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Volumn 4, Issue , 2013, Pages

Life cycle of phytoreoviruses visualized by electron microscopy and tomography

Author keywords

Electron microscopy; Electron tomography; Rice dwarf virus; Rice gall dwarf virus; Virus structure

Indexed keywords

ARTICLE; CRYOELECTRON MICROSCOPY; ELECTRON MICROSCOPY; ELECTRON TOMOGRAPHY; GENE MUTATION; INSECT VECTOR; INTRACELLULAR TRANSPORT; LIFE CYCLE ASSESSMENT; NONHUMAN; REOVIRIDAE; REOVIRUS INFECTION; RICE DWARF VIRUS; RICE GALL DWARF VIRUS; RNA SEQUENCE; VIRION; VIRUS ASSEMBLY; VIRUS ENTRY; VIRUS GENOME; VIRUS RELEASE; VIRUS REPLICATION; VIRUS TRANSMISSION;

EID: 85017012529     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2013.00306     Document Type: Article
Times cited : (17)

References (63)
  • 1
    • 84863115713 scopus 로고    scopus 로고
    • Crystallographic analysis reveals octamerization of viroplasm matrix protein P9-1 of Rice black streak dwarf virus
    • Akita, F., Higashiura, A., Shimizu, T., Pu, Y., Suzuki, M., Uehara-Ichiki, T., et al. (2012). Crystallographic analysis reveals octamerization of viroplasm matrix protein P9-1 of Rice black streak dwarf virus. J. Virol. 86, 746-756. doi: 10.1128/JVI.00826-11
    • (2012) J. Virol. , vol.86 , pp. 746-756
    • Akita, F.1    Higashiura, A.2    Shimizu, T.3    Pu, Y.4    Suzuki, M.5    Uehara-Ichiki, T.6
  • 2
    • 80051779148 scopus 로고    scopus 로고
    • Viroplasm matrix protein Pns9 from Rice gall dwarf virus forms an octameric cylindrical structure
    • Akita, F., Miyazaki, N., Hibino, H., Shimizu, T., HIgashiura, A., Uehara-Ichiki, T., et al. (2011). Viroplasm matrix protein Pns9 from Rice gall dwarf virus forms an octameric cylindrical structure. J. Gen. Virol. 92, 2214-2221. doi: 10.1099/vir.0.032524-0
    • (2011) J. Gen. Virol. , vol.92 , pp. 2214-2221
    • Akita, F.1    Miyazaki, N.2    Hibino, H.3    Shimizu, T.4    Higashiura, A.5    Uehara-Ichiki, T.6
  • 3
    • 33644838714 scopus 로고    scopus 로고
    • Cell-to-cell movement of potato potexvirus X is dependent on suppression of RNA silencing
    • Bayne, E. H., Rakitina, D. V., Moro-zov, S. Y., and Baulcombe, D. C. (2005). Cell-to-cell movement of potato potexvirus X is dependent on suppression of RNA silencing. Plant J. 44, 471-482. doi: 10.1111/j.1365-313X.2005.02539.x
    • (2005) Plant J , vol.44 , pp. 471-482
    • Bayne, E.H.1    Rakitina, D.V.2    Moro-Zov, S.Y.3    Baulcombe, D.C.4
  • 4
    • 26444446951 scopus 로고    scopus 로고
    • Identification of an RNA silencing suppressor from a plant double-stranded RNA virus
    • Cao, X., Zhou, P., Zhang, X, Zhu, S., Zhong, X., Xiao, Q., Ding, B., et al. (2005). Identification of an RNA silencing suppressor from a plant double-stranded RNA virus. J. Virol. 79, 13018-13027. doi: 10.1128/JVI.79.20.13018-13027.2005
    • (2005) J. Virol. , vol.79 , pp. 13018-13027
    • Cao, X.1    Zhou, P.2    Zhang, X.3    Zhu, S.4    Zhong, X.5    Xiao, Q.6    Ding, B.7
  • 5
    • 80052167039 scopus 로고    scopus 로고
    • Sequential infection of Rice dwarf virus in the internal organs of its insect vector after ingestion of virus
    • Chen, H., Chen, Q., Omura, T., Uehara-Ichiki, T., and Wei, T. (2011). Sequential infection of Rice dwarf virus in the internal organs of its insect vector after ingestion of virus. Virus Res. 160, 389-394. doi: 10.1016/j.virusres.2011.04.028
    • (2011) Virus Res , vol.160 , pp. 389-394
    • Chen, H.1    Chen, Q.2    Omura, T.3    Uehara-Ichiki, T.4    Wei, T.5
  • 6
    • 84870809425 scopus 로고    scopus 로고
    • Tubular structure induced by a plant virus facilitates viral spread in its vector insect
    • Chen, Q., Chen, H., Mao, Q., Liu, Q., Shimizu, T., Uehara-Ichiki, T., et al. (2012). Tubular structure induced by a plant virus facilitates viral spread in its vector insect. PLoS Pathog. 8:e1003032. doi: 10.1371/journal.ppat.1003032
