메뉴 건너뛰기




Volumn 11, Issue 10, 2015, Pages

Crystal Structures of a Piscine Betanodavirus: Mechanisms of Capsid Assembly and Viral Infection

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CALCIUM ION; CAPSID PROTEIN; MACROGOL; VIRUS RNA; WATER; CALCIUM; MACROGOL DERIVATIVE;

EID: 84946050691     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005203     Document Type: Article
Times cited : (111)

References (72)
  • 1
    • 0037123639 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerases, viruses, and RNA silencing
    • Ahlquist P, RNA-dependent RNA polymerases, viruses, and RNA silencing. Science. 2002;296: 1270–1273. 12016304
    • (2002) Science , vol.296 , pp. 1270-1273
    • Ahlquist, P.1
  • 2
    • 33646826348 scopus 로고    scopus 로고
    • Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses
    • Ahlquist P, Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses. Nat Rev Microbiol. 2005;4: 371–382.
    • (2005) Nat Rev Microbiol , vol.4 , pp. 371-382
    • Ahlquist, P.1
  • 4
    • 84885635441 scopus 로고    scopus 로고
    • RNA interference functions as an antiviral immunity mechanism in mammals
    • Li Y, Lu JF, Han YH, Fan XX, Ding SW, RNA interference functions as an antiviral immunity mechanism in mammals. Science. 2013;342: 231–234. doi: 10.1126/science.1241911 24115437
    • (2013) Science , vol.342 , pp. 231-234
    • Li, Y.1    Lu, J.F.2    Han, Y.H.3    Fan, X.X.4    Ding, S.W.5
  • 5
    • 23944506789 scopus 로고    scopus 로고
    • Animal virus replication and RNAi-mediated antiviral silencing in Caenorhabditis elegans
    • Lu R, Maduro M, Li F, Li HW, Broitman-Maduro G, Li WX, et al. Animal virus replication and RNAi-mediated antiviral silencing in Caenorhabditis elegans. Nature. 2005;436: 1040–1043. 16107851
    • (2005) Nature , vol.436 , pp. 1040-1043
    • Lu, R.1    Maduro, M.2    Li, F.3    Li, H.W.4    Broitman-Maduro, G.5    Li, W.X.6
  • 6
    • 34547828851 scopus 로고    scopus 로고
    • Identification of critical residues in nervous necrosis virus B2 for dsRNA-binding and RNAi-inhibiting activity through by bioinformatic analysis and mutagenesis
    • Ou MC, Chen YM, Jeng MF, Chu CJ, Yang HL, Chen TY, Identification of critical residues in nervous necrosis virus B2 for dsRNA-binding and RNAi-inhibiting activity through by bioinformatic analysis and mutagenesis. Biochem Bioph Res Co. 2007;361: 634–640.
    • (2007) Biochem Bioph Res Co , vol.361 , pp. 634-640
    • Ou, M.C.1    Chen, Y.M.2    Jeng, M.F.3    Chu, C.J.4    Yang, H.L.5    Chen, T.Y.6
  • 7
    • 5444234221 scopus 로고    scopus 로고
    • Genomic classification of new betanodavirus isolates by phylogenetic analysis of the coat protein gene suggests a low host-fish species specificity
    • Thiery R, Cozien J, de Boisseson C, Kerbart-Boscher S, Nevarez L, Genomic classification of new betanodavirus isolates by phylogenetic analysis of the coat protein gene suggests a low host-fish species specificity. J Gen Virol. 2004;85: 3079–3087. 15448371
    • (2004) J Gen Virol , vol.85 , pp. 3079-3087
    • Thiery, R.1    Cozien, J.2    de Boisseson, C.3    Kerbart-Boscher, S.4    Nevarez, L.5
  • 8
    • 84987476986 scopus 로고
    • Viral nervous necrosis in hatchery-reared larvae and juveniles of Japanese parrotfish, Oplegnathus fasciatus (Temminck and Schlegel)
    • Yoshikoshi K, Inoue K, Viral nervous necrosis in hatchery-reared larvae and juveniles of Japanese parrotfish, Oplegnathus fasciatus (Temminck and Schlegel). J Fish Dis. 1990;13: 69–77.
