome replication
    • (eds. B.L. Semler & E. Wimmer) (ASM Press, Washington, D.C.)
    • Paul, A.V. Possible unifying mechanism of picornavirus genome replication, in Molecular Biology of Picornaviruses (eds. B.L. Semler & E. Wimmer) 227-246 (ASM Press, Washington, D.C., 2002).
    • (2002) Molecular Biology of Picornaviruses , pp. 227-246
    • Paul, A.V.1
  • 7
    • 0023945724 scopus 로고
    • Construction and characterization of poliovirus subgenomic replicons
    • Kaplan, G. & Racaniello, V.R. Construction and characterization of poliovirus subgenomic replicons. J. Virol. 62, 1687-1696 (1988).
    • (1988) J. Virol. , vol.62 , pp. 1687-1696
    • Kaplan, G.1    Racaniello, V.R.2
  • 8
    • 0028136217 scopus 로고
    • Coupling between genome translation and replication in an RNA virus
    • Novak, J.E. & Kirkegaard, K. Coupling between genome translation and replication in an RNA virus. Genes Dev. 8, 1726-1737 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 1726-1737
    • Novak, J.E.1    Kirkegaard, K.2
  • 9
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle, J.M., Bullitt, E., Bienz, K. & Kirkegaard, K. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 296, 2218-2222 (2002).
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 10
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase
    • Thompson, A.A. & Peersen, O.B. Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J. 23, 3462-3471 (2004).
    • (2004) EMBO J. , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 11
    • 0033766003 scopus 로고    scopus 로고
    • Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg
    • Paul, A.V., Rieder, E., Kim, D.W., van Boom, J.H. & Wimmer, E. Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg. J. Virol. 74, 10359-10370 (2000).
    • (2000) J. Virol. , vol.74 , pp. 10359-10370
    • Paul, A.V.1    Rieder, E.2    Kim, D.W.3    Van Boom, J.H.4    Wimmer, E.5
  • 12
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz, I. Functional inactivation of genes by dominant negative mutations. Nature 329, 219-222 (1987).
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 13
    • 0037405787 scopus 로고    scopus 로고
    • Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: Analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA
    • Yin, J., Paul, A.V., Wimmer, E. & Rieder, E. Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA. J. Virol. 77, 5152-5166 (2003).
    • (2003) J. Virol. , vol.77 , pp. 5152-5166
    • Yin, J.1    Paul, A.V.2    Wimmer, E.3    Rieder, E.4
  • 14
    • 0037383425 scopus 로고    scopus 로고
    • Poliovirus CRE-dependent VPg uridylylation is required for positive-strand RNA synthesis but not for negative-strand RNA synthesis
    • Murray, K.E. & Barton, D.J. Poliovirus CRE-dependent VPg uridylylation is required for positive-strand RNA synthesis but not for negative-strand RNA synthesis. J. Virol. 77. 4739-4750 (2003).
    • (2003) J. Virol. , vol.77 , pp. 4739-4750
    • Murray, K.E.1    Barton, D.J.2
  • 15
    • 0027170180 scopus 로고
    • Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA
    • Andino, R., Rieckhof, G.E., Achacoso, P.L. & Baltimore, D. Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA. EMBO J. 12, 3587-3598 (1993).
    • (1993) EMBO J. , vol.12 , pp. 3587-3598
    • Andino, R.1    Rieckhof, G.E.2    Achacoso, P.L.3    Baltimore, D.4
  • 16
    • 0026443004 scopus 로고
    • Translational enhancement of the poliovirus 5′ noncoding region mediated by virus-encoded polypeptide 2A
    • Hambidge, S.J. & Sarnow, P. Translational enhancement of the poliovirus 5′ noncoding region mediated by virus-encoded polypeptide 2A. Proc. Natl. Acad. Sci. USA 89, 10272-10276 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10272-10276
    • Hambidge, S.J.1    Sarnow, P.2
  • 17
    • 0027976823 scopus 로고
    • Role for poliovirus protease 2A in cap independent translation
    • 1994
    • Macadam, A.J. et al. 1994. Role for poliovirus protease 2A in cap independent translation. EMBO J. 13, 924-927 (1994).
