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Volumn 5, Issue 5, 2014, Pages

A comprehensive functional map of the hepatitis C virus genome provides a resource for probing viral proteins

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; NONSTRUCTURAL PROTEIN 4B; VIRUS PROTEIN; TRANSPOSON; VIRUS DNA;

EID: 84908409935     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01469-14     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 84879413726 scopus 로고    scopus 로고
    • Transposon insertion sequencing: A new tool for systems-level analysis of microorganisms
    • van Opijnen T, Camilli A. 2013. Transposon insertion sequencing: a new tool for systems-level analysis of microorganisms. Nat. Rev. Microbiol. 11:435-442. http://dx.doi.org/10.1038/nrmicro3033.
    • (2013) Nat. Rev. Microbiol , vol.11 , pp. 435-442
    • van Opijnen, T.1    Camilli, A.2
  • 2
    • 0036228849 scopus 로고    scopus 로고
    • Functional genomics on potato virus A: Virus genome-wide map of sites essential for virus propagation
    • Kekarainen T, Savilahti H, Valkonen JP. 2002. Functional genomics on potato virus A: virus genome-wide map of sites essential for virus propagation. Genome Res. 12:584-594. http://dx.doi.org/10.1101/gr.220702.
    • (2002) Genome Res , vol.12 , pp. 584-594
    • Kekarainen, T.1    Savilahti, H.2    Valkonen, J.P.3
  • 4
    • 78449246344 scopus 로고    scopus 로고
    • Highresolution functional mapping of the Venezuelan equine encephalitis virus genome by insertional mutagenesis and massively parallel sequencing
    • Beitzel BF, Bakken RR, Smith JM, Schmaljohn CS. 2010. Highresolution functional mapping of the Venezuelan equine encephalitis virus genome by insertional mutagenesis and massively parallel sequencing. PLoS Pathog. 6:e1001146. http://dx.doi.org/10.1371/journal.ppat.1001146.
    • (2010) PLoS Pathog , vol.6
    • Beitzel, B.F.1    Bakken, R.R.2    Smith, J.M.3    Schmaljohn, C.S.4
  • 5
    • 84869052451 scopus 로고    scopus 로고
    • High-resolution functional profiling of the norovirus genome
    • Thorne L, Bailey D, Goodfellow I. 2012. High-resolution functional profiling of the norovirus genome. J. Virol. 86:11441-11456. http:// dx.doi.org/10.1128/JVI.00439-12.
    • (2012) J. Virol , vol.86 , pp. 11441-11456
    • Thorne, L.1    Bailey, D.2    Goodfellow, I.3
  • 6
    • 84890281675 scopus 로고    scopus 로고
    • Genome-wide mutagenesis of influenza virus reveals unique plasticity of the hemagglutinin and NS1 proteins
    • Heaton NS, Sachs D, Chen CJ, Hai R, Palese P. 2013. Genome-wide mutagenesis of influenza virus reveals unique plasticity of the hemagglutinin and NS1 proteins. Proc. Natl. Acad. Sci. U. S. A. 110:20248-20253. http://dx.doi.org/10.1073/pnas.1320524110.
    • (2013) Proc. Natl. Acad. Sci. U. S. A , vol.110 , pp. 20248-20253
    • Heaton, N.S.1    Sachs, D.2    Chen, C.J.3    Hai, R.4    Palese, P.5
  • 7
    • 34250679750 scopus 로고    scopus 로고
    • Epidemiology of hepatitis C virus infection
    • Alter MJ. 2007. Epidemiology of hepatitis C virus infection. World J. Gastroenterol. 13:2436 -2441. http://dx.doi.org/10.3748/ wjg.v13.i17.2436.
    • (2007) World J. Gastroenterol , vol.13 , pp. 2436-2441
    • Alter, M.J.1
  • 10
    • 23944476834 scopus 로고    scopus 로고
    • Unravelling hepatitis C virus replication from genome to function
    • Lindenbach BD, Rice CM. 2005. Unravelling hepatitis C virus replication from genome to function. Nature 436:933-938. http://dx.doi.org/ 10.1038/nature04077.
    • (2005) Nature , vol.436 , pp. 933-938
    • Lindenbach, B.D.1    Rice, C.M.2
  • 12
    • 0345188811 scopus 로고    scopus 로고
    • Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line
    • Lohmann V, Körner F, Koch J, Herian U, Theilmann L, Bartenschlager R. 1999. Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science 285:110 -113. http://dx.doi.org/10.1126/ science.285.5424.110.
