메뉴 건너뛰기




Volumn 211, Issue , 2016, Pages 159-164

New insights about ORF1 coding regions support the proposition of a new genus comprising arthropod viruses in the family Totiviridae

Author keywords

Armigeres subalbatus virus; Double strand RNA viruses; Drosophila melanogaster virus; Giardia lamblia virus; Infectious myonecrosis virus

Indexed keywords

CAPSID PROTEIN; POLYPEPTIDE; VIRUS RNA; VIRAL PROTEIN;

EID: 84951733649     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2015.10.020     Document Type: Article
Times cited : (15)

References (42)
  • 1
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 2
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M., Grünert S., Murzin A.G., Proctor M., St Johnston D. NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 1995, 14(14):3563.
    • (1995) EMBO J. , vol.14 , Issue.14 , pp. 3563
    • Bycroft, M.1    Grünert, S.2    Murzin, A.G.3    Proctor, M.4    St Johnston, D.5
  • 3
    • 0035036348 scopus 로고    scopus 로고
    • Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein
    • Chandran K., Zhang X., Olson N.H., Walker S.B., Chappell J.D., Dermody T.S., Baker T.S., Nibert M.L. Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein. J. Virol. 2001, 75:5335-5342.
    • (2001) J. Virol. , vol.75 , pp. 5335-5342
    • Chandran, K.1    Zhang, X.2    Olson, N.H.3    Walker, S.B.4    Chappell, J.D.5    Dermody, T.S.6    Baker, T.S.7    Nibert, M.L.8
  • 4
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein σ1 revels evolutionary relationchip to adenovirus fiber
    • Chappell J.D., Prota A.E., Dermody T.S., Stehle T. Crystal structure of reovirus attachment protein σ1 revels evolutionary relationchip to adenovirus fiber. EMBO J. 2002, 21:1-11.
    • (2002) EMBO J. , vol.21 , pp. 1-11
    • Chappell, J.D.1    Prota, A.E.2    Dermody, T.S.3    Stehle, T.4
  • 6
    • 84930788324 scopus 로고    scopus 로고
    • Analysis of new isolates reveals new genome organization and a hypervariable region in infectious myonecrosis virus (IMNV)
    • Dantas M.D.A., Chavante S.F., Teixeira D.I.A., Lima J.P.M., Lanza D.C. Analysis of new isolates reveals new genome organization and a hypervariable region in infectious myonecrosis virus (IMNV). Virus Res. 2015, 203:66-71.
    • (2015) Virus Res. , vol.203 , pp. 66-71
    • Dantas, M.D.A.1    Chavante, S.F.2    Teixeira, D.I.A.3    Lima, J.P.M.4    Lanza, D.C.5
  • 7
    • 79961228943 scopus 로고    scopus 로고
    • Crystal structure of the human astrovirus capsid spike
    • Dong J., Dong L., Méndez E., Tao Y. Crystal structure of the human astrovirus capsid spike. Proc. Natl. Acad. Sci. U. S. A. 2011, 108(31):12681-12686.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.31 , pp. 12681-12686
    • Dong, J.1    Dong, L.2    Méndez, E.3    Tao, Y.4
  • 8
    • 0035005706 scopus 로고    scopus 로고
    • The 'cleavage'activities of foot-and-mouth disease virus 2A site-directed mutants and naturally occurring '2A-like'sequences
    • Donnelly M.L., Hughes L.E., Luke G., Mendoza H., ten Dam E., Gani D., Ryan M.D. The 'cleavage'activities of foot-and-mouth disease virus 2A site-directed mutants and naturally occurring '2A-like'sequences. J. Gen. Virol. 2001, 82(5):1027-1041.
    • (2001) J. Gen. Virol. , vol.82 , Issue.5 , pp. 1027-1041
    • Donnelly, M.L.1    Hughes, L.E.2    Luke, G.3    Mendoza, H.4    ten Dam, E.5    Gani, D.6    Ryan, M.D.7
  • 10
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucl. Acids Res. 2004, 32(5):1792-1797.
    • (2004) Nucl. Acids Res. , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 11