    • (1990) J Fish Dis , vol.13 , pp. 69-77
    • Yoshikoshi, K.1    Inoue, K.2
  • 9
    • 0036208869 scopus 로고    scopus 로고
    • Betanodavirus infections of teleost fish: a review
    • Munday BL, Kwang J, Moody N, Betanodavirus infections of teleost fish: a review. J Fish Dis. 2002;25: 127–142.
    • (2002) J Fish Dis , vol.25 , pp. 127-142
    • Munday, B.L.1    Kwang, J.2    Moody, N.3
  • 10
    • 0030907218 scopus 로고    scopus 로고
    • Genomic classification of fish nodaviruses by molecular phylogenetic analysis of the coat protein gene
    • Nishizawa T, Furuhashi M, Nagai T, Nakai T, Muroga K, Genomic classification of fish nodaviruses by molecular phylogenetic analysis of the coat protein gene. Appl Environ Microb. 1997;63: 1633–1636.
    • (1997) Appl Environ Microb , vol.63 , pp. 1633-1636
    • Nishizawa, T.1    Furuhashi, M.2    Nagai, T.3    Nakai, T.4    Muroga, K.5
  • 11
    • 84908388846 scopus 로고    scopus 로고
    • A unique nodavirus with novel features: mosinovirus expresses two subgenomic RNAs, a capsid gene of unknown origin, and a suppressor of the antiviral RNA interference pathway
    • Schuster S, Zirkel F, Kurth A, van Cleef KWR, Drosten C, van Rij RP, et al. A unique nodavirus with novel features: mosinovirus expresses two subgenomic RNAs, a capsid gene of unknown origin, and a suppressor of the antiviral RNA interference pathway. J Virol. 2014;88: 13447–13459. doi: 10.1128/JVI.02144-14 25210176
    • (2014) J Virol , vol.88 , pp. 13447-13459
    • Schuster, S.1    Zirkel, F.2    Kurth, A.3    van Cleef, K.W.R.4    Drosten, C.5    van Rij, R.P.6
  • 12
    • 79956306174 scopus 로고    scopus 로고
    • Ultrastructural and sequence characterization of Penaeus vannamei nodavirus (PvNV) from Belize
    • Tang KF, Pantoja CR, Redman RM, Navarro SA, Lightner DV, Ultrastructural and sequence characterization of Penaeus vannamei nodavirus (PvNV) from Belize. Dis Aquat Organ. 2011;94: 179–187 doi: 10.3354/dao02335 21790065
    • (2011) Dis Aquat Organ , vol.94 , pp. 179-187
    • Tang, K.F.1    Pantoja, C.R.2    Redman, R.M.3    Navarro, S.A.4    Lightner, D.V.5
  • 13
    • 84874762174 scopus 로고    scopus 로고
    • Viral capsid proteins are segregated in structural fold space
    • Cheng SS, Brooks CL, Viral capsid proteins are segregated in structural fold space. PLoS Comput Biol. 2013;9: e1002905. doi: 10.1371/journal.pcbi.1002905 23408879
    • (2013) PLoS Comput Biol , vol.9 , pp. e1002905
    • Cheng, S.S.1    Brooks, C.L.2
  • 14
    • 0026757341 scopus 로고
    • Maturation cleavage required for infectivity of a nodavirus
    • Schneemann A, Zhong WD, Gallagher TM, Rueckert RR, Maturation cleavage required for infectivity of a nodavirus. J Virol. 1992;66: 6728–6734. 1404613
    • (1992) J Virol , vol.66 , pp. 6728-6734
    • Schneemann, A.1    Zhong, W.D.2    Gallagher, T.M.3    Rueckert, R.R.4
  • 16
    • 0027518457 scopus 로고
    • Ordered duplex RNA controls capsid architecture in an icosahedral animal virus
    • Fisher AJ, Johnson JE, Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature. 1993;361: 176–179. 8421524
    • (1993) Nature , vol.361 , pp. 176-179
    • Fisher, A.J.1    Johnson, J.E.2
  • 17
    • 0031776460 scopus 로고    scopus 로고
    • Particle polymorphism caused by deletion of a peptide molecular switch in a quasi-equivalent icosahedral virus