    • (1999) Science , vol.285 , pp. 110-113
    • Lohmann, V.1    Körner, F.2    Koch, J.3    Herian, U.4    Theilmann, L.5    Bartenschlager, R.6
  • 13
    • 84873032687 scopus 로고    scopus 로고
    • Subcellular localization and function of an epitope-tagged p7 viroporin in hepatitis C virus-producing cells
    • Vieyres G, Brohm C, Friesland M, Gentzsch J, Wölk B, Roingeard P, Steinmann E, Pietschmann T. 2013. Subcellular localization and function of an epitope-tagged p7 viroporin in hepatitis C virus-producing cells. J. Virol. 87:1664-1678. http://dx.doi.org/10.1128/JVI.02782-12.
    • (2013) J. Virol , vol.87 , pp. 1664-1678
    • Vieyres, G.1    Brohm, C.2    Friesland, M.3    Gentzsch, J.4    Wölk, B.5    Roingeard, P.6    Steinmann, E.7    Pietschmann, T.8
  • 14
    • 0034623816 scopus 로고    scopus 로고
    • Efficient initiation of HCV RNA replication in cell culture
    • Blight KJ, Kolykhalov AA, Rice CM. 2000. Efficient initiation of HCV RNA replication in cell culture. Science 290:1972-1974. http://dx.doi.org/ 10.1126/science.290.5498.1972.
    • (2000) Science , vol.290 , pp. 1972-1974
    • Blight, K.J.1    Kolykhalov, A.A.2    Rice, C.M.3
  • 15
    • 84876570860 scopus 로고    scopus 로고
    • Virion assembly and release
    • Lindenbach BD. 2013. Virion assembly and release. Curr. Top. Microbiol. Immunol. 369:199 -218. http://dx.doi.org/10.1007/978-3-642-27340-7 _8.
    • (2013) Curr. Top. Microbiol. Immunol , vol.369 , pp. 199-218
    • Lindenbach, B.D.1
  • 16
    • 77649175920 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural protein 4B: A journey into unexplored territory
    • Gouttenoire J, Penin F, Moradpour D. 2010. Hepatitis C virus nonstructural protein 4B: a journey into unexplored territory. Rev. Med. Virol. 20:117-129. http://dx.doi.org/10.1002/rmv.640.
    • (2010) Rev. Med. Virol , vol.20 , pp. 117-129
    • Gouttenoire, J.1    Penin, F.2    Moradpour, D.3
  • 17
    • 84880380982 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus genome encapsidation by nonstructural protein 4B
    • Han Q, Manna D, Belton K, Cole R, Konan KV. 2013. Modulation of hepatitis C virus genome encapsidation by nonstructural protein 4B. J. Virol. 87:7409-7422. http://dx.doi.org/10.1128/JVI.03523-12.
    • (2013) J. Virol , vol.87 , pp. 7409-7422
    • Han, Q.1    Manna, D.2    Belton, K.3    Cole, R.4    Konan, K.V.5
  • 18
    • 60049083503 scopus 로고    scopus 로고
    • The hepatitis C virus NS4B protein can trans-complement viral RNA replication and modulates production of infectious virus
    • Jones DM, Patel AH, Targett-Adams P, McLauchlan J. 2009. The hepatitis C virus NS4B protein can trans-complement viral RNA replication and modulates production of infectious virus. J. Virol. 83:2163-2177. http://dx.doi.org/10.1128/JVI.01885-08.
    • (2009) J. Virol , vol.83 , pp. 2163-2177
    • Jones, D.M.1    Patel, A.H.2    Targett-Adams, P.3    McLauchlan, J.4
  • 19
    • 79960406328 scopus 로고    scopus 로고
    • NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes
    • Paul D, Romero-Brey I, Gouttenoire J, Stoitsova S, Krijnse-Locker J, Moradpour D, Bartenschlager R. 2011. NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes. J. Virol. 85:6963- 6976. http://dx.doi.org/10.1128/JVI.00502-11.
