메뉴 건너뛰기




Volumn 476, Issue , 2015, Pages 323-333

An encapsidated viral protein and its role in RNA packaging by a non-enveloped animal RNA virus

Author keywords

Alphatetraviridae; P17 Encapsidation; RNA packaging; Virus like particles

Indexed keywords

PROTEIN P17; VIRUS PROTEIN; VIRUS RNA;

EID: 84920910013     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.12.026     Document Type: Article
Times cited : (5)

References (46)
  • 1
    • 0028906644 scopus 로고
    • Assembly of the T=4 Nudaurelia capensis ω virus capsid protein, post-translational cleavage, and specific encapsidation of its mRNA in a baculovirus expression system
    • Agrawal D.K., Johnson J.E. Assembly of the T=4 Nudaurelia capensis ω virus capsid protein, post-translational cleavage, and specific encapsidation of its mRNA in a baculovirus expression system. Virology 1995, 207:89-97.
    • (1995) Virology , vol.207 , pp. 89-97
    • Agrawal, D.K.1    Johnson, J.E.2
  • 2
    • 38349115693 scopus 로고    scopus 로고
    • Replication-coupled packaging mechanism in positive-strand RNA viruses: synchronized co-expression of functional multigenome RNA components of an animal and a pant virus in Nicotiana benthamiana cells by agroinfiltration
    • Annamalai P., Rofail F., DeMason D.A., Rao A.L.N. Replication-coupled packaging mechanism in positive-strand RNA viruses: synchronized co-expression of functional multigenome RNA components of an animal and a pant virus in Nicotiana benthamiana cells by agroinfiltration. J. Virol. 2008, 82:1484-1495.
    • (2008) J. Virol. , vol.82 , pp. 1484-1495
    • Annamalai, P.1    Rofail, F.2    DeMason, D.A.3    Rao, A.L.N.4
  • 3
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica multiple-nucleocapsid nucleopolyhedrovirus
    • Ayers M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D. The complete DNA sequence of Autographa californica multiple-nucleocapsid nucleopolyhedrovirus. Virology 1994, 202:586-605.
    • (1994) Virology , vol.202 , pp. 586-605
    • Ayers, M.D.1    Howard, S.C.2    Kuzio, J.3    Lopez-Ferber, M.4    Possee, R.D.5
  • 4
    • 84864069467 scopus 로고    scopus 로고
    • Structural comparison of insect RNA viruses
    • Caister Academic Press, Norfolk, UK. S. Asgari, K.N. Johnson (Eds.)
    • Banerjee M., Speir J.A., Johnson J.E. Structural comparison of insect RNA viruses. Insect Virology 2010, 327-346. Caister Academic Press, Norfolk, UK. S. Asgari, K.N. Johnson (Eds.).
    • (2010) Insect Virology , pp. 327-346
    • Banerjee, M.1    Speir, J.A.2    Johnson, J.E.3
  • 5
    • 14644438331 scopus 로고    scopus 로고
    • Maturation of a tetravirus capsid alters the dynamic properties and creates a metastable complex
    • Bothner B., Tayler D.J., Jun B., Lee K.K., Siuzdak G., Schlutz C.P., Johnson J.E. Maturation of a tetravirus capsid alters the dynamic properties and creates a metastable complex. Virology 2005, 334:17-27.
    • (2005) Virology , vol.334 , pp. 17-27
    • Bothner, B.1    Tayler, D.J.2    Jun, B.3    Lee, K.K.4    Siuzdak, G.5    Schlutz, C.P.6    Johnson, J.E.7
  • 6
    • 0034625320 scopus 로고    scopus 로고
    • Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω virus (NωV)
    • Canady M.A., Tihova M., Hanzlik T.M., Johnson J.E., Yeager M. Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω virus (NωV). J. Mol. Biol. 2000, 299:573-584.
    • (2000) J. Mol. Biol. , vol.299 , pp. 573-584
    • Canady, M.A.1    Tihova, M.2    Hanzlik, T.M.3    Johnson, J.E.4    Yeager, M.5
  • 7
    • 0035943387 scopus 로고    scopus 로고
    • Analysis of rapid, large-scale protein quaternary structural changes: time-resolved X-ray solution scattering of Nudaurelia capensis ω virus (NωV) maturation
    • Canady M.A., Tsuruta H., Johnson.J.E. Analysis of rapid, large-scale protein quaternary structural changes: time-resolved X-ray solution scattering of Nudaurelia capensis ω virus (NωV) maturation. J. Mol. Biol. 2001, 311:803-814.