    • Dong XF, Natarajan P, Tihova M, Johnson JE, Schneemann A, Particle polymorphism caused by deletion of a peptide molecular switch in a quasi-equivalent icosahedral virus. J Virol. 1998;72: 6024–6033. 9621065
    • (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
  • 18
    • 0036115177 scopus 로고    scopus 로고
    • Virus-like particles of a fish nodavirus display a capsid subunit domain organization different from that of insect nodaviruses
    • Tang L, Lin CS, Krishna NK, Yeager M, Schneemann A, Johnson JE, Virus-like particles of a fish nodavirus display a capsid subunit domain organization different from that of insect nodaviruses. J Virol. 2002;76: 6370–6375. 12021370
    • (2002) J Virol , vol.76 , pp. 6370-6375
    • Tang, L.1    Lin, C.S.2    Krishna, N.K.3    Yeager, M.4    Schneemann, A.5    Johnson, J.E.6
  • 19
    • 0034435933 scopus 로고    scopus 로고
    • 3D domain swapping modulates the stability of members of an icosahedral virus group
    • Qu CX, Liljas L, Opalka N, Brugidou C, Yeager M, Beachy RN, et al. 3D domain swapping modulates the stability of members of an icosahedral virus group. Structure. 2000;8: 1095–1103. 11080631
    • (2000) Structure , vol.8 , pp. 1095-1103
    • Qu, C.X.1    Liljas, L.2    Opalka, N.3    Brugidou, C.4    Yeager, M.5    Beachy, R.N.6
  • 20
    • 42749093687 scopus 로고    scopus 로고
    • Structure of recombinant capsids formed by the beta-annulus deletion mutant–rCP (Delta 48–59) of Sesbania mosaic virus
    • Pappachan A, Subashchandrabose C, Satheshkumar PS, Savithri HS, Murthy MRN, Structure of recombinant capsids formed by the beta-annulus deletion mutant–rCP (Delta 48–59) of Sesbania mosaic virus. Virology. 2008;375: 190–196. doi: 10.1016/j.virol.2008.01.023 18295296
    • (2008) Virology , vol.375 , pp. 190-196
    • Pappachan, A.1    Subashchandrabose, C.2    Satheshkumar, P.S.3    Savithri, H.S.4    Murthy, M.R.N.5
  • 21
    • 25144474643 scopus 로고    scopus 로고
    • The role of arginine-rich motif and beta-annulus in the assembly and stability of Sesbania mosaic virus capsids
    • Satheshkumar PS, Lokesh GL, Murthy MRN, Savithri HS, The role of arginine-rich motif and beta-annulus in the assembly and stability of Sesbania mosaic virus capsids. J Mol Biol. 2005;353: 447–458. 16169007
    • (2005) J Mol Biol , vol.353 , pp. 447-458
    • Satheshkumar, P.S.1    Lokesh, G.L.2    Murthy, M.R.N.3    Savithri, H.S.4
  • 22
    • 33744494819 scopus 로고    scopus 로고
    • X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity
    • Chen R, Neill JD, Estes MK, Prasad BVV, X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity. Proc Natl Acad Sci USA. 2006;103: 8048–8053. 16702551
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8048-8053
    • Chen, R.1    Neill, J.D.2    Estes, M.K.3    Prasad, B.V.V.4
  • 23
    • 0028871926 scopus 로고
    • Dali: a network tool for protein-structure comparison
    • Holm L, Sander C, Dali: a network tool for protein-structure comparison. Trends Biochem Sci. 1995;20: 478–480. 8578593
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 26
    • 84858168537 scopus 로고    scopus 로고
    • Principles of virus structural organization
    • Prasad BVV, Schmid MF, Principles of virus structural organization. Adv Exp Med Biol. 2012;726: 17–47. doi: 10.1007/978-1-4614-0980-9_3 22297509
    • (2012) Adv Exp Med Biol , vol.726 , pp. 17-47
    • Prasad, B.V.V.1    Schmid, M.F.2
  • 27
    • 77950789977 scopus 로고    scopus 로고