    • (2011) J. Virol , vol.85 , pp. 6963-6976
    • Paul, D.1    Romero-Brey, I.2    Gouttenoire, J.3    Stoitsova, S.4    Krijnse-Locker, J.5    Moradpour, D.6    Bartenschlager, R.7
  • 20
    • 84864391185 scopus 로고    scopus 로고
    • Structural analysis of hepatitis C virus core-E1 signal peptide and requirements for cleavage of the genotype 3a signal sequence by signal peptide peptidase
    • Oehler V, Filipe A, Montserret R, da Costa D, Brown G, Penin F, McLauchlan J. 2012. Structural analysis of hepatitis C virus core-E1 signal peptide and requirements for cleavage of the genotype 3a signal sequence by signal peptide peptidase. J. Virol. 86:7818 -7828. http://dx.doi.org/ 10.1128/JVI.00457-12.
    • (2012) J. Virol , vol.86 , pp. 7818-7828
    • Oehler, V.1    Filipe, A.2    Montserret, R.3    da Costa, D.4    Brown, G.5    Penin, F.6    McLauchlan, J.7
  • 21
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace CN, Scholtz JM. 1998. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 75:422- 427. http:// dx.doi.org/10.1016/S0006-3495(98)77529-0.
    • (1998) Biophys. J , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 22
    • 84879695534 scopus 로고    scopus 로고
    • Unusual architecture of the p7 channel from hepatitis C virus
    • OuYang B, Xie S, Berardi MJ, Zhao X, Dev J, Yu W, Sun B, Chou JJ. 2013. Unusual architecture of the p7 channel from hepatitis C virus. Nature 498:521-525. http://dx.doi.org/10.1038/nature12283.
    • (2013) Nature , vol.498 , pp. 521-525
    • OuYang, B.1    Xie, S.2    Berardi, M.J.3    Zhao, X.4    Dev, J.5    Yu, W.6    Sun, B.7    Chou, J.J.8
  • 24
    • 78651252353 scopus 로고    scopus 로고
    • Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly
    • Jirasko V, Montserret R, Lee JY, Gouttenoire J, Moradpour D, Penin F, Bartenschlager R. 2010. Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly. PLoS Pathog. 6:e1001233. http://dx.doi.org/10.1371/ journal.ppat.1001233.
    • (2010) PLoS Pathog , vol.6
    • Jirasko, V.1    Montserret, R.2    Lee, J.Y.3    Gouttenoire, J.4    Moradpour, D.5    Penin, F.6    Bartenschlager, R.7
  • 26
    • 78649445875 scopus 로고    scopus 로고
    • Identification of tolerated insertion sites in poliovirus non-structural proteins
    • Teterina NL, Lauber C, Jensen KS, Levenson EA, Gorbalenya AE, Ehrenfeld E. 2011. Identification of tolerated insertion sites in poliovirus non-structural proteins. Virology 409:1-11. http://dx.doi.org/10.1016/ j.virol.2010.09.028.
    • (2011) Virology , vol.409 , pp. 1-11
    • Teterina, N.L.1    Lauber, C.2    Jensen, K.S.3    Levenson, E.A.4    Gorbalenya, A.E.5    Ehrenfeld, E.6
  • 27
    • 79955398622 scopus 로고    scopus 로고
    • Analysis of poliovirus protein 3A interactions with viral and cellular proteins in infected cells
    • Teterina NL, Pinto Y, Weaver JD, Jensen KS, Ehrenfeld E. 2011. Analysis of poliovirus protein 3A interactions with viral and cellular proteins in infected cells. J. Virol. 85:4284-4296. http://dx.doi.org/10.1128/ JVI.02398-10.
    • (2011) J. Virol , vol.85 , pp. 4284-4296
    • Teterina, N.L.1    Pinto, Y.2    Weaver, J.D.3    Jensen, K.S.4    Ehrenfeld, E.5
  • 28
    • 77949810354 scopus 로고    scopus 로고
    • Challenging the limit: NMR assignment of a 31 kDa helical membrane protein
    • Huang C, Mohanty S. 2010. Challenging the limit: NMR assignment of a 31 kDa helical membrane protein. J. Am. Chem. Soc. 132:3662-3663. http://dx.doi.org/10.1021/ja100078z.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 3662-3663
    • Huang, C.1    Mohanty, S.2
  • 29
    • 3142764760 scopus 로고    scopus 로고
    • Insertion of green fluorescent protein into nonstructural protein 5A allows direct visualization of functional hepatitis C virus replication complexes
    • Moradpour D, Evans MJ, Gosert R, Yuan Z, Blum HE, Goff SP, Lindenbach BD, Rice CM. 2004. Insertion of green fluorescent protein into nonstructural protein 5A allows direct visualization of functional hepatitis C virus replication complexes. J. Virol. 78:7400-7409. http:// dx.doi.org/10.1128/JVI.78.14.7400-7409.2004.