    • (2012) PLoS Pathog , vol.8
    • Chen, Q.1    Chen, H.2    Mao, Q.3    Liu, Q.4    Shimizu, T.5    Uehara-Ichiki, T.6
  • 7
    • 35548988063 scopus 로고    scopus 로고
    • Whole cell cryo-electron tomography reveals distinct disassembly intermediates of vaccinia virus
    • Cyrklaff, M., Linaroudis, A., Boicu, M., Chlanda, P., Baumeister, W., Griffiths, G., et al. (2007). Whole cell cryo-electron tomography reveals distinct disassembly intermediates of vaccinia virus. PLoS ONE 2:e420. doi: 10.1371/journal.pone.0000420
    • (2007) PLoS ONE , vol.2
    • Cyrklaff, M.1    Linaroudis, A.2    Boicu, M.3    Chlanda, P.4    Baumeister, W.5    Griffiths, G.6
  • 8
    • 21244468590 scopus 로고    scopus 로고
    • Viral stop- And-go along microtubules: Taking a ride with dynein and kinesins
    • Döhner, K., Nagel, C. H., and Sodeik, B. (2005). Viral stop- and-go along microtubules: taking a ride with dynein and kinesins. Trends Microbiol. 13, 320-327. doi: 10.1016/j.tim.2005.05.010
    • (2005) Trends Microbiol , vol.13 , pp. 320-327
    • Döhner, K.1    Nagel, C.H.2    Sodeik, B.3
  • 9
    • 1642308801 scopus 로고    scopus 로고
    • Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation
    • Eichwald, C., Rodriguez, J. F., and Burrone, O. R. (2004). Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation. J. Gen. Virol. 85, 625-634. doi: 10.1099/vir.0.19611-0
    • (2004) J. Gen. Virol. , vol.85 , pp. 625-634
    • Eichwald, C.1    Rodriguez, J.F.2    Burrone, O.R.3
  • 10
    • 0032970118 scopus 로고    scopus 로고
    • Two nonstructural rotavirus proteins, NSP2 and NSP5 form viroplasm-like structures in vivo
    • Fabbretti, E., Afrikanova, I., Vascotto, F., and Burrone, O. R. (1999). Two nonstructural rotavirus proteins, NSP2 and NSP5 form viroplasm-like structures in vivo. J. Gen. Virol. 80, 333-339.
    • (1999) J. Gen. Virol. , vol.80 , pp. 333-339
    • Fabbretti, E.1    Afrikanova, I.2    Vascotto, F.3    Burrone, O.R.4
  • 11
    • 32944475622 scopus 로고    scopus 로고
    • A superhighway to virus infection
    • Greber, U. F., and Way, M. (2006). A superhighway to virus infection. Cell 124, 741-754. doi: 10.1016/j.cell.2006.02.018
    • (2006) Cell , vol.124 , pp. 741-754
    • Greber, U.F.1    Way, M.2
  • 12
    • 1542347737 scopus 로고    scopus 로고
    • The amino-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus
    • Hagiwara, K., Higashi, T., Miyazaki, N., Naitow, H., Cheng, R. H., Nakagawa, A., et al. (2004). The amino-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus. J. Virol. 78, 3145-3148. doi: 10.1128/JVI.78.6.3145-3148.2004
    • (2004) J. Virol. , vol.78 , pp. 3145-3148
    • Hagiwara, K.1    Higashi, T.2    Miyazaki, N.3    Naitow, H.4    Cheng, R.H.5    Nakagawa, A.6
  • 13
    • 0037384087 scopus 로고    scopus 로고
    • Assembly of single-shelled cores and double-shelled virus-like particles after baculovirus expression of major structural proteins P3, P7 and P8 of Rice dwarf virus
    • Hagiwara, K., Higashi, T., Namba, K., Uehara-Ichiki, T., and Omura, T. (2003). Assembly of single-shelled cores and double-shelled virus-like particles after baculovirus expression of major structural proteins P3, P7 and P8 of Rice dwarf virus. J. Gen. Virol. 84, 981-984. doi: 10.1099/vir.0.18904-0
    • (2003) J. Gen. Virol. , vol.84 , pp. 981-984
    • Hagiwara, K.1    Higashi, T.2    Namba, K.3    Uehara-Ichiki, T.4    Omura, T.5
  • 14
    • 5344220273 scopus 로고    scopus 로고
    • Potato virus X GBp1 induces plasmodesmata gating and moves between cells in several host species whereas CP moves only N. Benthamiana leaves