    • (2001) J. Mol. Biol. , vol.311 , pp. 803-814
    • Canady, M.A.1    Tsuruta, H.2    Johnson, J.E.3
  • 8
    • 0023664018 scopus 로고
    • Comparison of the consensus sequence flanking translational start sites in Drosophila and vertebrates
    • Cavener D.R. Comparison of the consensus sequence flanking translational start sites in Drosophila and vertebrates. Nucleic Acids Res. 1987, 15:1353-1361.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1353-1361
    • Cavener, D.R.1
  • 9
    • 0035141279 scopus 로고    scopus 로고
    • Pathology and properties of the tetravirus Helicoverpa armigera stunt virus
    • Christian P.D., Dorrian S.J., Gordon K.H.J., Hanzlik T.N. Pathology and properties of the tetravirus Helicoverpa armigera stunt virus. Biol. Control 2001, 20:65-75.
    • (2001) Biol. Control , vol.20 , pp. 65-75
    • Christian, P.D.1    Dorrian, S.J.2    Gordon, K.H.J.3    Hanzlik, T.N.4
  • 10
    • 84879842986 scopus 로고    scopus 로고
    • The asymmetric structure of an icosahedral virus bound to its receptor suggests a mechanism for genome release
    • Dent K.C., Thompson R., Barker A.M., Hiscox J.A., Barr J.N., Stockley P.G., Ranson N.A. The asymmetric structure of an icosahedral virus bound to its receptor suggests a mechanism for genome release. Structure 2013, 21:1225-1234.
    • (2013) Structure , vol.21 , pp. 1225-1234
    • Dent, K.C.1    Thompson, R.2    Barker, A.M.3    Hiscox, J.A.4    Barr, J.N.5    Stockley, P.G.6    Ranson, N.A.7
  • 11
    • 84866167965 scopus 로고    scopus 로고
    • Dissecting quasi-equivalence in non-enveloped viruses: membrane disruption is promoted by lytic peptides released from subunit pentamers, not hexamers
    • Domitrovic T., Matsui T., Johnson J.E. Dissecting quasi-equivalence in non-enveloped viruses: membrane disruption is promoted by lytic peptides released from subunit pentamers, not hexamers. J. Virol. 2012, 86:9976-9982.
    • (2012) J. Virol. , vol.86 , pp. 9976-9982
    • Domitrovic, T.1    Matsui, T.2    Johnson, J.E.3
  • 12
    • 0031776460 scopus 로고    scopus 로고
    • Particle polymorphism caused by deletion of a peptide molecular switch in a quasi-equivalent icosahedral virus
    • Dong X.F., Natarajan P., Tihova M., Johnson J.E., Schneemann A. Particle polymorphism caused by deletion of a peptide molecular switch in a quasi-equivalent icosahedral virus. J. Virol. 1998, 72:6024-6033.
    • (1998) J. Virol. , vol.72 , pp. 6024-6033
    • Dong, X.F.1    Natarajan, P.2    Tihova, M.3    Johnson, J.E.4    Schneemann, A.5
  • 13
    • 80051523747 scopus 로고    scopus 로고
    • Tetraviruses
    • Caister Academic Press, Norfolk, UK. S. Asgari, K.N. Johnson (Eds.)
    • Dorrington R.A., Short J.R. Tetraviruses. Insect Virology 2010, 283-305. Caister Academic Press, Norfolk, UK. S. Asgari, K.N. Johnson (Eds.).
    • (2010) Insect Virology , pp. 283-305
    • Dorrington, R.A.1    Short, J.R.2
  • 14
    • 84864044371 scopus 로고    scopus 로고
    • Family Tetraviridae
    • Oxford: Elsevier Academic Press, London, (pp. 1091-1102), A.M.O. King, M.J. Adams, E.B. Carstens, E.J. Lefkowitz (Eds.)
    • Dorrington R.A., Gorbalenya A.E., Gordon K.H.J., Lauber C., Ward, V.K.V.K. Family Tetraviridae. Virus Taxonomy 2011, Oxford: Elsevier Academic Press, London, (pp. 1091-1102). A.M.O. King, M.J. Adams, E.B. Carstens, E.J. Lefkowitz (Eds.).