    • (1994) EMBO J. , vol.13 , pp. 924-927
    • Macadam, A.J.1
  • 18
    • 0023043280 scopus 로고
    • A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein
    • Toyoda, H. et al. A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein. Cell 45, 761-770 (1986).
    • (1986) Cell , vol.45 , pp. 761-770
    • Toyoda, H.1
  • 19
    • 0026729556 scopus 로고
    • Determinants of substrate recognition by poliovirus 2A proteinase
    • Hellen, C.U., Lee, C.K. & Wimmer, E. Determinants of substrate recognition by poliovirus 2A proteinase. J. Virol. 66, 3330-3338 (1992).
    • (1992) J. Virol. , vol.66 , pp. 3330-3338
    • Hellen, C.U.1    Lee, C.K.2    Wimmer, E.3
  • 20
    • 0034740269 scopus 로고    scopus 로고
    • Poliovirus 5′-terminal cloverleaf RNA is required in cis for VPg uridylylation and the initiation of negative-strand RNA synthesis
    • Lyons, T., Murray, K.E., Roberts, A.W. & Barton, D.J. Poliovirus 5′-terminal cloverleaf RNA is required in cis for VPg uridylylation and the initiation of negative-strand RNA synthesis. J. Virol. 75, 10696-10708 (2001).
    • (2001) J. Virol. , vol.75 , pp. 10696-10708
    • Lyons, T.1    Murray, K.E.2    Roberts, A.W.3    Barton, D.J.4
  • 21
    • 0024518366 scopus 로고
    • A point mutation in the poliovirus polymerase gene determines a complementable temperature-sensitive defect of RNA replication
    • Agut, H. et al. A point mutation in the poliovirus polymerase gene determines a complementable temperature-sensitive defect of RNA replication. Virology 168, 302-311 (1989).
    • (1989) Virology , vol.168 , pp. 302-311
    • Agut, H.1
  • 22
    • 0025785399 scopus 로고
    • trans rescue of a mutant poliovirus RNA polymerase function
    • Charmi, W.A., Burns, C.C., Ehrenfeld, E. & Semler, B.L. trans rescue of a mutant poliovirus RNA polymerase function. J. Virol. 65, 2655-2665 (1991).
    • (1991) J. Virol. , vol.65 , pp. 2655-2665
    • Charmi, W.A.1    Burns, C.C.2    Ehrenfeld, E.3    Semler, B.L.4
  • 23
    • 0025835611 scopus 로고
    • Three poliovirus 2B mutants exhibit noncomplementable defects in viral RNA amplification and display dosage-dependent dominance over wild-type poliovirus
    • Johnson, K.L. & Sarnow, P. Three poliovirus 2B mutants exhibit noncomplementable defects in viral RNA amplification and display dosage-dependent dominance over wild-type poliovirus. J. Virol. 65, 4341-4349 (1991).
    • (1991) J. Virol. , vol.65 , pp. 4341-4349
    • Johnson, K.L.1    Sarnow, P.2
  • 24
    • 0025150548 scopus 로고
    • Temperature-sensitive poliovirus mutant fails to cleave VPO and accumulates provirions
    • Compton, S.R., Nelsen, B. & Kirkegaard, K. Temperature-sensitive poliovirus mutant fails to cleave VPO and accumulates provirions. J. Virol. 64, 4067-4075 (1990).
    • (1990) J. Virol. , vol.64 , pp. 4067-4075
    • Compton, S.R.1    Nelsen, B.2    Kirkegaard, K.3
  • 25
    • 0030732120 scopus 로고    scopus 로고
    • Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB
    • Hope, D.A., Diamond, S.E. & Kirkegaard, K. Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB. J. Virol. 71, 9490-9498 (1997).
    • (1997) J. Virol. , vol.71 , pp. 9490-9498
    • Hope, D.A.1    Diamond, S.E.2    Kirkegaard, K.3
  • 26
    • 0022632902 scopus 로고
    • Prevention of rhinovirus and poliovirus uncoating by WIN 51711, a new antiviral drug
    • Fox, M.P., Otto, M.J. & McKinlay, M.A. Prevention of rhinovirus and poliovirus uncoating by WIN 51711, a new antiviral drug. Antimicrob. Agents Chemother. 30, 110-116 (1986).
