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Volumn 32, Issue 14, 2004, Pages 4377-4389

SELEX-derived aptamers of the duck hepatitis B virus RNA encapsidation signal distinguish critical and non-critical residues for productive initiation of reverse transcription

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; CAPSID PROTEIN; RNA BINDING PROTEIN; RNA DIRECTED DNA POLYMERASE; VIRUS RNA; OLIGORIBONUCLEOTIDE;

EID: 4043152931     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh772     Document Type: Article
Times cited : (31)

References (49)
  • 1
    • 0030740450 scopus 로고    scopus 로고
    • Hepatitis B virus, the vaccine, and the control of primary cancer of the liver
    • Blumberg,B.S. (1997) Hepatitis B virus, the vaccine, and the control of primary cancer of the liver. Proc. Natl Acad. Sci. USA, 94, 7121-7125.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7121-7125
    • Blumberg, B.S.1
  • 2
    • 0032845490 scopus 로고    scopus 로고
    • Hepatitis B virus replication: Novel roles for virus-host interactions
    • Nassal,M. (1999) Hepatitis B virus replication: novel roles for virus-host interactions. Intervirology, 42, 100-116.
    • (1999) Intervirology , vol.42 , pp. 100-116
    • Nassal, M.1
  • 3
    • 0001903859 scopus 로고    scopus 로고
    • Macromolecular interactions in hepatitis B virus replication and particle assembly
    • Cann,A.J. (ed.), Oxford University Press, Oxford, UK
    • Nassal,M. (2000) Macromolecular interactions in hepatitis B virus replication and particle assembly. In Cann,A.J. (ed.), DNA Virus Replication. Oxford University Press, Oxford, UK, Vol. 26, pp. 1-40.
    • (2000) DNA Virus Replication , vol.26 , pp. 1-40
    • Nassal, M.1
  • 4
    • 0001435504 scopus 로고    scopus 로고
    • Hepadnaviridae: The viruses and their replication
    • Fields,B.N. et al. (eds) 4th edn Lippincott Williams & Wilkins, Philadelphia, PA
    • Ganem,D. and Schneider,R. (2001) Hepadnaviridae: the viruses and their replication. In Fields,B.N. et al. (eds) Fields Virology, 4th edn Lippincott Williams & Wilkins, Philadelphia, PA
    • (2001) Fields Virology
    • Ganem, D.1    Schneider, R.2
  • 5
    • 0002687402 scopus 로고
    • Origin and evolutionary relationships of retroelements
    • Morse,S.S (ed.), Raven Press, New York, NY
    • Eickbush,T.H. (1994) Origin and evolutionary relationships of retroelements. In Morse,S.S. (ed.), The Evolutionary Biology of Viruses. Raven Press, New York, NY, pp. 121-160.
    • (1994) The Evolutionary Biology of Viruses , pp. 121-160
    • Eickbush, T.H.1
  • 6
    • 0035041976 scopus 로고    scopus 로고
    • Molecular modeling and biochemical characterization reveal the mechanism of hepatitis B virus polymerase resistance to lamivudine (3TC) and emtricitabine (FTC)
    • Das,K., Xiong,X., Yang,H., Westland,C.E., Gibbs,C.S., Sarafianos,S.G. and Arnold,E. (2001) Molecular modeling and biochemical characterization reveal the mechanism of hepatitis B virus polymerase resistance to lamivudine (3TC) and emtricitabine (FTC). J. Virol., 75, 4771-4779.
