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Volumn 3, Issue 2, 2013, Pages 137-142

Viral precursor polyproteins: Keys of regulation from replication to maturation

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; GAG PROTEIN; MEMBRANE PROTEIN; NONSTRUCTURAL PROTEIN P23; NONSTRUCTURAL PROTEIN P3; NUCLEOCAPSID PROTEIN; POLYPROTEIN; PROTEINASE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

EID: 84880049355     PISSN: 18796257     EISSN: 18796265     Source Type: Journal    
DOI: 10.1016/j.coviro.2013.03.009     Document Type: Review
Times cited : (57)

References (54)
  • 1
    • 0036891835 scopus 로고    scopus 로고
    • African swine fever virus polyproteins pp220 and pp62 assemble into the core shell
    • Andres G, Alejo A, Salas J, Salas ML: African swine fever virus polyproteins pp220 and pp62 assemble into the core shell. J Virol 2002, 76:12473-12482.
    • (2002) J Virol , vol.76 , pp. 12473-12482
    • Andres, G.1    Alejo, A.2    Salas, J.3    Salas, M.L.4
  • 2
    • 0001552353 scopus 로고    scopus 로고
    • Alphaviruses
    • Edited by David M, Knipe PMH. Lippincott Williams & Wilkins
    • Griffin DE: Alphaviruses. In Fields Virology, vol 1. Edited by David M, Knipe PMH. Lippincott Williams & Wilkins; 2007:1023-1067.
    • (2007) Fields Virology , vol.1 , pp. 1023-1067
    • Griffin, D.E.1
  • 3
    • 0025352629 scopus 로고
    • Cleavage-site preferences of Sindbis virus polyproteins containing the nonstructural proteinase. Evidence for temporal regulation of polyprotein processing in vivo
    • de Groot RJ, Hardy WR, Shirako Y, Strauss JH: Cleavage-site preferences of Sindbis virus polyproteins containing the nonstructural proteinase. Evidence for temporal regulation of polyprotein processing in vivo. EMBO J 1990, 9:2631-2638.
    • (1990) EMBO J , vol.9 , pp. 2631-2638
    • De Groot, R.J.1    Hardy, W.R.2    Shirako, Y.3    Strauss, J.H.4
  • 5
    • 0027979138 scopus 로고
    • Regulation of Sindbis virus RNA replication: Uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis
    • Shirako Y, Strauss JH: Regulation of Sindbis virus RNA replication: uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis. J Virol 1994, 68:1874-1885.
    • (1994) J Virol , vol.68 , pp. 1874-1885
    • Shirako, Y.1    Strauss, J.H.2
  • 6
    • 0028221438 scopus 로고
    • Polypeptide requirements for assembly of functional Sindbis virus replication complexes: A model for the temporal regulation of minus- and plus-strand RNA synthesis
    • Lemm JA, Rümenapf T, Strauss EG, Strauss JH, Rice CM: Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus- and plus-strand RNA synthesis. EMBO J 1994, 13:2925-2934.
    • (1994) EMBO J , vol.13 , pp. 2925-2934
    • Lemm, J.A.1    Rümenapf, T.2    Strauss, E.G.3    Strauss, J.H.4    Rice, C.M.5
  • 8
    • 0025336486 scopus 로고
    • Cleavage between nsP1 and nsP2 initiates the processing pathway of Sindbis virus nonstructural polyprotein P123
    • Shirako Y, Strauss JH: Cleavage between nsP1 and nsP2 initiates the processing pathway of Sindbis virus nonstructural polyprotein P123. Virology 1990, 177:54-64.
    • (1990) Virology , vol.177 , pp. 54-64
    • Shirako, Y.1    Strauss, J.H.2
  • 9
    • 0024421374 scopus 로고
    • Processing the nonstructural polyproteins of sindbis virus: Nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans
    • Hardy WR, Strauss JH: Processing the nonstructural polyproteins of sindbis virus: nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans. J Virol 1989, 63:4653-4664.
    • (1989) J Virol , vol.63 , pp. 4653-4664
    • Hardy, W.R.1    Strauss, J.H.2
  • 11
    • 0031550546 scopus 로고    scopus 로고
    • Identification of mutations in a Sindbis virus variant able to establish persistent infection in BHK cells: The importance of a mutation in the nsP2 gene
    • Dryga SA, Dryga OA, Schlesinger S: Identification of mutations in a Sindbis virus variant able to establish persistent infection in BHK cells: the importance of a mutation in the nsP2 gene. Virology 1997, 228:74-83.