    • Howard, A. R., Heppler, M. L., Ju, H. J., Krishnamuthy, K., Payton, M. E., and Verchot-Lubicz, J. (2004). Potato virus X GBp1 induces plasmodesmata gating and moves between cells in several host species whereas CP moves only N. benthamiana leaves. Virology 328, 185-197. doi: 10.1016/j.virol.2004.06.039
    • (2004) Virology , vol.328 , pp. 185-197
    • Howard, A.R.1    Heppler, M.L.2    Ju, H.J.3    Krishnamuthy, K.4    Payton, M.E.5    Verchot-Lubicz, J.6
  • 15
    • 84855255301 scopus 로고    scopus 로고
    • Cryo electron tomography of herpes simplex virus during axonal transport and secondary envelopment in primary neurons
    • Ibiricu, I., Huiskonen, J. T., Döhner, K., Bradke, F., Sodeik, B., and Grünewald, K. (2011). Cryo electron tomography of herpes simplex virus during axonal transport and secondary envelopment in primary neurons. PLoS Pathog. 7:e1002406. doi: 10.1371/journal.ppat.1002406
    • (2011) PLoS Pathog , vol.7
    • Ibiricu, I.1    Huiskonen, J.T.2    Döhner, K.3    Bradke, F.4    Sodeik, B.5    Grünewald, K.6
  • 16
    • 0031806240 scopus 로고    scopus 로고
    • Detection and assignment of proteins encoded by rice black streaked dwarf fijivirus S7, S8, S9 and S10
    • Isogai, M., Uyeda, I., and Lee, B. C. (1998). Detection and assignment of proteins encoded by rice black streaked dwarf fijivirus S7, S8, S9 and S10. J. Gen. Virol. 79, 1487-1494.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1487-1494
    • Isogai, M.1    Uyeda, I.2    Lee, B.C.3
  • 17
    • 78049444131 scopus 로고    scopus 로고
    • Electron tomography of the supramolec-ular structure of virus-infected cells
    • Iwasaki, K., and Omura, T. (2010). Electron tomography of the supramolec-ular structure of virus-infected cells. Curr. Opin. Struct. Biol. 20, 632-639. doi: 10.1016/j.sbi.2010.08.007
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 632-639
    • Iwasaki, K.1    Omura, T.2
  • 18
    • 0037118101 scopus 로고    scopus 로고
    • Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold
    • Jayaram, H., Taraporewala, Z., Patton, J. T., and Prasad, B. V. V. (2002). Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold. Nature 417, 311-315. doi: 10.1038/417311a
    • (2002) Nature , vol.417 , pp. 311-315
    • Jayaram, H.1    Taraporewala, Z.2    Patton, J.T.3    Prasad, B.V.V.4
  • 19
    • 80052927283 scopus 로고    scopus 로고
    • Movement protein Pns6 of Rice dwarf phytoreovirus has both ATPase and RNA binding activities
    • Ji, X., Qian, D., Wei, C., Ye, G., Zhang, Z., Wu, Z., et al. (2011). Movement protein Pns6 of Rice dwarf phytoreovirus has both ATPase and RNA binding activities. PLoS ONE 6:e24986. doi: 10.1371/jour-nal.pone.0024986
    • (2011) PLoS ONE , vol.6
    • Ji, X.1    Qian, D.2    Wei, C.3    Ye, G.4    Zhang, Z.5    Wu, Z.6
  • 20
    • 33748273804 scopus 로고    scopus 로고
    • Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: Implications for genome replication
    • Jiang, X. F., Jayaram, H., Kumar, M., Ludtke, S. J., Estes, M. K., and Prasad, B. V. V. (2006). Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication. J. Virol. 80, 10829-10835. doi: 10.1128/JVI.01347-06
    • (2006) J. Virol. , vol.80 , pp. 10829-10835
    • Jiang, X.F.1    Jayaram, H.2    Kumar, M.3    Ludtke, S.J.4    Estes, M.K.5    Prasad, B.V.V.6
  • 21
    • 3242707647 scopus 로고    scopus 로고
    • Transport of African swine fever virus from assembly sites to the plasma membrane is dependent on microtubules and conventional kinesin
    • Jouvenet, N., Monaghan, P., Way, M., and Wileman, T. (2004). Transport of African swine fever virus from assembly sites to the plasma membrane is dependent on microtubules and conventional kinesin. J. Virol. 78, 7990-8001. doi: 10.1128/ JVI.78.15.7990-8001.2004
    • (2004) J. Virol. , vol.78 , pp. 7990-8001
