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Volumn 88, Issue 4, 2014, Pages 1990-1999

Inhibition of hepatitis C virus production by aptamers against the core protein

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; ANTIBODIES, MONOCLONAL; APTAMERS, NUCLEOTIDE; BLOTTING, WESTERN; CELL LINE; DNA PRIMERS; ENZYME-LINKED IMMUNOSORBENT ASSAY; FLUORESCENT ANTIBODY TECHNIQUE; GENE LIBRARY; HEPACIVIRUS; HUMANS; IMMUNOPRECIPITATION; MICE; PLASMIDS; PROTEIN BINDING; REAL-TIME POLYMERASE CHAIN REACTION; SELEX APTAMER TECHNIQUE; VIRAL CORE PROTEINS; VIRION;

EID: 84893490750     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03312-13     Document Type: Article
Times cited : (42)

References (33)
  • 1
    • 59149085501 scopus 로고    scopus 로고
    • The global burden of hepatitis C
    • Lavanchy D. 2009. The global burden of hepatitis C. Liver Int. 29(Suppl 1):74-81. http://dx.doi.org/10.1111/j.1478-3231.2008.01934.x.
    • (2009) Liver Int. , vol.29 , Issue.SUPPL. 1 , pp. 74-81
    • Lavanchy, D.1
  • 2
    • 16844373963 scopus 로고    scopus 로고
    • Usefulness of the hepatitisCvirus core antigen assay for screening of a population undergoing routine medical checkup
    • Gaudy C, Thevenas C, Tichet J, Mariotte N, Goudeau A, Dubois F. 2005. Usefulness of the hepatitisCvirus core antigen assay for screening of a population undergoing routine medical checkup. J. Clin. Microbiol. 43:1722-1726. http://dx.doi.org/10.1128/JCM.43.4.1722-1726.2005.
    • (2005) J. Clin. Microbiol. , vol.43 , pp. 1722-1726
    • Gaudy, C.1    Thevenas, C.2    Tichet, J.3    Mariotte, N.4    Goudeau, A.5    Dubois, F.6
  • 4
    • 84856032592 scopus 로고    scopus 로고
    • New insights into HCV replication: potential antiviral targets
    • Rice CM. 2011. New insights into HCV replication: potential antiviral targets. Top. Antivir. Med. 19:117-120. http://www.iasusa.org/sites/default/files/tam/19-3-117.pdf.
    • (2011) Top. Antivir. Med. , vol.19 , pp. 117-120
    • Rice, C.M.1
  • 5
    • 67249088420 scopus 로고    scopus 로고
    • Trans-complementation of an NS2 defect in a late step in hepatitis C virus (HCV) particle assembly and maturation
    • Yi M, Ma Y, Yates J, Lemon SM. 2009. Trans-complementation of an NS2 defect in a late step in hepatitis C virus (HCV) particle assembly and maturation. PLoS Pathog. 5:e1000403. http://dx.doi.org/10.1371/journal.ppat.1000403.
    • (2009) PLoS Pathog. , vol.5
    • Yi, M.1    Ma, Y.2    Yates, J.3    Lemon, S.M.4
  • 7
    • 84878524570 scopus 로고    scopus 로고
    • Syndecan-1 serves as the major receptor for attachment of hepatitis C virus to the surfaces of hepatocytes
    • Shi Q, Jiang J, Luo G. 2013. Syndecan-1 serves as the major receptor for attachment of hepatitis C virus to the surfaces of hepatocytes. J. Virol. 87:6866-6875. http://dx.doi.org/10.1128/JVI.03475-12.
    • (2013) J. Virol. , vol.87 , pp. 6866-6875
    • Shi, Q.1    Jiang, J.2    Luo, G.3
  • 8
    • 78651227688 scopus 로고    scopus 로고
    • Core as a novel viral target for hepatitis C drugs
    • Strosberg AD, Kota S, Akahashi TV, Snyder JK, Mousseau G. 2010. Core as a novel viral target for hepatitis C drugs. Virus 2:1734-1751. http://dx.doi.org/10.3390/v2081734.
    • (2010) Virus , vol.2 , pp. 1734-1751
    • Strosberg, A.D.1    Kota, S.2    Akahashi, T.V.3    Snyder, J.K.4    Mousseau, G.5
  • 12
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that binds specific ligands
    • Ellington AD, Szostak JW. 1990. In vitro selection of RNA molecules that binds specific ligands. Nature 346:818-822. http://dx.doi.org/10.1038/346818a0.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 13
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk C, Gold L. 1990. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 249:505-510. http://dx.doi.org/10.1126/science.2200121.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 15
    • 0036893332 scopus 로고    scopus 로고
    • High permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication
    • Blight KJ, McKeating JA, Marcotrigiano J, Rice CM. 2002. High permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. J. Virol. 76:13001-13014. http://dx.doi.org/10.1128/JVI.76.24.13001-13014.2002.