    • (2004) J. Virol , vol.78 , pp. 7400-7409
    • Moradpour, D.1    Evans, M.J.2    Gosert, R.3    Yuan, Z.4    Blum, H.E.5    Goff, S.P.6    Lindenbach, B.D.7    Rice, C.M.8
  • 30
    • 84864007958 scopus 로고    scopus 로고
    • Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5A
    • Nevo-Yassaf I, Yaffe Y, Asher M, Ravid O, Eizenberg S, Henis YI, Nahmias Y, Hirschberg K, Sklan EH. 2012. Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5A. J. Virol. 86:6491- 6502. http://dx.doi.org/ 10.1128/JVI.00496-12.
    • (2012) J. Virol , vol.86 , pp. 6491-6502
    • Nevo-Yassaf, I.1    Yaffe, Y.2    Asher, M.3    Ravid, O.4    Eizenberg, S.5    Henis, Y.I.6    Nahmias, Y.7    Hirschberg, K.8    Sklan, E.H.9
  • 31
    • 55249090938 scopus 로고    scopus 로고
    • A dynamic view of hepatitis C virus replication complexes
    • Wölk B, Büchele B, Moradpour D, Rice CM. 2008. A dynamic view of hepatitis C virus replication complexes. J. Virol. 82:10519-10531. http:// dx.doi.org/10.1128/JVI.00640-08.
    • (2008) J. Virol , vol.82 , pp. 10519-10531
    • Wölk, B.1    Büchele, B.2    Moradpour, D.3    Rice, C.M.4
  • 32
    • 78650062692 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteins
    • Ma Y, Anantpadma M, Timpe JM, Shanmugam S, Singh SM, Lemon SM, Yi M. 2011. Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteins. J. Virol. 85:86-97. http://dx.doi.org/10.1128/JVI.01070-10.
    • (2011) J. Virol , vol.85 , pp. 86-97
    • Ma, Y.1    Anantpadma, M.2    Timpe, J.M.3    Shanmugam, S.4    Singh, S.M.5    Lemon, S.M.6    Yi, M.7
  • 35
    • 78650270216 scopus 로고    scopus 로고
    • Hepatitis C virus expressing flag-tagged envelope protein 2 has unaltered infectivity and density, is specifically neutralized by flag antibodies and can be purified by affinity chromatography
    • Prentoe J, Bukh J. 2011. Hepatitis C virus expressing flag-tagged envelope protein 2 has unaltered infectivity and density, is specifically neutralized by flag antibodies and can be purified by affinity chromatography. Virology 409:148-155. http://dx.doi.org/10.1016/j.virol.2010.10.034.
    • (2011) Virology , vol.409 , pp. 148-155
    • Prentoe, J.1    Bukh, J.2
  • 36
    • 78951472458 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes
    • Stapleford KA, Lindenbach BD. 2011. Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes. J. Virol. 85:1706 -1717. http://dx.doi.org/10.1128/JVI.02268-10.
    • (2011) J. Virol , vol.85 , pp. 1706-1717
    • Stapleford, K.A.1    Lindenbach, B.D.2
  • 38
    • 37549005607 scopus 로고    scopus 로고
    • The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly
    • Shavinskaya A, Boulant S, Penin F, McLauchlan J, Bartenschlager R. 2007. The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly. J. Biol. Chem. 282: 37158-37169. http://dx.doi.org/10.1074/jbc.M707329200.
    • (2007) J. Biol. Chem , vol.282 , pp. 37158-37169
    • Shavinskaya, A.1    Boulant, S.2    Penin, F.3    McLauchlan, J.4    Bartenschlager, R.5
  • 39
    • 80055073369 scopus 로고    scopus 로고
    • Trafficking of hepatitis C virus core protein during virus particle assembly
    • Counihan NA, Rawlinson SM, Lindenbach BD. 2011. Trafficking of hepatitis C virus core protein during virus particle assembly. PLoS Pathog. 7:e1002302. http://dx.doi.org/10.1371/journal.ppat.1002302.