    • Jouvenet, N.1    Monaghan, P.2    Way, M.3    Wileman, T.4
  • 22
    • 33749542714 scopus 로고    scopus 로고
    • African swine fever virus induces filopodia-like projections at the plasma membrane
    • Jouvenet, N., Windsor, M., Rietdorf, J., Hawes, P., Monaghan, P., Way, M., et al. (2006). African swine fever virus induces filopodia-like projections at the plasma membrane. Cell. Microbiol. 8, 1803-1811. doi: 10.1111/j.1462-5822.2006.00750.x
    • (2006) Cell. Microbiol. , vol.8 , pp. 1803-1811
    • Jouvenet, N.1    Windsor, M.2    Rietdorf, J.3    Hawes, P.4    Monaghan, P.5    Way, M.6
  • 23
    • 35948971367 scopus 로고    scopus 로고
    • Three-dimensional architecture of virus-packed tubule
    • Katayama, S., Wei, T., Omura, T., Takagi, J., and Iwasaki, K. (2007). Three-dimensional architecture of virus-packed tubule. J. Electron Microsc. 56, 77-81. doi: 10.1093/jmicro/dfm009
    • (2007) J. Electron Microsc. , vol.56 , pp. 77-81
    • Katayama, S.1    Wei, T.2    Omura, T.3    Takagi, J.4    Iwasaki, K.5
  • 24
    • 0026344821 scopus 로고
    • Viruses in the phytoreoviruses genus of the Reoviridae family have the same conserved terminal sequences
    • Kudo, H., Uyeda, I., and Shikata, E. (1991). Viruses in the phytoreoviruses genus of the Reoviridae family have the same conserved terminal sequences. J. Gen. Virol. 72, 2857-2866. doi: 10.1099/0022-1317-72-12-2857
    • (1991) J. Gen. Virol. , vol.72 , pp. 2857-2866
    • Kudo, H.1    Uyeda, I.2    Shikata, E.3
  • 25
    • 0141675998 scopus 로고    scopus 로고
    • Involvement of the secretory pathway and the cytoskeleton in intracellular targeting and tubule assembly of Grapevine fanleaf virus movement protein in tobacco BY-2 cells
    • Laporte, C., Vetter, G., Loudes, A. M., Robinson, D. G., Hillmer, S., Stussi-Garaud, C., et al. (2003). Involvement of the secretory pathway and the cytoskeleton in intracellular targeting and tubule assembly of Grapevine fanleaf virus movement protein in tobacco BY-2 cells. Plant Cell 15, 2058-2075. doi: 10.1105/tpc.013896
    • (2003) Plant Cell , vol.15 , pp. 2058-2075
    • Laporte, C.1    Vetter, G.2    Loudes, A.M.3    Robinson, D.G.4    Hillmer, S.5    Stussi-Garaud, C.6
  • 26
    • 22944446447 scopus 로고    scopus 로고
    • Actin- And myosin-driven movement of viruses along filopodia precedes their entry into cells
    • Lehmann, M. J., Sherer, N. M., Marks, C. B., Pypaert, M., and Mothes, W. (2005). Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells. J. Cell Biol. 170, 317-325. doi: 10.1083/jcb.200503059
    • (2005) J. Cell Biol. , vol.170 , pp. 317-325
    • Lehmann, M.J.1    Sherer, N.M.2    Marks, C.B.3    Pypaert, M.4    Mothes, W.5
  • 27
    • 2342468818 scopus 로고    scopus 로고
    • Rice dwarf phytoreovirus segment S6-encoded nonstructural protein has a cell-to-cell movement function
    • Li, Y., Bao, Y. M., Wei, C. H., Kang, Z. S., Khong, Y. W., Mao, P., et al. (2004). Rice dwarf phytoreovirus segment S6-encoded nonstructural protein has a cell-to-cell movement function. J. Virol. 78, 5382-5389. doi: 10.1128/JVI.78.10.5382-5389.2004
    • (2004) J. Virol. , vol.78 , pp. 5382-5389
    • Li, Y.1    Bao, Y.M.2    Wei, C.H.3    Kang, Z.S.4    Khong, Y.W.5    Mao, P.6
  • 28
    • 48749114826 scopus 로고    scopus 로고
    • Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry
    • Maurer, U. E., Sodeik, B., and Grünewald, K. (2008). Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry. Proc. Natl. Acad. Sci. U.S.A. 105, 10559-10564. doi: 10.1073/pnas.0801674105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10559-10564
    • Maurer, U.E.1    Sodeik, B.2    Grünewald, K.3
  • 29
    • 84885594462 scopus 로고    scopus 로고
    • Cryo-electron tomography: Moving towards revealing the viral life cycle of Rice dwarf virus