    • (2011) Virus Taxonomy
    • Dorrington, R.A.1    Gorbalenya, A.E.2    Gordon, K.H.J.3    Lauber, C.4    Ward, V.K.V.K.5
  • 15
    • 0015243262 scopus 로고
    • Fragments generated by pH dissociation of ME-virus and their relation to the structure of the virion
    • Dunker A.K., Rueckert R.R. Fragments generated by pH dissociation of ME-virus and their relation to the structure of the virion. J. Mol. Biol. 1971, 58:217-235.
    • (1971) J. Mol. Biol. , vol.58 , pp. 217-235
    • Dunker, A.K.1    Rueckert, R.R.2
  • 17
    • 84875429396 scopus 로고    scopus 로고
    • Sequence-specific, RNA-protein interactions overcome electrostatic barriers preventing assembly of satellite tobacco necrosis virus coat protein
    • Ford R.J., Barker A.M., Bakker S.E., Coutts R.H., Ranson N.A., Phillips S.E.V., Pearson A.R., Stockley P.G. Sequence-specific, RNA-protein interactions overcome electrostatic barriers preventing assembly of satellite tobacco necrosis virus coat protein. J. Mol. Biol. 2013, 425:1050-1064.
    • (2013) J. Mol. Biol. , vol.425 , pp. 1050-1064
    • Ford, R.J.1    Barker, A.M.2    Bakker, S.E.3    Coutts, R.H.4    Ranson, N.A.5    Phillips, S.E.V.6    Pearson, A.R.7    Stockley, P.G.8
  • 19
    • 0027282648 scopus 로고
    • A novel small RNA virus isolated from the cotton bollworm, Helicoverpa armigera
    • Hanzlik T.N., Dorrian S.J., Gordon K.H.J., Christian P.J. A novel small RNA virus isolated from the cotton bollworm, Helicoverpa armigera. J. Gen. Virol. 1993, 74:1805-1810.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1805-1810
    • Hanzlik, T.N.1    Dorrian, S.J.2    Gordon, K.H.J.3    Christian, P.J.4
  • 20
    • 0028923849 scopus 로고
    • Sequence of RNA2 of the Helicoverpa armigera stunt virus (Tetraviridae) and bacterial expression of its genes
    • Hanzlik T.N., Dorrian S.J., Johnson K.N., Brooks E.M., Gordon K.H.J. Sequence of RNA2 of the Helicoverpa armigera stunt virus (Tetraviridae) and bacterial expression of its genes. J. Gen. Virol. 1995, 76:799-811.
    • (1995) J. Gen. Virol. , vol.76 , pp. 799-811
    • Hanzlik, T.N.1    Dorrian, S.J.2    Johnson, K.N.3    Brooks, E.M.4    Gordon, K.H.J.5
  • 21
    • 1242319463 scopus 로고    scopus 로고
    • The refined structure of Nudaurelia capensis ω virus reveals control elements for a T=4 capsid maturation
    • Helgstrand C., Munshi S., Johnson J.E., Liljas L. The refined structure of Nudaurelia capensis ω virus reveals control elements for a T=4 capsid maturation. Virology 2004, 318:192-203.
    • (2004) Virology , vol.318 , pp. 192-203
    • Helgstrand, C.1    Munshi, S.2    Johnson, J.E.3    Liljas, L.4
  • 22
    • 84920886488 scopus 로고    scopus 로고
    • Release
    • ICTV Virus Taxonomy: 2011. Release http://www.ictvonline.org/virusTaxonomy.asp?version=201http://www.ictvonline.org/virusTaxonomy.asp?version=201.
    • (2011)
  • 23
    • 0015307752 scopus 로고
    • Stages in phage R17 infection: VI. Injection of a protein and RNA into the host cell
    • Krahn P.M., O'Callaghan R.J., Paranchych W. Stages in phage R17 infection: VI. Injection of a protein and RNA into the host cell. Virology 1972, 47:628-637.
    • (1972) Virology , vol.47 , pp. 628-637
    • Krahn, P.M.1    O'Callaghan, R.J.2    Paranchych, W.3
  • 24
    • 33746082812 scopus 로고    scopus 로고
    • Surface display of an internal His-tag on virus-like particles of Nudaurelia capensis ω virus (NωV) produced in a baculovirus expression system
    • Maree H.J., van der Walt E., Tiedt F.A.C., Hanzlik T.N., Appel M. Surface display of an internal His-tag on virus-like particles of Nudaurelia capensis ω virus (NωV) produced in a baculovirus expression system. J. Virol. Methods 2006, 136:283-288.