    • (2011) PLoS Pathog , vol.7
    • Counihan, N.A.1    Rawlinson, S.M.2    Lindenbach, B.D.3
  • 40
    • 84884186559 scopus 로고    scopus 로고
    • Analysis of hepatitis C virus core/NS5A protein co-localization using novel cell culture systems expressing core-NS2 and NS5A of genotypes 1-7
    • Galli A, Scheel TK, Prentoe JC, Mikkelsen LS, Gottwein JM, Bukh J. 2013. Analysis of hepatitis C virus core/NS5A protein co-localization using novel cell culture systems expressing core-NS2 and NS5A of genotypes 1-7. J. Gen. Virol. 94:2221-2235. http://dx.doi.org/10.1099/vir.0.053868 -0.
    • (2013) J. Gen. Virol , vol.94 , pp. 2221-2235
    • Galli, A.1    Scheel, T.K.2    Prentoe, J.C.3    Mikkelsen, L.S.4    Gottwein, J.M.5    Bukh, J.6
  • 41
    • 84908429857 scopus 로고    scopus 로고
    • Visualization and analysis of hepatitis C virus structural proteins at lipid droplets by superresolution microscopy
    • Eggert D, Rosch K, Reimer R, Herker E. 2014. Visualization and analysis of hepatitis C virus structural proteins at lipid droplets by superresolution microscopy. PLoS One 9:e102511. http://dx.doi.org/10.1371/ journal.pone.0102511.
    • (2014) PLoS One , vol.9
    • Eggert, D.1    Rosch, K.2    Reimer, R.3    Herker, E.4
  • 42
    • 80052056964 scopus 로고    scopus 로고
    • Conserved GXXXG- and S/T-like motifs in the transmembrane domains of NS4B protein are required for hepatitis C virus replication
    • Han Q, Aligo J, Manna D, Belton K, Chintapalli SV, Hong Y, Patterson RL, van Rossum DB, Konan KV. 2011. Conserved GXXXG- and S/T-like motifs in the transmembrane domains of NS4B protein are required for hepatitis C virus replication. J. Virol. 85:6464-6479. http://dx.doi.org/ 10.1128/JVI.02298-10.
    • (2011) J. Virol , vol.85 , pp. 6464-6479
    • Han, Q.1    Aligo, J.2    Manna, D.3    Belton, K.4    Chintapalli, S.V.5    Hong, Y.6    Patterson, R.L.7    van Rossum, D.B.8    Konan, K.V.9
  • 43
    • 4644281168 scopus 로고    scopus 로고
    • An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication
    • Elazar M, Liu P, Rice CM, Glenn JS. 2004. An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication. J. Virol. 78:11393-11400. http://dx.doi.org/10.1128/ JVI.78.20.11393-11400.2004.
    • (2004) J. Virol , vol.78 , pp. 11393-11400
    • Elazar, M.1    Liu, P.2    Rice, C.M.3    Glenn, J.S.4
  • 44
    • 70350330475 scopus 로고    scopus 로고
    • An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association
    • Gouttenoire J, Montserret R, Kennel A, Penin F, Moradpour D. 2009. An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association. J. Virol. 83: 11378-11384. http://dx.doi.org/10.1128/JVI.01122-09.
    • (2009) J. Virol , vol.83 , pp. 11378-11384
    • Gouttenoire, J.1    Montserret, R.2    Kennel, A.3    Penin, F.4    Moradpour, D.5
  • 45
    • 79961196705 scopus 로고    scopus 로고
    • Charged residues in hepatitis C virus NS4B are critical for multiple NS4B functions in RNA replication
    • Blight KJ. 2011. Charged residues in hepatitis C virus NS4B are critical for multiple NS4B functions in RNA replication. J. Virol. 85:8158-8171. http://dx.doi.org/10.1128/JVI.00858-11.
    • (2011) J. Virol , vol.85 , pp. 8158-8171
    • Blight, K.J.1
  • 46
    • 84892479515 scopus 로고    scopus 로고
    • In vitro systems for the study of hepatitis C virus infection
    • Wilson GK, Stamataki Z. 2012. In vitro systems for the study of hepatitis C virus infection. Int. J. Hepatol. 2012:292591.
    • (2012) Int. J. Hepatol , vol.2012
    • Wilson, G.K.1    Stamataki, Z.2


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