    • Structure and function of a genetically engineered mimic of a nonenveloped virus entry intermediate
    • Banerjee M, Speir JA, Kwan MH, Huang R, Aryanpur PP, Bothner B, et al. Structure and function of a genetically engineered mimic of a nonenveloped virus entry intermediate. J Virol. 2010;84: 4737–4746. doi: 10.1128/JVI.02670-09 20164221
    • (2010) J Virol , vol.84 , pp. 4737-4746
    • Banerjee, M.1    Speir, J.A.2    Kwan, M.H.3    Huang, R.4    Aryanpur, P.P.5    Bothner, B.6
  • 28
    • 84886256460 scopus 로고    scopus 로고
    • Atomic structure of Cucumber necrosis virus and the role of the capsid in vector transmission
    • Li M, Kakani K, Katpally U, Johnson S, Rochon D, Smith TJ, Atomic structure of Cucumber necrosis virus and the role of the capsid in vector transmission. J Virol. 2013;87: 12166–12175. doi: 10.1128/JVI.01965-13 24006433
    • (2013) J Virol , vol.87 , pp. 12166-12175
    • Li, M.1    Kakani, K.2    Katpally, U.3    Johnson, S.4    Rochon, D.5    Smith, T.J.6
  • 30
    • 0021112767 scopus 로고
    • Divalent-cation sites in tomato bushy stunt virus—difference maps at 2.9 Å resolution
    • Hogle J, Kirchhausen T, Harrison SC, Divalent-cation sites in tomato bushy stunt virus—difference maps at 2.9 Å resolution. J Mol Biol. 1983;171: 95–100. 6417343
    • (1983) J Mol Biol , vol.171 , pp. 95-100
    • Hogle, J.1    Kirchhausen, T.2    Harrison, S.C.3
  • 31
    • 4444284258 scopus 로고    scopus 로고
    • Role of metal ion-mediated interactions in the assembly and stability of Sesbania mosaic virus T = 3 and T = 1 capsids
    • Satheshkumar PS, Lokesh GL, Sangita V, Saravanan V, Vijay CS, Murthy MRN, et al. Role of metal ion-mediated interactions in the assembly and stability of Sesbania mosaic virus T = 3 and T = 1 capsids. J Mol Biol. 2004;342: 1001–1014. 15342252
    • (2004) J Mol Biol , vol.342 , pp. 1001-1014
    • Satheshkumar, P.S.1    Lokesh, G.L.2    Sangita, V.3    Saravanan, V.4    Vijay, C.S.5    Murthy, M.R.N.6
  • 32
    • 0027953618 scopus 로고
    • The refined three-dimensional structure of an insect virus at 2.8 Å resolution
    • Wery JP, Reddy VS, Hosur MV, Johnson JE, The refined three-dimensional structure of an insect virus at 2.8 Å resolution. J Mol Biol. 1994;235: 565–586. 8289282
    • (1994) J Mol Biol , vol.235 , pp. 565-586
    • Wery, J.P.1    Reddy, V.S.2    Hosur, M.V.3    Johnson, J.E.4
  • 33
    • 69149085271 scopus 로고    scopus 로고
    • Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding
    • Guu TSY, Liu Z, Ye QZ, Mata DA, Li KP, Yin CC, et al. Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding. Proc Natl Acad Sci USA. 2009;106: 12992–12997. doi: 10.1073/pnas.0904848106 19622744
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12992-12997
    • Guu, T.S.Y.1    Liu, Z.2    Ye, Q.Z.3    Mata, D.A.4    Li, K.P.5    Yin, C.C.6
  • 34
    • 69149100932 scopus 로고    scopus 로고
    • Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure
    • Yamashita T, Mori Y, Miyazaki N, Cheng RH, Yoshimura M, Unno H, et al. Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure. Proc Natl Acad Sci USA. 2009;106: 12986–12991. doi: 10.1073/pnas.0903699106 19620712
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12986-12991
    • Yamashita, T.1    Mori, Y.2    Miyazaki, N.3    Cheng, R.H.4    Yoshimura, M.5    Unno, H.6
  • 35
    • 32944475390 scopus 로고    scopus 로고