    • Miyazaki, N., Akita, F., Nakagawa, A., Murata, K., Omura, T., and Iwasaki, K. (2013). Cryo-electron tomography: moving towards revealing the viral life cycle of Rice dwarf virus. J. Synchrotron Radiat. 20. doi: 10.1107/S090904951302219X
    • (2013) J. Synchrotron Radiat. , vol.20
    • Miyazaki, N.1    Akita, F.2    Nakagawa, A.3    Murata, K.4    Omura, T.5    Iwasaki, K.6
  • 30
    • 9644264004 scopus 로고    scopus 로고
    • Transcapsidation and the conserved interactions of two major structural proteins of a pair of phytoreoviruses confirm the mechanism of assembly of the outer capsid layer
    • Miyazaki, N., Hagiwara, K., Naitow, H., Higashi, T., Cheng, R. H., Tsukihara, T., et al. (2005). Transcapsidation and the conserved interactions of two major structural proteins of a pair of phytoreoviruses confirm the mechanism of assembly of the outer capsid layer. J. Mol. Biol. 345, 229-237. doi: 10.1016/j.jmb.2004.10.044
    • (2005) J. Mol. Biol. , vol.345 , pp. 229-237
    • Miyazaki, N.1    Hagiwara, K.2    Naitow, H.3    Higashi, T.4    Cheng, R.H.5    Tsukihara, T.6
  • 31
    • 77953725201 scopus 로고    scopus 로고
    • The functional organization of the internal components of Rice dwarf virus
    • Miyazaki, N., Wu, B., Hagiwara, K., Wang, C. Y., Xing, L., Hammar, L., et al. (2010). The functional organization of the internal components of Rice dwarf virus. J. Biochem. 147, 843-850. doi: 10.1093/jb/mvq017
    • (2010) J. Biochem. , vol.147 , pp. 843-850
    • Miyazaki, N.1    Wu, B.2    Hagiwara, K.3    Wang, C.Y.4    Xing, L.5    Hammar, L.6
  • 32
    • 12444292684 scopus 로고    scopus 로고
    • The atomic structure of Rice dwarf virus reveals the self-assembly mechanism of component proteins
    • Nakagawa, A., Miyazaki, N., Taka, J., Naitow, H., Ogawa, A., Fujimoto, Z., et al. (2003). The atomic structure of Rice dwarf virus reveals the self-assembly mechanism of component proteins. Structure 11, 1227-1238. doi: 10.1016/j.str.2003.08.012
    • (2003) Structure , vol.11 , pp. 1227-1238
    • Nakagawa, A.1    Miyazaki, N.2    Taka, J.3    Naitow, H.4    Ogawa, A.5    Fujimoto, Z.6
  • 33
    • 85008018941 scopus 로고
    • Electron microscopy studies on transovarial passage of Rice dwarf virus
    • Nasu, S. (1965). Electron microscopy studies on transovarial passage of Rice dwarf virus. Jpn. J. Appl. Entomol. Zool. 9, 225-237. doi: 10.1303/jjaez.9.225
    • (1965) Jpn. J. Appl. Entomol. Zool. , vol.9 , pp. 225-237
    • Nasu, S.1
  • 34
    • 0024747178 scopus 로고
    • The outer capsid protein of Rice dwarf virus is encoded by genome segment S8
    • Omura, T., Ishikawa, K., Hibino, H., Ugaki, M., Minobe, Y., Tsuchizaki, T., et al. (1989). The outer capsid protein of Rice dwarf virus is encoded by genome segment S8. J. Gen. Virol. 70, 2759-2764. doi: 10.1099/0022-1317-70-10-2759
    • (1989) J. Gen. Virol. , vol.70 , pp. 2759-2764
    • Omura, T.1    Ishikawa, K.2    Hibino, H.3    Ugaki, M.4    Minobe, Y.5    Tsuchizaki, T.6
  • 36
    • 0032679318 scopus 로고    scopus 로고
    • Role of outer capsid proteins in transmission of Phytoreovirus by insect vectors
    • Omura, T., and Yan, J. (1999). Role of outer capsid proteins in transmission of Phytoreovirus by insect vectors. Adv. Virus Res. 54, 15-43. doi: 10.1016/S0065-3527(08)60364-4
    • (1999) Adv. Virus Res. , vol.54 , pp. 15-43
    • Omura, T.1    Yan, J.2
  • 37
    • 19244384954 scopus 로고    scopus 로고
    • The P2 protein of Rice dwarf phytoreovirus is required for adsorption of the virus to cells of the insect vector
    • Omura, T., Yan, J., Zhong, B., Wada, M., Zhu, Y., Tomaru, M., et al. (1998). The P2 protein of Rice dwarf phytoreovirus is required for adsorption of the virus to cells of the insect vector. J. Virol. 72, 9370-9373.