    • (1997) Virology , vol.228 , pp. 74-83
    • Dryga, S.A.1    Dryga, O.A.2    Schlesinger, S.3
  • 12
    • 47749118026 scopus 로고    scopus 로고
    • Role for conserved residues of sindbis virus nonstructural protein 2 methyltransferase-like domain in regulation of minus-strand synthesis and development of cytopathic infection
    • Mayuri, Geders TW, Smith JL, Kuhn RJ: Role for conserved residues of sindbis virus nonstructural protein 2 methyltransferase-like domain in regulation of minus-strand synthesis and development of cytopathic infection. J Virol 2008, 82:7284-7297.
    • (2008) J Virol , vol.82 , pp. 7284-7297
    • Mayuri Geders, T.W.1    Smith, J.L.2    Kuhn, R.J.3
  • 13
    • 0033814973 scopus 로고    scopus 로고
    • Replicon vectors derived from Sindbis virus and Semliki forest virus that establish persistent replication in host cells
    • Perri S, Driver DA, Gardner JP, Sherrill S, Belli BA, Dubensky TW, Polo JM: Replicon vectors derived from Sindbis virus and Semliki forest virus that establish persistent replication in host cells. J Virol 2000, 74:9802-9807.
    • (2000) J Virol , vol.74 , pp. 9802-9807
    • Perri, S.1    Driver, D.A.2    Gardner, J.P.3    Sherrill, S.4    Belli, B.A.5    Dubensky, T.W.6    Polo, J.M.7
  • 14
    • 19944373420 scopus 로고    scopus 로고
    • Noncytopathic replication of Venezuelan equine encephalitis virus and eastern equine encephalitis virus replicons in mammalian cells
    • Petrakova O, Volkova E, Gorchakov R, Paessler S, Kinney RM, Frolov I: Noncytopathic replication of Venezuelan equine encephalitis virus and eastern equine encephalitis virus replicons in mammalian cells. J Virol 2005, 79:7597-7608.
    • (2005) J Virol , vol.79 , pp. 7597-7608
    • Petrakova, O.1    Volkova, E.2    Gorchakov, R.3    Paessler, S.4    Kinney, R.M.5    Frolov, I.6
  • 15
  • 16
    • 0009928786 scopus 로고
    • The 50 end of poliovirus mRNA is not capped with m7G(50)ppp(50)Np
    • Nomoto A, Lee YF, Wimmer E: The 50 end of poliovirus mRNA is not capped with m7G(50)ppp(50)Np. Proc Natl Acad Sci U S A 1976, 73:375-380.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 375-380
    • Nomoto, A.1    Lee, Y.F.2    Wimmer, E.3
  • 17
    • 0014266643 scopus 로고
    • Evidence for large precursor proteins in poliovirus synthesis
    • Summers DF, Maizel JV Jr: Evidence for large precursor proteins in poliovirus synthesis. Proc Natl Acad Sci U S A 1968, 59:966-971.
    • (1968) Proc Natl Acad Sci U S A , vol.59 , pp. 966-971
    • Summers, D.F.1    Maizel Jr., J.V.2
  • 19
    • 0009927995 scopus 로고
    • Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome
    • Racaniello VR, Baltimore D: Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome. Proc Natl Acad Sci U S A 1981, 78:4887-4891.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 4887-4891
    • Racaniello, V.R.1    Baltimore, D.2
  • 20
    • 0023952330 scopus 로고
    • Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro
    • Jore J, De Geus B, Jackson RJ, Pouwels PH, Enger-Valk BE: Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro. J Gen Virol 1988, 69(Pt 7):1627-1636.
    • (1988) J Gen Virol , vol.69 , Issue.PART 7 , pp. 1627-1636
    • Jore, J.1    De Geus, B.2    Jackson, R.J.3    Pouwels, P.H.4    Enger-Valk, B.E.5
  • 21
    • 0024077061 scopus 로고
    • Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor
    • Ypma-Wong MF, Dewalt PG, Johnson VH, Lamb JG, Semler BL: Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology 1988, 166:265-270.