    • (2002) J. Virol. , vol.76 , pp. 13001-13014
    • Blight, K.J.1    McKeating, J.A.2    Marcotrigiano, J.3    Rice, C.M.4
  • 17
    • 84893457029 scopus 로고    scopus 로고
    • Hepatitis C virus core protein detection by DNA aptamer
    • Zhang Z, Zhao Z, Xu L, Wu X, Zhu H, Tan W, Fang X. 2011. Hepatitis C virus core protein detection by DNA aptamer. Scientia Sinica Chimica 41:1312-1318. http://dx.doi.org/10.1360/032011-198.
    • (2011) Scientia Sinica Chimica , vol.41 , pp. 1312-1318
    • Zhang, Z.1    Zhao, Z.2    Xu, L.3    Wu, X.4    Zhu, H.5    Tan, W.6    Fang, X.7
  • 18
    • 84878607908 scopus 로고    scopus 로고
    • 2-Octynoic acid inhibits hepatitis C virus infection through activation of AMPactivated protein kinase
    • Yang D, Xue B, Wang X, Yu X, Liu N, Gao Y, Zhu H. 2013. 2-Octynoic acid inhibits hepatitis C virus infection through activation of AMPactivated protein kinase. PLoS One 8:e64932. http://dx.doi.org/10.1371/journal.pone.0064932.
    • (2013) PLoS One , vol.8
    • Yang, D.1    Xue, B.2    Wang, X.3    Yu, X.4    Liu, N.5    Gao, Y.6    Zhu, H.7
  • 19
    • 80555154422 scopus 로고    scopus 로고
    • Innate immune response of primary human hepatocytes with hepatitis C viral infection
    • Yang D, Liu N, Zuo C, Lei S, Wu X, Zhou F, Liu C, Zhu H. 2011. Innate immune response of primary human hepatocytes with hepatitis C viral infection. PLoS One 6:e27552. http://dx.doi.org/10.1371/journal.pone.0027552.
    • (2011) PLoS One , vol.6
    • Yang, D.1    Liu, N.2    Zuo, C.3    Lei, S.4    Wu, X.5    Zhou, F.6    Liu, C.7    Zhu, H.8
  • 20
    • 49149113893 scopus 로고    scopus 로고
    • Interaction of hepatitis C virus nonstructural protein 5A with core protein is critical for the production of infectious virus particles
    • Masaki T, Suzuki R, Murakami K, Aizaki H, Ishii K, Murayama A, Date T, Matsuura Y, Miyamura T, Wakita T, Suzuki T. 2008. Interaction of hepatitis C virus nonstructural protein 5A with core protein is critical for the production of infectious virus particles. J. Virol. 82:7964-7976. http://dx.doi.org/10.1128/JVI.00826-08.
    • (2008) J. Virol. , vol.82 , pp. 7964-7976
    • Masaki, T.1    Suzuki, R.2    Murakami, K.3    Aizaki, H.4    Ishii, K.5    Murayama, A.6    Date, T.7    Matsuura, Y.8    Miyamura, T.9    Wakita, T.10    Suzuki, T.11
  • 21
    • 80055073369 scopus 로고    scopus 로고
    • Trafficking of hepatitis C virus core protein during virus particle assembly
    • Counihan NA, Rawlison 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    Rawlison, S.M.2    Lindenbach, B.D.3
  • 22
    • 84872000411 scopus 로고    scopus 로고
    • The potential role of HCV core protein antigen testing in diagnosing HCV infection
    • Dawson GJ. 2012. The potential role of HCV core protein antigen testing in diagnosing HCV infection. Antivir. Ther. 17:1431-1435. http://dx.doi.org/10.3851/IMP2463.
    • (2012) Antivir. Ther. , vol.17 , pp. 1431-1435
    • Dawson, G.J.1
  • 23
    • 34248200600 scopus 로고    scopus 로고
    • Chip-based detection of hepatitisCvirus usingRNAaptamers that specifically bind toHCVcore protein
    • Lee S, Kim YS, Jo M, Jin M, Lee DK, Kim S. 2007. Chip-based detection of hepatitisCvirus usingRNAaptamers that specifically bind toHCVcore protein. Biochem. Biophys. Res. Commun. 358:47-52. http://dx.doi.org/10.1016/j.bbrc.2007.04.057.
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 47-52
    • Lee, S.1    Kim, Y.S.2    Jo, M.3    Jin, M.4    Lee, D.K.5    Kim, S.6
  • 24
    • 80052123459 scopus 로고    scopus 로고
    • Differential efficacy of protease inhibitors againstHCVgenotypes 2a, 3a, 5a, and 6a NS3/4A protease recombinant virus
    • Gottwein JM, Scheel TK, Jensen TB, Ghanem L, Bukh J. 2011. Differential efficacy of protease inhibitors againstHCVgenotypes 2a, 3a, 5a, and 6a NS3/4A protease recombinant virus. Gastroenterology 141:1067-1079. http://dx.doi.org/10.1053/j.gastro.2011.06.004.
    • (2011) Gastroenterology , vol.141 , pp. 1067-1079
    • Gottwein, J.M.1    Scheel, T.K.2    Jensen, T.B.3    Ghanem, L.4    Bukh, J.5