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 110-116
    • Fox, M.P.1    Otto, M.J.2    McKinlay, M.A.3
  • 28
    • 0028109679 scopus 로고
    • Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions
    • Mosser, A.G., Sgro, J.Y. & Rueckert, R.R. Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions. J. Virol. 68, 8193-8201 (1994).
    • (1994) J. Virol. , vol.68 , pp. 8193-8201
    • Mosser, A.G.1    Sgro, J.Y.2    Rueckert, R.R.3
  • 30
    • 0024522337 scopus 로고
    • Clearance of a persistent human enterovirus infection of the mouse central nervous system by the antiviral agent disoxaril
    • Jubelt, B., Wilson, A.K., Ropka, S.L., Guidinger, P.L. & McKinlay, M.A. Clearance of a persistent human enterovirus infection of the mouse central nervous system by the antiviral agent disoxaril. J. Infect. Dis. 159, 866-871 (1989).
    • (1989) J. Infect. Dis. , vol.159 , pp. 866-871
    • Jubelt, B.1    Wilson, A.K.2    Ropka, S.L.3    Guidinger, P.L.4    McKinlay, M.A.5
  • 31
    • 0033028818 scopus 로고    scopus 로고
    • Attenuated virulence of pleconaril-resistant coxsackie-virus B3 variants
    • Groarke, J.M. & Pevear, D.C. Attenuated virulence of pleconaril-resistant coxsackie-virus B3 variants. J. Infect. Dis. 179, 1538-1541 (1999).
    • (1999) J. Infect. Dis. , vol.179 , pp. 1538-1541
    • Groarke, J.M.1    Pevear, D.C.2
  • 32
    • 0025033393 scopus 로고
    • In vitro processing of Dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3
    • Preugschat, F., Yao, C.-W. & Strauss, J.H. In vitro processing of Dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3. J. Virol. 64, 4364-4374 (1990).
    • (1990) J. Virol. , vol.64 , pp. 4364-4374
    • Preugschat, F.1    Yao, C.-W.2    Strauss, J.H.3
  • 33
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost, B. & Sander, C. Conservation and prediction of solvent accessibility in protein families. Proteins 20, 216-226 (1994).
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 34
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 35
    • 0025060763 scopus 로고
    • Mutations in VP1 of poliovirus specifically affect both encapsidation and release of viral RNA
    • Kirkegaard, K. Mutations in VP1 of poliovirus specifically affect both encapsidation and release of viral RNA. J. Virol. 64, 195-206 (1990).
    • (1990) J. Virol. , vol.64 , pp. 195-206
    • Kirkegaard, K.1
  • 36
    • 0035868852 scopus 로고    scopus 로고
    • 5′ cloverleaf in poliovirus RNA is a cis-acting replication element required for negative-strand synthesis
    • Barton, D.J., O'Donnell, B.J. & Flanegan, J.B. 5′ cloverleaf in poliovirus RNA is a cis-acting replication element required for negative-strand synthesis. EMBO J. 20, 1439-1448 (2001).
    • (2001) EMBO J. , vol.20 , pp. 1439-1448
    • Barton, D.J.1    O'Donnell, B.J.2    Flanegan, J.B.3
  • 37
    • 0026623162 scopus 로고
    • Poliovirus RNA recombination: Mechanistic studies in the absence of selection
    • Jarvis, T.C. & Kirkegaard, K. Poliovirus RNA recombination: mechanistic studies in the absence of selection. EMBO J. 11, 3135-3145 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3135-3145
    • Jarvis, T.C.1    Kirkegaard, K.2
  • 38
    • 0028896662 scopus 로고
    • Amino acid substitutions in the polioivirus maturation cleavage site affect assembly and result in accumulation of provirions
    • Ansardi, D.C. & Morrow, C.D. Amino acid substitutions in the polioivirus maturation cleavage site affect assembly and result in accumulation of provirions. J. Virol. 69, 1540-1547 (1995).