    • (2001) J. Virol. , vol.75 , pp. 4771-4779
    • Das, K.1    Xiong, X.2    Yang, H.3    Westland, C.E.4    Gibbs, C.S.5    Sarafianos, S.G.6    Arnold, E.7
  • 7
    • 0036529639 scopus 로고    scopus 로고
    • dNTP versus NTP discrimination by phenylalanine 451 in duck hepatitis B virus P protein indicates a common structure of the dNTP-binding pocket with other reverse transcriptases
    • Beck,J., Vogel,M. and Nassal,M. (2002) dNTP versus NTP discrimination by phenylalanine 451 in duck hepatitis B virus P protein indicates a common structure of the dNTP-binding pocket with other reverse transcriptases. Nucleic Acids Res., 30, 1679-1687.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1679-1687
    • Beck, J.1    Vogel, M.2    Nassal, M.3
  • 8
    • 0026493753 scopus 로고
    • The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis
    • Wang,G.H. and Seeger,C. (1992) The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell, 71, 663-670.
    • (1992) Cell , vol.71 , pp. 663-670
    • Wang, G.H.1    Seeger, C.2
  • 9
    • 0027323570 scopus 로고
    • The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function
    • Knaus,T. and Nassal,M. (1993) The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function. Nucleic Acids Res., 21, 3967-3975.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3967-3975
    • Knaus, T.1    Nassal, M.2
  • 10
    • 0028095240 scopus 로고
    • Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis
    • Pollack,J.R. and Ganem,D. (1994) Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis. J. Virol., 68, 5579-5587.
    • (1994) J. Virol. , vol.68 , pp. 5579-5587
    • Pollack, J.R.1    Ganem, D.2
  • 11
    • 0028300388 scopus 로고
    • Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription
    • Weber,M., Bronsema,V., Bartos,H., Bosserhoff,A., Bartenschlager,R. and Schaller,H. (1994) Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. J. Virol., 68, 2994-2999.
    • (1994) J. Virol. , vol.68 , pp. 2994-2999
    • Weber, M.1    Bronsema, V.2    Bartos, H.3    Bosserhoff, A.4    Bartenschlager, R.5    Schaller, H.6
  • 12
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu,J. and Seeger,C. (1996) Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl Acad. Sci. USA, 93, 1060-1064.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 13
    • 0031018112 scopus 로고    scopus 로고
    • Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
    • Hu,J., Toft,D.O. and Seeger,C. (1997) Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J., 16, 59-68.
    • (1997) EMBO J. , vol.16 , pp. 59-68
    • Hu, J.1    Toft, D.O.2    Seeger, C.3
  • 14
    • 0034468780 scopus 로고    scopus 로고
    • In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: Posttranslational activation by Hsp90
    • Hu,J. and Anselmo,D. (2000) In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90. J. Virol., 74, 11447-11455.
    • (2000) J. Virol. , vol.74 , pp. 11447-11455
    • Hu, J.1    Anselmo, D.2
  • 15
    • 0034909748 scopus 로고    scopus 로고
    • Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli
    • Beck,J. and Nassal,M. (2001) Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli. J. Virol., 75, 7410-7419.
    • (2001) J. Virol. , vol.75 , pp. 7410-7419
    • Beck, J.1    Nassal, M.2
  • 16
    • 0141815723 scopus 로고    scopus 로고
    • Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatits B virus reverse transcriptase, an assumed Hsp90 client protein
    • Beck,J. and Nassal,M. (2003) Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatits B virus reverse transcriptase, an assumed Hsp90 client protein. J. Biol. Chem., 278, 36128-36138.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36128-36138
    • Beck, J.1    Nassal, M.2
  • 17
    • 0036133258 scopus 로고    scopus 로고
    • In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins
    • Hu,J., Toft,D., Anselmo,D. and Wang,X. (2002) In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins. J. Virol., 76, 269-279.
    • (2002) J. Virol. , vol.76 , pp. 269-279
    • Hu, J.1    Toft, D.2    Anselmo, D.3    Wang, X.4
  • 18
    • 0030908648 scopus 로고    scopus 로고
    • Sequence- and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses
    • Beck,J. and Nassal,M. (1997) Sequence- and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses. J. Virol., 71, 4971-4980.