    • 79956132830 scopus 로고    scopus 로고
    • Cardiomyopathy syndrome of Atlantic salmon (Salmo salar L.) is caused by a double-stranded RNA virus of the Totiviridae family
    • Haugland O., Mikalsen A.B., Nilsen P., Lindmo K., Thu B.J., Eliassen T.M., Roos N., Rode M., Evensen O. Cardiomyopathy syndrome of Atlantic salmon (Salmo salar L.) is caused by a double-stranded RNA virus of the Totiviridae family. J. Virol. 2011, 8:5275-5286.
    • (2011) J. Virol. , vol.8 , pp. 5275-5286
    • Haugland, O.1    Mikalsen, A.B.2    Nilsen, P.3    Lindmo, K.4    Thu, B.J.5    Eliassen, T.M.6    Roos, N.7    Rode, M.8    Evensen, O.9
  • 12
    • 84934894169 scopus 로고    scopus 로고
    • Virus Taxonomy: 2014 Release
    • (accessed 13.07.15).
    • ICTV-International Committee on Taxonomy of Viruses. Virus Taxonomy: 2014 Release. <>(accessed 13.07.15). http://www.ictvonline.org/virusTaxonomy.asp.
  • 15
    • 84900036094 scopus 로고    scopus 로고
    • Different activities of the conserved lysine residues in the double-stranded RNA binding domains of RNA helicase A in vitro and in the cell
    • Li X., Niu M., Zhao X., Kleiman L. Different activities of the conserved lysine residues in the double-stranded RNA binding domains of RNA helicase A in vitro and in the cell. Biochim. Biophys. Acta 2014, 1840:2234-2243.
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 2234-2243
    • Li, X.1    Niu, M.2    Zhao, X.3    Kleiman, L.4
  • 17
    • 17044438215 scopus 로고    scopus 로고
    • The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture
    • Merckel M.C., Huiskonen J.T., Bamford D.H., Goldman A., Tuma R. The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture. Mol. Cell 2005, 18(2):161-170.
    • (2005) Mol. Cell , vol.18 , Issue.2 , pp. 161-170
    • Merckel, M.C.1    Huiskonen, J.T.2    Bamford, D.H.3    Goldman, A.4    Tuma, R.5
  • 19
    • 0032530310 scopus 로고    scopus 로고
    • Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation
    • Nanduri S., Carpick B.W., Yang Y., Williams B.R., Qin J. Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation. EMBO J. 1998, 18:5458-5465.
    • (1998) EMBO J. , vol.18 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.3    Williams, B.R.4    Qin, J.5
  • 20
    • 34047133271 scopus 로고    scopus 로고
    • '2A-like' and 'shifty heptamer' motifs in penaeid shrimp infectious myonecrosis virus, a monosegmented double-stranded RNA virus
    • Nibert M.L. '2A-like' and 'shifty heptamer' motifs in penaeid shrimp infectious myonecrosis virus, a monosegmented double-stranded RNA virus. J. Gen. Virol. 2007, 88(4):1315-1318.
    • (2007) J. Gen. Virol. , vol.88 , Issue.4 , pp. 1315-1318
    • Nibert, M.L.1
  • 21
    • 84874650792 scopus 로고    scopus 로고
    • Fibers come and go: differences in cell-entry components among related dsRNA viruses
    • Nibert M.L., Takagi Y. Fibers come and go: differences in cell-entry components among related dsRNA viruses. Curr. Opin. Virol. 2013, 3(1):20-26.
    • (2013) Curr. Opin. Virol. , vol.3 , Issue.1 , pp. 20-26
    • Nibert, M.L.1    Takagi, Y.2
  • 22
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: a novel method for fast and accurate multiple sequence alignment
    • Notredame C., Higgins D.G., Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 2000, 302(1):205-217.
    • (2000) J. Mol. Biol. , vol.302 , Issue.1 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 23
    • 84904271146 scopus 로고    scopus 로고
    • In silico single strand melting curve: a new approach to identify nucleic acid polymorphisms in Totiviridae