    • (1995) J. Virol. , vol.69 , pp. 1540-1547
    • Ansardi, D.C.1    Morrow, C.D.2
  • 39
    • 0025882931 scopus 로고
    • Identification of residues in VP2 that contribute to poliovirus neutralization antigenic site 3B
    • Reynolds, C., Page, G., Zhou, H. & Chow, M. Identification of residues in VP2 that contribute to poliovirus neutralization antigenic site 3B. Virology 184, 391-396 (1991).
    • (1991) Virology , vol.184 , pp. 391-396
    • Reynolds, C.1    Page, G.2    Zhou, H.3    Chow, M.4
  • 40
    • 0025825159 scopus 로고
    • Identification of essential ammo acid residues n the functional activity of poliovirus 2A proteinase
    • Yu, S.F. & Lloyd, R.E. Identification of essential ammo acid residues n the functional activity of poliovirus 2A proteinase. Virology 182, 615-625 (1991).
    • (1991) Virology , vol.182 , pp. 615-625
    • Yu, S.F.1    Lloyd, R.E.2
  • 41
    • 0018026449 scopus 로고
    • O4-(5′-uridylyl)tyrosine is the bond between the genome-linked protein and the RNA of poliovirus
    • Rothberg, P.G., Harris, T.J., Nomoto, A. & Wimmer, E. O4-(5′-uridylyl)tyrosine is the bond between the genome-linked protein and the RNA of poliovirus. Proc. Natl. Acad. Sci. USA 75, 4868-4872 (1978).
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4868-4872
    • Rothberg, P.G.1    Harris, T.J.2    Nomoto, A.3    Wimmer, E.4
  • 42
    • 0017809191 scopus 로고
    • Protein is linked to the 5′ end of poliovirus RNA by a phosphodiester linkage to tyrosine
    • Ambros, V. & Baltimore, D. Protein is linked to the 5′ end of poliovirus RNA by a phosphodiester linkage to tyrosine. J. Biol. Chem. 253, 5263-5266 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 5263-5266
    • Ambros, V.1    Baltimore, D.2
  • 43
    • 0026095274 scopus 로고
    • Site-directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase
    • Hammerle, T., Hellen, C.U. & Wimmer, E. Site-directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase. J. Biol. Chem. 266, 5412-5416 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 5412-5416
    • Hammerle, T.1    Hellen, C.U.2    Wimmer, E.3
  • 44
    • 0035283140 scopus 로고    scopus 로고
    • Oligomeric structures of poliovirus polymerase are important for function
    • Hobson, S.D. et al. Oligomeric structures of poliovirus polymerase are important for function. EMBO J. 20, 1153-1163 (2001).
    • (2001) EMBO J. , vol.20 , pp. 1153-1163
    • Hobson, S.D.1
  • 45
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen, J.L., Long, A.M. & Schultz, S.C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 5, 1109-1122 (1997).
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 46
    • 0024459018 scopus 로고
    • Effects of mutations in poliovirus 3Dpol on RNA polymerase activity and on polyprotein cleavage
    • Burns, C.C., Lawson, M.A., Semler, B.L. & Ehrenfeld, E. Effects of mutations in poliovirus 3Dpol on RNA polymerase activity and on polyprotein cleavage. J. Virol. 63, 4866-4874 (1989).
    • (1989) J. Virol. , vol.63 , pp. 4866-4874
    • Burns, C.C.1    Lawson, M.A.2    Semler, B.L.3    Ehrenfeld, E.4
  • 47
    • 0034003829 scopus 로고    scopus 로고
    • Identification of a cis-acting replication element within the poliovirus coding region
    • Goodfellow, I. et al. Identification of a cis-acting replication element within the poliovirus coding region. J. Virol. 74, 4590-4600 (2000).
    • (2000) J. Virol. , vol.74 , pp. 4590-4600
    • Goodfellow, I.1
  • 48
    • 0033570164 scopus 로고    scopus 로고
    • The structure of the 2A proteinase from a common cold virus: A proteinase responsible for the shut-off of host-cell protein synthesis
    • Petersen, J.F. et al. The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis. EMBO J. 18. 5463-5475 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5463-5475
    • Petersen, J.F.1


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