    • (1997) J. Virol. , vol.71 , pp. 4971-4980
    • Beck, J.1    Nassal, M.2
  • 19
    • 0033621452 scopus 로고    scopus 로고
    • A small 2′-OH- and base-dependent recognition element downstream of the initiation site in the RNA encapsidation signal is essential for hepatitis B virus replication initiation
    • Schaaf,S.G., Beck,J. and Nassal,M. (1999) A small 2′-OH- and base-dependent recognition element downstream of the initiation site in the RNA encapsidation signal is essential for hepatitis B virus replication initiation. J. Biol. Chem., 274, 37787-37794.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37787-37794
    • Schaaf, S.G.1    Beck, J.2    Nassal, M.3
  • 20
    • 0031774329 scopus 로고    scopus 로고
    • Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template
    • Beck,J. and Nassal,M. (1998) Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template. Mol. Cell. Biol., 18, 6265-6272.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6265-6272
    • Beck, J.1    Nassal, M.2
  • 21
    • 0036849272 scopus 로고    scopus 로고
    • The apical stem-loop of the hepatitis B virus encapsidation signal folds into a stable tri-loop with two underlying pyrimidine bulges
    • Flodell,S., Schleucher,J., Cromsigt,J., Ippel,H., Kidd-Ljunggren,K. and Wijmenga,S. (2002) The apical stem-loop of the hepatitis B virus encapsidation signal folds into a stable tri-loop with two underlying pyrimidine bulges. Nucleic Acids Res., 30, 4803-4811.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4803-4811
    • Flodell, S.1    Schleucher, J.2    Cromsigt, J.3    Ippel, H.4    Kidd-Ljunggren, K.5    Wijmenga, S.6
  • 22
    • 0023803399 scopus 로고
    • Isolation and characterization of a hepatitis B virus endemic in herons
    • Sprengel,R., Kaleta,E.F. and Will,H. (1988) Isolation and characterization of a hepatitis B virus endemic in herons. J. Virol., 62, 3832-3839.
    • (1988) J. Virol. , vol.62 , pp. 3832-3839
    • Sprengel, R.1    Kaleta, E.F.2    Will, H.3
  • 23
    • 0031579235 scopus 로고    scopus 로고
    • Experimental confirmation of a hepatitis B virus (HBV) epsilon-like bulge-and-loop structure in avian HBV RNA encapsidation signals
    • Beck,J., Bartos,H. and Nassal,M. (1997) Experimental confirmation of a hepatitis B virus (HBV) epsilon-like bulge-and-loop structure in avian HBV RNA encapsidation signals. Virology, 227, 500-504.
    • (1997) Virology , vol.227 , pp. 500-504
    • Beck, J.1    Bartos, H.2    Nassal, M.3
  • 24
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl,F.U. and Hayer-Hartl,M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science, 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 25
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk,C. and Gold,L. (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science, 249, 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 26
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington,A.D. and Szostak,J.W. (1990) In vitro selection of RNA molecules that bind specific ligands. Nature, 346, 818-822.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 27
    • 0032853242 scopus 로고    scopus 로고
    • In vitro selection of functional nucleic acids
    • Wilson,D.S. and Szostak,J.W. (1999) In vitro selection of functional nucleic acids. Annu. Rev. Biochem., 68, 611-647.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 611-647
    • Wilson, D.S.1    Szostak, J.W.2
  • 28
    • 0005620475 scopus 로고    scopus 로고
    • Aptamers as therapeutic and diagnostic agents
    • Brody,E.N. and Gold,L. (2000) Aptamers as therapeutic and diagnostic agents. J. Biotechnol., 74, 5-13.