    • (1998) J. Virol. , vol.72 , pp. 9370-9373
    • Omura, T.1    Yan, J.2    Zhong, B.3    Wada, M.4    Zhu, Y.5    Tomaru, M.6
  • 38
    • 0033592867 scopus 로고    scopus 로고
    • HSP70 homolog functions in cell-to-cell movement of a plant virus
    • Peremyslov, V. V., Hagiwara, Y., and Dolja, V. V. (1999). HSP70 homolog functions in cell-to-cell movement of a plant virus. Proc. Natl. Acid. Sci. U.S.A. 96, 14771-14776. doi: 10.1073/pnas.96.26.14771
    • (1999) Proc. Natl. Acid. Sci. U.S.A. , vol.96 , pp. 14771-14776
    • Peremyslov, V.V.1    Hagiwara, Y.2    Dolja, V.V.3
  • 39
    • 79952390995 scopus 로고    scopus 로고
    • Rice dwarf viruses with dysfunctional genomes generated in plants are filtered out in vector insects: Implications for the origin of the virus
    • Pu, Y., Kikuchi, A., Moriyasu, Y., Tomaru, M., Jin, Y., Suga, H., et al. (2011). Rice dwarf viruses with dysfunctional genomes generated in plants are filtered out in vector insects: implications for the origin of the virus. J. Virol. 85, 2972-2979. doi: 10.1128/JVI.02147-10
    • (2011) J. Virol. , vol.85 , pp. 2972-2979
    • Pu, Y.1    Kikuchi, A.2    Moriyasu, Y.3    Tomaru, M.4    Jin, Y.5    Suga, H.6
  • 40
    • 33644822448 scopus 로고    scopus 로고
    • Viral interactions with the cytoskeleton: A hitchhiker's guide to the cell
    • Radtke, K., Döhner, K., and Sodeik, B. (2006). Viral interactions with the cytoskeleton: a hitchhiker's guide to the cell. Cell. Microbiol. 8, 387-400. doi: 10.1111/j.1462-5822.2005.00679.x
    • (2006) Cell. Microbiol. , vol.8 , pp. 387-400
    • Radtke, K.1    Döhner, K.2    Sodeik, B.3
  • 41
    • 78649432027 scopus 로고    scopus 로고
    • Multiple functions of Rice dwarf phytoreovirus Pns10 in suppressing systemic RNA silencing
    • Ren, B., Guo, Y., Gao, F., Zhou, P., Wu, F., Meng, Z., et al. (2010). Multiple functions of Rice dwarf phytoreovirus Pns10 in suppressing systemic RNA silencing. J. Virol. 84, 12914-12923. doi: 10.1128/JVI.00864-10
    • (2010) J. Virol. , vol.84 , pp. 12914-12923
    • Ren, B.1    Guo, Y.2    Gao, F.3    Zhou, P.4    Wu, F.5    Meng, Z.6
  • 42
    • 0035736471 scopus 로고    scopus 로고
    • Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus
    • Rietdorf, J., Ploubidou, A., Reckmann, I., Holmstrom, A., Frischknecht, F., Zettl, M., et al. (2001). Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus. Nat. Cell Biol. 3, 992-1000. doi: 10.1038/ncb1101-992
    • (2001) Nat. Cell Biol. , vol.3 , pp. 992-1000
    • Rietdorf, J.1    Ploubidou, A.2    Reckmann, I.3    Holmstrom, A.4    Frischknecht, F.5    Zettl, M.6
  • 43
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • Robinson, C. V., Sali, A., and Baumeister, W. (2007). The molecular sociology of the cell. Nature 450, 973-982. doi: 10.1038/nature06523
    • (2007) Nature , vol.450 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 44
    • 0042389493 scopus 로고    scopus 로고
    • Microtubule-dependent intracellular transport of murine polyomavirus
    • Sanjuan, N., Porras, A., and Otero, J. (2003). Microtubule-dependent intracellular transport of murine polyomavirus. Virology 313, 105-116. doi: 10.1016/S0042-6822(03) 00309-X
    • (2003) Virology , vol.313 , pp. 105-116
    • Sanjuan, N.1    Porras, A.2    Otero, J.3
  • 45
    • 54149119141 scopus 로고    scopus 로고
    • Avoiding the void: Cell-to-cell spread of human viruses
    • Sattentau, Q. (2008). Avoiding the void: cell-to-cell spread of human viruses. Nat. Rev. Microbiol. 6, 815-826. doi: 10.1038/nrmicro1972
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 815-826
    • Sattentau, Q.1
  • 46
    • 57649171916 scopus 로고    scopus 로고
    • Silencing by RNAi of the gene for Pns12, a viroplasm matrix protein of Rice dwarf virus, results in strong resistance of transgenic rice plants to the virus
    • Shimizu, T., Yoshii, M., Wei, T., Hirochika, H., and Omura, T. (2009). Silencing by RNAi of the gene for Pns12, a viroplasm matrix protein of Rice dwarf virus, results in strong resistance of transgenic rice plants to the virus. Plant Biotech-nol. J. 7, 24-32. doi: 10.1111/j.1467-7652.2008.00366.x
    • (2009) Plant Biotech-Nol. J. , vol.7 , pp. 24-32
    • Shimizu, T.1    Yoshii, M.2    Wei, T.3    Hirochika, H.4    Omura, T.5
  • 47
    • 0034307164 scopus 로고    scopus 로고
    • Mechanisms of viral transport in the cytoplasm
    • Sodeik, B. (2000). Mechanisms of viral transport in the cytoplasm. Trends Microbiol. 8, 465-472. doi: 10.1016/S0966-842X(00)01824-2
    • (2000) Trends Microbiol , vol.8 , pp. 465-472
    • Sodeik, B.1
  • 48
    • 0028008430 scopus 로고
    • Conserved primary structures in core capsid proteins and reassembly of core particles and outer capsids between rice gall dwarf and rice dwarf phytoreoviruses
    • Takahashi, Y., Tomiyama, M., Hibino, H., and Omura, T. (1994). Conserved primary structures in core capsid proteins and reassembly of core particles and outer capsids between rice gall dwarf and rice dwarf phytoreoviruses. J. Gen. Virol. 75, 269-275. doi: 10.1099/0022-1317-75-2-269
    • (1994) J. Gen. Virol. , vol.75 , pp. 269-275
    • Takahashi, Y.1    Tomiyama, M.2    Hibino, H.3    Omura, T.4
  • 49
    • 0030874795 scopus 로고    scopus 로고
    • The loss of outer capsid P2 results in nontransmissibility by the insect vector of rice dwarf phytoreovirus
    • Tomaru, M., Maruyama, W., Kikuchi, A., Yan, J., Zhu, Y., Suzuki, N., et al. (1997). The loss of outer capsid P2 results in nontransmissibility by the insect vector of rice dwarf phytoreovirus. J. Virol. 71, 8019-8023.