    • (2006) J. Virol. Methods , vol.136 , pp. 283-288
    • Maree, H.J.1    van der Walt, E.2    Tiedt, F.A.C.3    Hanzlik, T.N.4    Appel, M.5
  • 25
    • 0030576341 scopus 로고    scopus 로고
    • The 2.8Å structure of a T=4 animal virus and its implications for membrane translocation of RNA
    • Munshi S., Liljas L., Cavarelli J., Bomu W., McKinney B., Reddy V., Johnson J.E. The 2.8Å structure of a T=4 animal virus and its implications for membrane translocation of RNA. J. Mol. Biol. 1996, 261:1-10.
    • (1996) J. Mol. Biol. , vol.261 , pp. 1-10
    • Munshi, S.1    Liljas, L.2    Cavarelli, J.3    Bomu, W.4    McKinney, B.5    Reddy, V.6    Johnson, J.E.7
  • 26
    • 58149517675 scopus 로고    scopus 로고
    • Characterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid
    • Matsui T., Lander G.C., Johnson J.E. Characterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid. J. Virol. 2009, 83:1126-1134.
    • (2009) J. Virol. , vol.83 , pp. 1126-1134
    • Matsui, T.1    Lander, G.C.2    Johnson, J.E.3
  • 27
    • 77956269342 scopus 로고    scopus 로고
    • Subunits fold at position-dependent rates during maturation of a eukaryotic RNA virus
    • Matsui T., Lander G.C., Khayat R., Johnson J.E. Subunits fold at position-dependent rates during maturation of a eukaryotic RNA virus. Proc. Natl. Acad. Sci. U.S.A. 2010, 10:14111-14115.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.10 , pp. 14111-14115
    • Matsui, T.1    Lander, G.C.2    Khayat, R.3    Johnson, J.E.4
  • 29
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of poliovirus replicon RNA
    • Nugent C.L., Johnson K.L., Sarnow P., Kirkegaard K. Functional coupling between replication and packaging of poliovirus replicon RNA. J. Virol. 1999, 73:427-435.
    • (1999) J. Virol. , vol.73 , pp. 427-435
    • Nugent, C.L.1    Johnson, K.L.2    Sarnow, P.3    Kirkegaard, K.4
  • 31
    • 0037440765 scopus 로고    scopus 로고
    • Providence virus: a new member of the Tetraviridae that infects cultured insect cells
    • Pringle F.M., Johnson K.N., Goodman C.L., McIntosh A.H., Ball L.A. Providence virus: a new member of the Tetraviridae that infects cultured insect cells. J. Gen. Virol. 2003, 306:359-370.
    • (2003) J. Gen. Virol. , vol.306 , pp. 359-370
    • Pringle, F.M.1    Johnson, K.N.2    Goodman, C.L.3    McIntosh, A.H.4    Ball, L.A.5
  • 33
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Reichsteiner M., Rogers S.W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 1996, 21:267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Reichsteiner, M.1    Rogers, S.W.2
  • 34
    • 84863181640 scopus 로고    scopus 로고
    • Host RNAs, including transposons, are encapsidated by a eukaryotic single-stranded RNA virus
    • Routh A., Domitrovic T., Johnson J.E. Host RNAs, including transposons, are encapsidated by a eukaryotic single-stranded RNA virus. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:1907-1912.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 1907-1912
    • Routh, A.1    Domitrovic, T.2    Johnson, J.E.3
  • 35
    • 0028171039 scopus 로고
    • G1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover
    • Salaman S.R., Hendricks K.B., Thorner J. G1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover. Mol. Cell. Biol. 1994, 14:7953-7966.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7953-7966
    • Salaman, S.R.1    Hendricks, K.B.2    Thorner, J.3
  • 38
    • 0023053998 scopus 로고
    • Structure of turnip crinkle virus: III. Identification of a unique coat protein dimer
    • Stockley P.G., Kirsh A.L., Chow E.P., Smart J.E., Harrison S.C. Structure of turnip crinkle virus: III. Identification of a unique coat protein dimer. J. Mol. Biol. 1986, 191:721-725.