    • (2000) J. Biotechnol. , vol.74 , pp. 5-13
    • Brody, E.N.1    Gold, L.2
  • 29
    • 0029912764 scopus 로고    scopus 로고
    • A sensitive procedure for mapping the boundaries of RNA elements binding in vitro translated proteins defines a minimal hepatitis B virus encapsidation signal
    • Beck,J. and Nassal,M. (1996) A sensitive procedure for mapping the boundaries of RNA elements binding in vitro translated proteins defines a minimal hepatitis B virus encapsidation signal. Nucleic Acids Res., 24, 4364-4366.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4364-4366
    • Beck, J.1    Nassal, M.2
  • 30
    • 0032825042 scopus 로고    scopus 로고
    • Interferon gene transfer by a hepatitis B virus vector efficiently suppresses wild-type virus infection
    • Protzer,U., Nassal,M., Chiang,P.W., Kirschfink,M. and Schaller,H. (1999) Interferon gene transfer by a hepatitis B virus vector efficiently suppresses wild-type virus infection. Proc. Natl Acad. Sci. USA, 96, 10818-10823.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10818-10823
    • Protzer, U.1    Nassal, M.2    Chiang, P.W.3    Kirschfink, M.4    Schaller, H.5
  • 32
    • 0036721370 scopus 로고    scopus 로고
    • Characterization of the cis-acting contributions to avian hepadnavirus RNA encapsidation
    • Ostrow,K.M. and Loeb,D.D. (2002) Characterization of the cis-acting contributions to avian hepadnavirus RNA encapsidation. J. Virol., 76, 9087-9095.
    • (2002) J. Virol. , vol.76 , pp. 9087-9095
    • Ostrow, K.M.1    Loeb, D.D.2
  • 33
    • 0028274118 scopus 로고
    • Two regions of an avian hepadnavirus RNA pregenome are required in cis for encapsidation
    • Calvert,J. and Summers,J. (1994) Two regions of an avian hepadnavirus RNA pregenome are required in cis for encapsidation. J. Virol., 68, 2084-2090.
    • (1994) J. Virol. , vol.68 , pp. 2084-2090
    • Calvert, J.1    Summers, J.2
  • 34
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: Primary structure requirements in the core protein
    • Birnbaum,F. and Nassal,M. (1990) Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein. J. Virol., 64, 3319-3330.
    • (1990) J. Virol. , vol.64 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 37
    • 0035844150 scopus 로고    scopus 로고
    • Systematic evolution of a DNA aptamer binding to rat brain tumor microvessels. Selective targeting of endothelial regulatory protein pigpen
    • Blank,M., Weinschenk,T., Priemer,M. and Schluesener,H. (2001) Systematic evolution of a DNA aptamer binding to rat brain tumor microvessels. Selective targeting of endothelial regulatory protein pigpen. J. Biol. Chem., 276, 16464-16468.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16464-16468
    • Blank, M.1    Weinschenk, T.2    Priemer, M.3    Schluesener, H.4
  • 39
    • 0033797244 scopus 로고    scopus 로고
    • Nucleic acid aptamers-from selection in vitro to applications in vivo
    • Famulok,M., Mayer,G. and Blind,M. (2000) Nucleic acid aptamers-from selection in vitro to applications in vivo. Acc. Chem. Res., 33, 591-599.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 591-599
    • Famulok, M.1    Mayer, G.2    Blind, M.3
  • 40
    • 0035989626 scopus 로고    scopus 로고
    • RNA as the catalyst for drug screening
    • Gold,L. (2002) RNA as the catalyst for drug screening. Nat. Biotechnol., 20, 671-672.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 671-672
    • Gold, L.1
  • 41
    • 0347364648 scopus 로고    scopus 로고
    • Tenascin-C aptamer identified by tumor cell SELEX: Systematic evolution of ligands by exponential enrichment
    • Daniels,D.A., Chen,H., Hicke,B.J., Swiderek,K.M. and Gold,L. (2003) A tenascin-C aptamer identified by tumor cell SELEX: systematic evolution of ligands by exponential enrichment. Proc. Natl Acad. Sci. USA, 100, 15416-15421.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15416-15421
    • Daniels, D.A.1    Chen, H.2    Hicke, B.J.3    Swiderek, K.M.4    Gold, L.A.5
  • 42
    • 0034856805 scopus 로고    scopus 로고
    • Functional analysis of prokaryotic SELB proteins
    • Thanbichler,M. and Böck,A. (2001) Functional analysis of prokaryotic SELB proteins. Biofactors, 14, 53-59.