    • Structure of a mutant T = 1 capsid of Sesbania mosaic virus: role of water molecules in capsid architecture and integrity
    • Sangita V, Satheshkumar PS, Savithri HS, Murthy MRN, Structure of a mutant T = 1 capsid of Sesbania mosaic virus: role of water molecules in capsid architecture and integrity. Acta Crystallogr D Biol Crystallogr. 2005;61: 1406–1412. 16204894
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 1406-1412
    • Sangita, V.1    Satheshkumar, P.S.2    Savithri, H.S.3    Murthy, M.R.N.4
  • 36
    • 36949038870 scopus 로고    scopus 로고
    • Hepatitis B virus infection initiates with a large surface protein-dependent binding to heparan sulfate proteoglycans
    • Schulze A, Gripon P, Urban S, Hepatitis B virus infection initiates with a large surface protein-dependent binding to heparan sulfate proteoglycans. Hepatology. 2007;46: 1759–1768. 18046710
    • (2007) Hepatology , vol.46 , pp. 1759-1768
    • Schulze, A.1    Gripon, P.2    Urban, S.3
  • 37
    • 33749462736 scopus 로고    scopus 로고
    • The structural and functional role of RNA in icosahedral virus assembly
    • Schneemann A, The structural and functional role of RNA in icosahedral virus assembly. Annu Rev Microbiol. 2006;60: 51–67. 16704342
    • (2006) Annu Rev Microbiol , vol.60 , pp. 51-67
    • Schneemann, A.1
  • 38
    • 4444242208 scopus 로고    scopus 로고
    • T = 1 capsid structures of Sesbania mosaic virus coat protein mutants: determinants of T = 3 and T = 1 capsid assembly
    • Sangita V, Lokesh GL, Satheshkumar PS, Vijay CS, Saravanan V, Savithri HS, et al. T = 1 capsid structures of Sesbania mosaic virus coat protein mutants: determinants of T = 3 and T = 1 capsid assembly. J Mol Biol. 2004;342: 1402–1405.
    • (2004) J Mol Biol , vol.342 , pp. 1402-1405
    • Sangita, V.1    Lokesh, G.L.2    Satheshkumar, P.S.3    Vijay, C.S.4    Saravanan, V.5    Savithri, H.S.6
  • 40
    • 0023645549 scopus 로고
    • Refined structure of southern bean mosaic-virus at 2.9 Å resolution
    • Silva AM, Rossmann MG, Refined structure of southern bean mosaic-virus at 2.9 Å resolution. J Mol Biol. 1987;197: 69–87. 3681993
    • (1987) J Mol Biol , vol.197 , pp. 69-87
    • Silva, A.M.1    Rossmann, M.G.2
  • 41
    • 84887269915 scopus 로고    scopus 로고
    • Structures of B-lymphotropic polyomavirus VP1 in complex with oligosaccharide ligands
    • Neu U, Khan ZM, Schuch B, Palma AS, Liu Y, Pawlita M, et al. Structures of B-lymphotropic polyomavirus VP1 in complex with oligosaccharide ligands. PLoS Pathog. 2013;9: e1003714. doi: 10.1371/journal.ppat.1003714 24204265
    • (2013) PLoS Pathog , vol.9 , pp. e1003714
    • Neu, U.1    Khan, Z.M.2    Schuch, B.3    Palma, A.S.4    Liu, Y.5    Pawlita, M.6
  • 42
    • 0035794638 scopus 로고    scopus 로고
    • Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion
    • Mathieu M, Petitpas I, Navaza J, Lepault J, Kohli E, Pothier P, et al. Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion. EMBO J. 2001;20: 1485–1497. 11285213
    • (2001) EMBO J , vol.20 , pp. 1485-1497
    • Mathieu, M.1    Petitpas, I.2    Navaza, J.3    Lepault, J.4    Kohli, E.5    Pothier, P.6
  • 43
    • 50849096677 scopus 로고    scopus 로고
    • Role of the DxxDxD motif in the assembly and stability of betanodavirus particles
    • Wu YM, Hsu CH, Wang CH, Liu WT, Chang WH, Lin CS, Role of the DxxDxD motif in the assembly and stability of betanodavirus particles. Arch Virol. 2008;53: 1633–1642.