    • (1997) J. Virol. , vol.71 , pp. 8019-8023
    • Tomaru, M.1    Maruyama, W.2    Kikuchi, A.3    Yan, J.4    Zhu, Y.5    Suzuki, N.6
  • 50
    • 34447252122 scopus 로고    scopus 로고
    • Entry of Rice dwarf virus into cultured cells of its insect vector involves clathrin-mediated endocytosis
    • Wei, T., Chen, H., Ichiki-Uehara, T., Hibino, H., and Omura, T. (2007). Entry of Rice dwarf virus into cultured cells of its insect vector involves clathrin-mediated endocytosis. J. Virol. 81, 7811-7815. doi: 10.1128/JVI.00050-07
    • (2007) J. Virol. , vol.81 , pp. 7811-7815
    • Wei, T.1    Chen, H.2    Ichiki-Uehara, T.3    Hibino, H.4    Omura, T.5
  • 51
    • 69249131775 scopus 로고    scopus 로고
    • Release of Rice dwarf virus from insect vector cells involves secretory exosomes derived from multivesicular bodies
    • Wei, T., Hibino, H., and Omura, T. (2009a). Release of Rice dwarf virus from insect vector cells involves secretory exosomes derived from multivesicular bodies. Commun. Integr. Biol. 2, 324-326. doi: 10.4161/cib.2.4.8335
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 324-326
    • Wei, T.1    Hibino, H.2    Omura, T.3
  • 52
    • 70349754471 scopus 로고    scopus 로고
    • Association of Rice gall dwarf virus with microtubules is necessary for viral release from cultured insect cells
    • Wei, T., Uehara-Ichiki, T., Miyazaki, N., Hibino, H., Iwasaki, K., and Omura, T. (2009b). Association of Rice gall dwarf virus with microtubules is necessary for viral release from cultured insect cells. J. Virol. 83, 10830-10835. doi: 10.1128/JVI.01 067-09
    • (2009) J. Virol. , vol.83 , pp. 10830-10835
    • Wei, T.1    Uehara-Ichiki, T.2    Miyazaki, N.3    Hibino, H.4    Iwasaki, K.5    Omura, T.6
  • 53
    • 33748676100 scopus 로고    scopus 로고
    • The spread of Rice dwarf virus among cells of its insect vector exploit virus-induced tubular structures
    • Wei, T., Kikuchi, A., Moriyasu, Y., Suzuki, N., Shimizu, T., Hagiwara, K., et al. (2006a). The spread of Rice dwarf virus among cells of its insect vector exploit virus-induced tubular structures. J. Virol. 80, 8593-8602. doi: 10.1128/JVI. 00537-06
    • (2006) J. Virol. , vol.80 , pp. 8593-8602
    • Wei, T.1    Kikuchi, A.2    Moriyasu, Y.3    Suzuki, N.4    Shimizu, T.5    Hagiwara, K.6
  • 54
    • 33747140527 scopus 로고    scopus 로고
    • Pns4 of Rice dwarf virus is a phosphoprotein, is localized around the viroplasm matrix, and forms minitubules
    • Wei, T., Kikuchi, A., Suzuki, N., Shimizu, T., Hagiwara, K., Chen, H., et al. (2006b). Pns4 of Rice dwarf virus is a phosphoprotein, is localized around the viroplasm matrix, and forms minitubules. Arch. Virol. 151, 1701-1712. doi: 10.1007/s00705-006-0757-4
    • (2006) Arch. Virol. , vol.151 , pp. 1701-1712
    • Wei, T.1    Kikuchi, A.2    Suzuki, N.3    Shimizu, T.4    Hagiwara, K.5    Chen, H.6
  • 55
    • 31644432215 scopus 로고    scopus 로고
    • Pns12 protein of Rice dwarf virus is essential for formation of viroplasms and nucleation of viral-assembly complexes
    • Wei, T., Shimizu, T., Hagiwara, K., Kikuchi, A., Moriyasu, Y., Suzuki, N., et al. (2006c). Pns12 protein of Rice dwarf virus is essential for formation of viroplasms and nucleation of viral-assembly complexes. J. Gen. Virol. 87, 429-438. doi: 10.1099/vir.0.81425-0
    • (2006) J. Gen. Virol. , vol.87 , pp. 429-438
    • Wei, T.1    Shimizu, T.2    Hagiwara, K.3    Kikuchi, A.4    Moriyasu, Y.5    Suzuki, N.6
  • 56
    • 39449121139 scopus 로고    scopus 로고