    • (2001) Biofactors , vol.14 , pp. 53-59
    • Thanbichler, M.1    Böck, A.2
  • 43
    • 0031010402 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB
    • Klug,S.J., Hüttenhofer,A., Kromayer,M. and Famulok,M. (1997) In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB. Proc. Natl Acad. Sci. USA, 94, 6676-6681.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6676-6681
    • Klug, S.J.1    Hüttenhofer, A.2    Kromayer, M.3    Famulok, M.4
  • 44
    • 0344564163 scopus 로고    scopus 로고
    • In vitro selection of RNA aptamers that bind special elongation factor SelB, a protein with multiple RNA-binding sites, reveals one major interaction domain at the carboxyl terminus
    • Klug,S.J., Hüttenhofer,A. and Famulok,M. (1999) In vitro selection of RNA aptamers that bind special elongation factor SelB, a protein with multiple RNA-binding sites, reveals one major interaction domain at the carboxyl terminus. RNA, 5, 1180-1190.
    • (1999) RNA , vol.5 , pp. 1180-1190
    • Klug, S.J.1    Hüttenhofer, A.2    Famulok, M.3
  • 45
    • 0036799597 scopus 로고    scopus 로고
    • RNA recognition site of PP7 coat protein
    • Lim,F. and Peabody,D.S. (2002) RNA recognition site of PP7 coat protein. Nucleic Acids Res., 30, 4138-4144.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4138-4144
    • Lim, F.1    Peabody, D.S.2
  • 46
    • 0030582678 scopus 로고    scopus 로고
    • Bent pseudoknots and novel RNA inhibitors of type 1 human immunodeficiency virus (HIV-1) reverse transcriptase
    • Burke,D.H., Scates,L., Andrews,K. and Gold,L. (1996) Bent pseudoknots and novel RNA inhibitors of type 1 human immunodeficiency virus (HIV-1) reverse transcriptase. J. Mol. Biol., 264, 650-666.
    • (1996) J. Mol. Biol. , vol.264 , pp. 650-666
    • Burke, D.H.1    Scates, L.2    Andrews, K.3    Gold, L.4
  • 47
    • 0032480010 scopus 로고    scopus 로고
    • The structure of HIV-1 reverse transcriptase complexed with an RNA pseudoknot inhibitor
    • Jaeger,J., Restle,T. and Steitz,T.A. (1998) The structure of HIV-1 reverse transcriptase complexed with an RNA pseudoknot inhibitor. EMBO J., 17, 4535-4542.
    • (1998) EMBO J. , vol.17 , pp. 4535-4542
    • Jaeger, J.1    Restle, T.2    Steitz, T.A.3
  • 48
    • 0034674431 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase-pseudoknot RNA aptamer interaction has a binding-affinity in the low picomolar range coupled with high specificity
    • Kensch,O., Connolly,B.A., Steinhoff,H.J., McGregor,A., Goody,R.S. and Restle,T. (2000) HIV-1 reverse transcriptase-pseudoknot RNA aptamer interaction has a binding-affinity in the low picomolar range coupled with high specificity. J. Biol. Chem., 275, 18271-18278.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18271-18278
    • Kensch, O.1    Connolly, B.A.2    Steinhoff, H.J.3    McGregor, A.4    Goody, R.S.5    Restle, T.6
  • 49
    • 0037106622 scopus 로고    scopus 로고
    • Endogenous expression of a high-affinity pseudoknot RNA aptamer suppresses replication of HIV-1
    • Chaloin,L., Lehmann,M.J., Sczakiel,G. and Restle,T. (2002) Endogenous expression of a high-affinity pseudoknot RNA aptamer suppresses replication of HIV-1. Nucleic Acids Res., 30, 4001-4008.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4001-4008
    • Chaloin, L.1    Lehmann, M.J.2    Sczakiel, G.3    Restle, T.4


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