    • Oliveira R.A., Almeida R.V., Dantas M.D., Castro F.N., Lima J.P.M., Lanza D.C. In silico single strand melting curve: a new approach to identify nucleic acid polymorphisms in Totiviridae. BMC Bioinform. 2014, 15(1):243.
    • (2014) BMC Bioinform. , vol.15 , Issue.1 , pp. 243
    • Oliveira, R.A.1    Almeida, R.V.2    Dantas, M.D.3    Castro, F.N.4    Lima, J.P.M.5    Lanza, D.C.6
  • 24
    • 0026758421 scopus 로고
    • Proteolytic processing of the cardioviral P2 region: primary 2A/2B cleavage in clone-derived precursors
    • Palmenberg A.C., Parks G.D., Hall D.J., Ingraham R.H., Seng T.W., Pallai P.V. Proteolytic processing of the cardioviral P2 region: primary 2A/2B cleavage in clone-derived precursors. Virology 1992, 190(2):754-762.
    • (1992) Virology , vol.190 , Issue.2 , pp. 754-762
    • Palmenberg, A.C.1    Parks, G.D.2    Hall, D.J.3    Ingraham, R.H.4    Seng, T.W.5    Pallai, P.V.6
  • 25
    • 0026056961 scopus 로고
    • Formation and intracellular transport of a heterodimeric viral spike protein complex
    • Persson R., Pettersson R.F. Formation and intracellular transport of a heterodimeric viral spike protein complex. J. Cell Biol. 1991, 112(2):257-266.
    • (1991) J. Cell Biol. , vol.112 , Issue.2 , pp. 257-266
    • Persson, R.1    Pettersson, R.F.2
  • 26
    • 33645550079 scopus 로고    scopus 로고
    • Purification and characterization of infectious myonecrosis virus of penaeid shrimp
    • Poulos B.T., Tang K.F., Pantoja C.R., Bonami J.R., Lightner D.V. Purification and characterization of infectious myonecrosis virus of penaeid shrimp. J. Gen. Virol. 2006, 87(4):987-996.
    • (2006) J. Gen. Virol. , vol.87 , Issue.4 , pp. 987-996
    • Poulos, B.T.1    Tang, K.F.2    Pantoja, C.R.3    Bonami, J.R.4    Lightner, D.V.5
  • 28
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A., Kucukural A., Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 2010, 5(4):725-738.
    • (2010) Nat. Protoc. , vol.5 , Issue.4 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 29
    • 0028867257 scopus 로고
    • The complete sequence of Leishmania RNA virus LRV2-1, a virus of an Old World parasite strain
    • Scheffter S.M., Ro Y.T., Chung I.K., Patterson J.L. The complete sequence of Leishmania RNA virus LRV2-1, a virus of an Old World parasite strain. Virology 1995, 212(1):84-90.
    • (1995) Virology , vol.212 , Issue.1 , pp. 84-90
    • Scheffter, S.M.1    Ro, Y.T.2    Chung, I.K.3    Patterson, J.L.4
  • 31
    • 32044468729 scopus 로고    scopus 로고
    • Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs
    • Stefl R., Xu M., Skrisovska L., Emeson R.B., Allain F.H.T. Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs. Structure 2006, 14(2):345-355.
    • (2006) Structure , vol.14 , Issue.2 , pp. 345-355
    • Stefl, R.1    Xu, M.2    Skrisovska, L.3    Emeson, R.B.4    Allain, F.H.T.5
  • 33
    • 16344378145 scopus 로고    scopus 로고
    • In situ hybridization demonstrates that Litopenaeus vannamei, L. stylirostris and Penaeus monodon are susceptible to experimental infection with infectious myonecrosis virus (IMNV)
    • Tang K.F., Pantoja C.R., Poulos B.T., Redman R.M., Lightner D.V. In situ hybridization demonstrates that Litopenaeus vannamei, L. stylirostris and Penaeus monodon are susceptible to experimental infection with infectious myonecrosis virus (IMNV). Dis. Aquat. Org. 2005, 63:261-265.
    • (2005) Dis. Aquat. Org. , vol.63 , pp. 261-265
    • Tang, K.F.1    Pantoja, C.R.2    Poulos, B.T.3    Redman, R.M.4    Lightner, D.V.5
  • 34