  • 25
    • 79958830099 scopus 로고    scopus 로고
    • Hepatitis C virus resistance to protease inhibitors
    • Halfon P, Locarnini S. 2011. Hepatitis C virus resistance to protease inhibitors. J. Hepatol. 55:192-206. http://dx.doi.org/10.1016/j.jhep.2011.01.011.
    • (2011) J. Hepatol. , vol.55 , pp. 192-206
    • Halfon, P.1    Locarnini, S.2
  • 26
    • 84862897605 scopus 로고    scopus 로고
    • Characterization of naturally occurring protease inhibitor-resistance mutations in genotype 1b hepatitis C virus patients
    • Shindo H, Maekawa S, Komase K, Sueki R, Miura M, Kadokura M, Shindo K. 2012. Characterization of naturally occurring protease inhibitor-resistance mutations in genotype 1b hepatitis C virus patients. Hepatol. Int. 6:482-490. http://dx.doi.org/10.1007/s12072-011-9306-7.
    • (2012) Hepatol. Int. , vol.6 , pp. 482-490
    • Shindo, H.1    Maekawa, S.2    Komase, K.3    Sueki, R.4    Miura, M.5    Kadokura, M.6    Shindo, K.7
  • 27
    • 78650066594 scopus 로고    scopus 로고
    • RNA aptamers directed to human immunodeficiency virus type 1 Gag protein bind to matrix and nucleocapsid domains and inhibit virus production
    • Ramalingam D, Duclair S, Datta SAK, Ellington A, Rein A, Prasad VR. 2011. RNA aptamers directed to human immunodeficiency virus type 1 Gag protein bind to matrix and nucleocapsid domains and inhibit virus production. J. Virol. 85:305-314. http://dx.doi.org/10.1128/JVI.02626-09.
    • (2011) J. Virol. , vol.85 , pp. 305-314
    • Ramalingam, D.1    Duclair, S.2    Datta, S.A.K.3    Ellington, A.4    Rein, A.5    Prasad, V.R.6
  • 29
    • 84859336804 scopus 로고    scopus 로고
    • 5-Triphosphate-RNA-independent activation of RIG-I via RNA aptamer with enhanced antiviral activity
    • Hwang SY, Sun HY, Lee KH, Oh BH, Cha YJ, Kim BH, Yoo JY. 2012. 5-Triphosphate-RNA-independent activation of RIG-I via RNA aptamer with enhanced antiviral activity. Nucleic Acids Res. 40:2724-2733. http://dx.doi.org/10.1093/nar/gkr1098.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2724-2733
    • Hwang, S.Y.1    Sun, H.Y.2    Lee, K.H.3    Oh, B.H.4    Cha, Y.J.5    Kim, B.H.6    Yoo, J.Y.7
  • 30
    • 84857069862 scopus 로고    scopus 로고
    • Formation of higher-order foot-and-mouth disease virus 3Dpol complexes is dependent on elongation activity
    • Bentham M, Holmes K, Forrest S, Rowlands DJ, Stonehouse NJ. 2012. Formation of higher-order foot-and-mouth disease virus 3Dpol complexes is dependent on elongation activity. J. Virol. 86:2371-2374. http://dx.doi.org/10.1128/JVI.05696-11.
    • (2012) J. Virol. , vol.86 , pp. 2371-2374
    • Bentham, M.1    Holmes, K.2    Forrest, S.3    Rowlands, D.J.4    Stonehouse, N.J.5
  • 31
    • 78951493762 scopus 로고    scopus 로고
    • Protection of HIV neutralizing aptamers against rectal and vaginal nucleases: implications for RNAbased therapeutics
    • Moore MD, Cookson J, Coventry VK, Sproat B, Rabe L, Cranston RD, McGowan I, James W. 2011. Protection of HIV neutralizing aptamers against rectal and vaginal nucleases: implications for RNAbased therapeutics. J. Biol. Chem. 286:2526-2535. http://dx.doi.org/10.1074/jbc.M110.178426.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2526-2535
    • Moore, M.D.1    Cookson, J.2    Coventry, V.K.3    Sproat, B.4    Rabe, L.5    Cranston, R.D.6    McGowan, I.7    James, W.8
  • 32
    • 48249122367 scopus 로고    scopus 로고
    • Liquid-crystal NMR structure of HIV TARRNAbound to its SELEXRNAaptamer reveals the origins of the high stability of the complex
    • Van Melckebeke H, Devany M, Di Primo C, Beaurain F, Toulme JJ, Bryce DL, Boisbouvier J. 2008. Liquid-crystal NMR structure of HIV TARRNAbound to its SELEXRNAaptamer reveals the origins of the high stability of the complex. Proc. Natl. Acad. Sci. U.S.A. 105:9210-9215. http://dx.doi.org/10.1073/pnas.0712121105.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9210-9215
    • Van Melckebeke, H.1    Devany, M.2    Di Primo, C.3    Beaurain, F.4    Toulme, J.J.5    Bryce, D.L.6    Boisbouvier, J.7


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