    • Endomembranes and myosin mediate assembly into tubules of Pns10 of Rice dwarf virus and intercellular spreading of the virus in cultured insect vector cells
    • Wei, T., Shimizu, T., and Omura, T. (2008a). Endomembranes and myosin mediate assembly into tubules of Pns10 of Rice dwarf virus and intercellular spreading of the virus in cultured insect vector cells. Virology 372, 349-356. doi: 10.1016/j.virol.2007.10.034
    • (2008) Virology , vol.372 , pp. 349-356
    • Wei, T.1    Shimizu, T.2    Omura, T.3
  • 57
    • 56349099753 scopus 로고    scopus 로고
    • Rice dwarf virus is engulfed into and released via vesicular compartments in cultured insect vector cells
    • Wei, T., Hibino, H., and Omura, T. (2008b). Rice dwarf virus is engulfed into and released via vesicular compartments in cultured insect vector cells. J. Gen. Virol. 89, 2915-2920. doi: 10.1099/vir.0.2008/ 002063-0
    • (2008) J. Gen. Virol. , vol.89 , pp. 2915-2920
    • Wei, T.1    Hibino, H.2    Omura, T.3
  • 58
    • 33645069960 scopus 로고
    • Movement protein of tobacco mosaic virus modifies plasmodesmatal size exclusion limit
    • Wolf, S., Deom, C. M., Beachy, R. N., and Lucas, W. J. (1989). Movement protein of tobacco mosaic virus modifies plasmodesmatal size exclusion limit. Science 246, 377-379. doi: 10.1126/science.246.4928.377
    • (1989) Science , vol.246 , pp. 377-379
    • Wolf, S.1    Deom, C.M.2    Beachy, R.N.3    Lucas, W.J.4
  • 59
    • 0032518480 scopus 로고    scopus 로고
    • Rice dwarf phytoreovirus segment S11 encodes a nucleic acid binding protein
    • Xu, H., Li, Y., Mao, Z., Li, Y., Wu, Z., Lin, Q., et al. (1998). Rice dwarf phytoreovirus segment S11 encodes a nucleic acid binding protein. Virology 240, 267-272. doi: 10.1006/viro.1997.8945
    • (1998) Virology , vol.240 , pp. 267-272
    • Xu, H.1    Li, Y.2    Mao, Z.3    Li, Y.4    Wu, Z.5    Lin, Q.6
  • 60
    • 0030588318 scopus 로고    scopus 로고
    • P2 protein encoded by genome segment S2 of Rice dwarf phytoreovirus is essential for virus infection
    • Yan, J., Tomaru, M., Takahashi, A., Kimura, I., Hibino, H., and Omura, T. (1996). P2 protein encoded by genome segment S2 of Rice dwarf phytoreovirus is essential for virus infection. Virology 224, 539-541. doi: 10.1006/viro.1996.0560
    • (1996) Virology , vol.224 , pp. 539-541
    • Yan, J.1    Tomaru, M.2    Takahashi, A.3    Kimura, I.4    Hibino, H.5    Omura, T.6
  • 62
    • 37649002522 scopus 로고    scopus 로고
    • The P2 capsid protein of the nonen-veloped Rice dwarf virus phytoreovirus induces membrane fusion in insect host cells
    • Zhou, F., Pu, Y., Wei, T., Liu, H., Deng, W., Wei, C., et al. (2007). The P2 capsid protein of the nonen-veloped Rice dwarf virus phytoreovirus induces membrane fusion in insect host cells. Proc. Natl. Acad. Sci. U. S. A. 104, 19547-19552. doi: 10.1073/pnas.070894 6104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19547-19552
    • Zhou, F.1    Pu, Y.2    Wei, T.3    Liu, H.4    Deng, W.5    Wei, C.6
  • 63
    • 77955890402 scopus 로고    scopus 로고
    • Stable expression of Rice dwarf virus Pns10 suppresses the post-transcriptional gene silencing in transgenic Nico-tiana benthamiana plants
    • Zhou, P., Ren, B., Zhang, X. M., Wang, Y., Wei, C. H., and Li, Y. (2010). Stable expression of Rice dwarf virus Pns10 suppresses the post-transcriptional gene silencing in transgenic Nico-tiana benthamiana plants. Acta Virol. 54, 99-104. doi: 10.4149/av_2010_ 02_99
    • (2010) Acta Virol , vol.54 , pp. 99-104
    • Zhou, P.1    Ren, B.2    Zhang, X.M.3    Wang, Y.4    Wei, C.H.5    Li, Y.6


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