    • 0033613385 scopus 로고    scopus 로고
    • A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
    • van Raaij M.J., Mitraki A., Lavigne G., Cusack S. A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature 1999, 401:935-938.
    • (1999) Nature , vol.401 , pp. 935-938
    • van Raaij, M.J.1    Mitraki, A.2    Lavigne, G.3    Cusack, S.4
  • 35
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2-a multiple sequence alignment editor and analysis workbench
    • Waterhouse A.M., Procter J.B., Martin D.M., Clamp M., Barton G.J. Jalview Version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics 2009, 25(9):1189-1191.
    • (2009) Bioinformatics , vol.25 , Issue.9 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 37
    • 76249103869 scopus 로고    scopus 로고
    • Virus discovery by deep sequencing and assembly of virus-derived small silencing RNAs
    • Wu Q., Luo Y., Lu R., Lau N., Lai E.C., Li W.X., Ding S.W. Virus discovery by deep sequencing and assembly of virus-derived small silencing RNAs. Proc. Natl. Acad. Sci. U. S. A. 2010, 107(4):1606-1611.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.4 , pp. 1606-1611
    • Wu, Q.1    Luo, Y.2    Lu, R.3    Lau, N.4    Lai, E.C.5    Li, W.X.6    Ding, S.W.7
  • 38
    • 84862828125 scopus 로고    scopus 로고
    • A novel totivirus-like virus isolated from bat guano
    • Yang X., Zhang Y., Ge X., Yuan J., Shi Z. A novel totivirus-like virus isolated from bat guano. Arch. Virol. 2012, 157(6):1093-1099.
    • (2012) Arch. Virol. , vol.157 , Issue.6 , pp. 1093-1099
    • Yang, X.1    Zhang, Y.2    Ge, X.3    Yuan, J.4    Shi, Z.5
  • 39
    • 0028205688 scopus 로고
    • Threedimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis
    • Yeager M., Berriman J.A., Baker T.S., Bellamy A.R. Threedimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis. EMBO J. 1994, 13:1011-1018.
    • (1994) EMBO J. , vol.13 , pp. 1011-1018
    • Yeager, M.1    Berriman, J.A.2    Baker, T.S.3    Bellamy, A.R.4
  • 40
    • 78049390214 scopus 로고    scopus 로고
    • Isolation and full-length sequence analysis of Armigeres subalbatus totivirus, the first totivirus isolate from mosquitoes representing a proposed novel genus (Artivirus) of the family Totiviridae
    • Zhai Y., Attoui H., Jaafar F.M., Wang H.Q., Cao Y.X., Fan S.P., Sun Y.X., Liu L.D., Mertens P.P., Meng W.S., Wang D., Liang G. Isolation and full-length sequence analysis of Armigeres subalbatus totivirus, the first totivirus isolate from mosquitoes representing a proposed novel genus (Artivirus) of the family Totiviridae. J. Gen. Virol. 2010, 91(11):2836-2845.
    • (2010) J. Gen. Virol. , vol.91 , Issue.11 , pp. 2836-2845
    • Zhai, Y.1    Attoui, H.2    Jaafar, F.M.3    Wang, H.Q.4    Cao, Y.X.5    Fan, S.P.6    Sun, Y.X.7    Liu, L.D.8    Mertens, P.P.9    Meng, W.S.10    Wang, D.11    Liang, G.12
  • 41
    • 27644594455 scopus 로고    scopus 로고
    • Structure of avian orthoreovirus virion by electron cryomicroscopy and image reconstruction
    • Zhang X., Tang J., Walker S.B., O'Hara D., Nibert M.L., Duncan R., Baker T.S. Structure of avian orthoreovirus virion by electron cryomicroscopy and image reconstruction. Virology 2005, 343:25-35.
    • (2005) Virology , vol.343 , pp. 25-35
    • Zhang, X.1    Tang, J.2    Walker, S.B.3    O'Hara, D.4    Nibert, M.L.5    Duncan, R.6    Baker, T.S.7
  • 42
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinform. 2008, 9(1):40.
    • (2008) BMC Bioinform. , vol.9 , Issue.1 , pp. 40
    • Zhang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.