    • (1988) Virology , vol.166 , pp. 265-270
    • Ypma-Wong, M.F.1    Dewalt, P.G.2    Johnson, V.H.3    Lamb, J.G.4    Semler, B.L.5
  • 22
    • 0026464666 scopus 로고
    • Purification and characterization of poliovirus polypeptide 3CD, a proteinase and a precursor for RNA polymerase
    • Harris KS, Reddigari SR, Nicklin MJ, Hammerle T, Wimmer E: Purification and characterization of poliovirus polypeptide 3CD, a proteinase and a precursor for RNA polymerase. J Virol 1992, 66:7481-7489.
    • (1992) J Virol , vol.66 , pp. 7481-7489
    • Harris, K.S.1    Reddigari, S.R.2    Nicklin, M.J.3    Hammerle, T.4    Wimmer, E.5
  • 23
    • 0029044382 scopus 로고
    • Interaction between the 50-terminal cloverleaf and 3AB/3CDpro of poliovirus is essential for RNA replication
    • Xiang W, Harris KS, Alexander L, Wimmer E: Interaction between the 50-terminal cloverleaf and 3AB/3CDpro of poliovirus is essential for RNA replication. J Virol 1995, 69:3658-3667.
    • (1995) J Virol , vol.69 , pp. 3658-3667
    • Xiang, W.1    Harris, K.S.2    Alexander, L.3    Wimmer, E.4
  • 24
    • 34548172905 scopus 로고    scopus 로고
    • Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication
    • Belov GA, Habbersett C, Franco D, Ehrenfeld E: Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication. J Virol 2007, 81:9259-9267.
    • (2007) J Virol , vol.81 , pp. 9259-9267
    • Belov, G.A.1    Habbersett, C.2    Franco, D.3    Ehrenfeld, E.4
  • 25
    • 33947386595 scopus 로고    scopus 로고
    • Crystal structure of poliovirus 3CD protein: Virally encoded protease and precursor to the RNAdependent RNA polymerase
    • Marcotte L, Wass A, Gohara D, Pathak H, Arnold J, Filman D, Cameron C, Hogle J: Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNAdependent RNA polymerase. J Virol 2007, 81:3583.
    • (2007) J Virol , vol.81 , pp. 3583
    • Marcotte, L.1    Wass, A.2    Gohara, D.3    Pathak, H.4    Arnold, J.5    Filman, D.6    Cameron, C.7    Hogle, J.8
  • 26
    • 1842562401 scopus 로고    scopus 로고
    • The poliovirus replication machinery can escape inhibition by an antiviral drug that targets a host cell protein
    • Crotty S, Saleh MC, Gitlin L, Beske O, Andino R: The poliovirus replication machinery can escape inhibition by an antiviral drug that targets a host cell protein. J Virol 2004, 78:3378-3386.
    • (2004) J Virol , vol.78 , pp. 3378-3386
    • Crotty, S.1    Saleh, M.C.2    Gitlin, L.3    Beske, O.4    Andino, R.5
  • 27
    • 34748873170 scopus 로고    scopus 로고
    • Rice: Flaviviridae: The viruses and their replication
    • Edited by David, Knipe PMH. Lippincott Williams & Wilkins;
    • Brett D, Lindenbach H-JT, Charles M: Rice: flaviviridae: the viruses and their replication. In Fields Virology, vol 1. Edited by David, Knipe PMH. Lippincott Williams & Wilkins; 2007:1101-1152.
    • (2007) Fields Virology , vol.1 , pp. 1101-1152
    • Brett, D.1    H-Jt, L.2    Charles, M.3
  • 28
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein e
    • Allison SL, Schalich J, Stiasny K, Mandl CW, Heinz FX: Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J Virol 2001, 75:4268-4275.
    • (2001) J Virol , vol.75 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 29
    • 0036094683 scopus 로고    scopus 로고
    • Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and e in the endoplasmic reticulum
    • Lorenz IC, Allison SL, Heinz FX, Helenius A: Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum. J Virol 2002, 76:5480-5491.
    • (2002) J Virol , vol.76 , pp. 5480-5491
    • Lorenz, I.C.1    Allison, S.L.2    Heinz, F.X.3    Helenius, A.4
  • 30
    • 0027478991 scopus 로고
    • Proper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein
    • Konishi E, Mason PW: Proper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein. J Virol 1993, 67:1672-1675.