    • (1986) J. Mol. Biol. , vol.191 , pp. 721-725
    • Stockley, P.G.1    Kirsh, A.L.2    Chow, E.P.3    Smart, J.E.4    Harrison, S.C.5
  • 39
    • 84897646219 scopus 로고    scopus 로고
    • Dynamic and geometric analyses of Nudaurelia capensis ω virus maturation reveal the energy landscape of particle transitions
    • Tang J., Kearney B.M., Wang Q., Doerschuk P.C., Baker T.S., Johnson J.E. Dynamic and geometric analyses of Nudaurelia capensis ω virus maturation reveal the energy landscape of particle transitions. J. Mol. Recognit. 2014, 27:230-237.
    • (2014) J. Mol. Recognit. , vol.27 , pp. 230-237
    • Tang, J.1    Kearney, B.M.2    Wang, Q.3    Doerschuk, P.C.4    Baker, T.S.5    Johnson, J.E.6
  • 41
    • 0036776532 scopus 로고    scopus 로고
    • Large-scale, pH-dependent, quaternary structure changes in an RNA virus capsid are reversible in the absence of subunit autoproteolysis
    • Taylor D.J., Krishna N.K., Canady M.A., Schneeman A., Johnson J.E. Large-scale, pH-dependent, quaternary structure changes in an RNA virus capsid are reversible in the absence of subunit autoproteolysis. J. Virol. 2002, 76:9972-9980.
    • (2002) J. Virol. , vol.76 , pp. 9972-9980
    • Taylor, D.J.1    Krishna, N.K.2    Canady, M.A.3    Schneeman, A.4    Johnson, J.E.5
  • 42
    • 84887446592 scopus 로고    scopus 로고
    • Family Nodaviridae
    • Oxford: Elsevier Academic Press, London, A.M.O. King, M.J. Adams, E.B. Carstens, E.J. Lefkowitz (Eds.)
    • Thiéry R., Johnson K.L., Nakai T., Schneemann A., Bonami J.R., Lightner D.V. Family Nodaviridae. Virus Taxonomy 2011, 1061-1067. Oxford: Elsevier Academic Press, London. A.M.O. King, M.J. Adams, E.B. Carstens, E.J. Lefkowitz (Eds.).
    • (2011) Virus Taxonomy , pp. 1061-1067
    • Thiéry, R.1    Johnson, K.L.2    Nakai, T.3    Schneemann, A.4    Bonami, J.R.5    Lightner, D.V.6
  • 43
    • 34248225008 scopus 로고    scopus 로고
    • Induction of apoptosis in Saccharomyces cerevisiae results in spontaneous maturation of tetravirus procapsids in vivo
    • Tomasicchio M., Venter P.A., Gordon K.H.J., Hanzlik T.N., Dorrington R.A. Induction of apoptosis in Saccharomyces cerevisiae results in spontaneous maturation of tetravirus procapsids in vivo. J. Gen. Virol. 2007, 881:576-582.
    • (2007) J. Gen. Virol. , vol.881 , pp. 576-582
    • Tomasicchio, M.1    Venter, P.A.2    Gordon, K.H.J.3    Hanzlik, T.N.4    Dorrington, R.A.5
  • 44
    • 18144391518 scopus 로고    scopus 로고
    • Capsid protein synthesis from replicating RNA directs specific packaging of the genome of a multipartite, positive-strand RNA virus
    • Venter P.A.N.P., Krishna, Schneemann A. Capsid protein synthesis from replicating RNA directs specific packaging of the genome of a multipartite, positive-strand RNA virus. J. Virol. 2005, 79:6239-6248.
    • (2005) J. Virol. , vol.79 , pp. 6239-6248
    • Venter, P.A.N.P.K.1    Schneemann, A.2
  • 45
    • 14744306947 scopus 로고    scopus 로고
    • Isolation and identification of a new tetravirus from Dendrolimus punctatus larvae collected from Yunnan province, China
    • Yi F., Zhang J., Yu H., Liu C., Wang J., Hu Y. Isolation and identification of a new tetravirus from Dendrolimus punctatus larvae collected from Yunnan province, China. J. Gen. Virol. 2005, 86:789-796.
    • (2005) J. Gen. Virol. , vol.86 , pp. 789-796
    • Yi, F.1    Zhang, J.2    Yu, H.3    Liu, C.4    Wang, J.5    Hu, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.