    • (1993) J Virol , vol.67 , pp. 1672-1675
    • Konishi, E.1    Mason, P.W.2
  • 31
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: Structure and maturation
    • Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, Chen J, Rossmann MG: The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 2008, 319:1830-1834.
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3    Zhang, Y.4    Kuhn, R.J.5    Chen, J.6    Rossmann, M.G.7
  • 32
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A ° resolution
    • Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC: The envelope glycoprotein from tick-borne encephalitis virus at 2 A ° resolution. Nature 1995, 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 35
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y, Ogata S, Clements D, Harrison SC: Structure of the dengue virus envelope protein after membrane fusion. Nature 2004, 427:313-319.
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 38
    • 0027081630 scopus 로고
    • The Murray valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of e glycoprotein
    • Guirakhoo F, Bolin RA, Roehrig JT: The Murray valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Virology 1992, 191:921-931.
    • (1992) Virology , vol.191 , pp. 921-931
    • Guirakhoo, F.1    Bolin, R.A.2    Roehrig, J.T.3
  • 45
    • 0001469617 scopus 로고    scopus 로고
    • Retroviridae: The retroviruses and their replication
    • Edited by David M, Knipe PMH. Lippincott Williams & Wilkins
    • Goff SP: Retroviridae: the retroviruses and their replication. In Fields Virology, vol 2. Edited by David M, Knipe PMH. Lippincott Williams & Wilkins; 2007:1999-2069.
    • (2007) Fields Virology , vol.2 , pp. 1999-2069
    • Goff, S.P.1
  • 46
    • 80051766524 scopus 로고    scopus 로고
    • Structural determinants and mechanism of HIV-1 genome packaging
    • Lu K, Heng X, Summers MF: Structural determinants and mechanism of HIV-1 genome packaging. J Mol Biol 2011, 410:609-633.
    • (2011) J Mol Biol , vol.410 , pp. 609-633
    • Lu, K.1    Heng, X.2    Summers, M.F.3
  • 47
    • 0032795497 scopus 로고    scopus 로고
    • Mass determination of rous sarcoma virus virions by scanning transmission electron microscopy
    • Vogt VM, Simon MN: Mass determination of rous sarcoma virus virions by scanning transmission electron microscopy. J Virol 1999, 73:7050-7055.
    • (1999) J Virol , vol.73 , pp. 7050-7055
    • Vogt, V.M.1    Simon, M.N.2
  • 48
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang C, Ndassa Y, Summers MF: Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat Struct Biol 2002, 9:537-543.
    • (2002) Nat Struct Biol , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 50
    • 0034653538 scopus 로고    scopus 로고
    • Proline residues in the HIV-1 NH2-terminal capsid domain: Structure determinants for proper core assembly and subsequent steps of early replication
    • Fitzon T, Leschonsky B, Bieler K, Paulus C, Schroder J, Wolf H, Wagner R: Proline residues in the HIV-1 NH2-terminal capsid domain: structure determinants for proper core assembly and subsequent steps of early replication. Virology 2000, 268:294-307.
    • (2000) Virology , vol.268 , pp. 294-307
    • Fitzon, T.1    Leschonsky, B.2    Bieler, K.3    Paulus, C.4    Schroder, J.5    Wolf, H.6    Wagner, R.7
  • 51
    • 0034855639 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells
    • Tang S, Murakami T, Agresta BE, Campbell S, Freed EO, Levin JG: Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells. J Virol 2001, 75:9357-9366.
    • (2001) J Virol , vol.75 , pp. 9357-9366
    • Tang, S.1    Murakami, T.2    Agresta, B.E.3    Campbell, S.4    Freed, E.O.5    Levin, J.G.6
  • 52
    • 0028152426 scopus 로고
    • Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: Structure of the empty capsid assembly intermediate at 2.9 A ° resolution
    • Basavappa R, Syed R, Flore O, Icenogle JP, Filman DJ, Hogle JM: Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A ° resolution. Protein Sci 1994, 3:1651-1669.
    • (1994) Protein Sci , vol.3 , pp. 1651-1669
    • Basavappa, R.1    Syed, R.2    Flore, O.3    Icenogle, J.P.4    Filman, D.J.5    Hogle, J.M.6
  • 53
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC: Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 1998, 95:409-417.
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6


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