    • (2008) Arch Virol , vol.53 , pp. 1633-1642
    • Wu, Y.M.1    Hsu, C.H.2    Wang, C.H.3    Liu, W.T.4    Chang, W.H.5    Lin, C.S.6
  • 44
    • 0026489233 scopus 로고
    • Anatomy and evolution of proteins displaying the viral capsid jellyroll topology
    • Chelvanayagam G, Heringa J, Argos P, Anatomy and evolution of proteins displaying the viral capsid jellyroll topology. J Mol Biol 1992;228: 220–242. 1447783
    • (1992) J Mol Biol , vol.228 , pp. 220-242
    • Chelvanayagam, G.1    Heringa, J.2    Argos, P.3
  • 45
    • 77953870682 scopus 로고    scopus 로고
    • Roles of cysteines Cys115 and Cys201 in the assembly and thermostability of grouper betanodavirus particles
    • Wang CH, Hsu CH, Wu YM, Luo YC, Tu MH, Chang WH, et al. Roles of cysteines Cys115 and Cys201 in the assembly and thermostability of grouper betanodavirus particles. Virus Genes. 2010;41: 73–80. doi: 10.1007/s11262-010-0488-1 20446029
    • (2010) Virus Genes , vol.41 , pp. 73-80
    • Wang, C.H.1    Hsu, C.H.2    Wu, Y.M.3    Luo, Y.C.4    Tu, M.H.5    Chang, W.H.6
  • 47
    • 17644376907 scopus 로고    scopus 로고
    • The birnavirus crystal structure reveals structural relationships among icosahedral viruses
    • Coulibaly F, Chevalier C, Gutsche I, Pous J, Navaza J, Bressanelli S, et al. The birnavirus crystal structure reveals structural relationships among icosahedral viruses. Cell. 2005;120: 761–772. 15797378
    • (2005) Cell , vol.120 , pp. 761-772
    • Coulibaly, F.1    Chevalier, C.2    Gutsche, I.3    Pous, J.4    Navaza, J.5    Bressanelli, S.6
  • 48
    • 44949202387 scopus 로고    scopus 로고
    • Variable region of betanodavirus RNA2 is sufficient to determine host specificity
    • Ito Y, Okinaka Y, Mori KI, Sugaya T, Nishioka T, Oka M, et al. Variable region of betanodavirus RNA2 is sufficient to determine host specificity. Dis Aquat Organ. 2008;79: 199–205. doi: 10.3354/dao01906 18589996
    • (2008) Dis Aquat Organ , vol.79 , pp. 199-205
    • Ito, Y.1    Okinaka, Y.2    Mori, K.I.3    Sugaya, T.4    Nishioka, T.5    Oka, M.6
  • 49
    • 84876205224 scopus 로고    scopus 로고
    • Chromatographically-purified capsid proteins of red-spotted grouper nervous necrosis virus expressed in Saccharomyces cerevisiae form virus-like particles
    • Choi YR, Kim HJ, Lee JY, Kang HA, Kim HJ, Chromatographically-purified capsid proteins of red-spotted grouper nervous necrosis virus expressed in Saccharomyces cerevisiae form virus-like particles. Protein Expres Purif. 2013;89: 162–168.
    • (2013) Protein Expres Purif , vol.89 , pp. 162-168
    • Choi, Y.R.1    Kim, H.J.2    Lee, J.Y.3    Kang, H.A.4    Kim, H.J.5
  • 50
    • 38449106713 scopus 로고    scopus 로고
    • Penetration of nonenveloped viruses into the cytoplasm
    • Tsai B, Penetration of nonenveloped viruses into the cytoplasm. Annu Rev Cell Dev Biol. 2007;23: 23–43. 17456018
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 23-43
    • Tsai, B.1
  • 51
    • 0014905804 scopus 로고
    • The self-assembly of spherical plant viruses
    • Bancroft JB, The self-assembly of spherical plant viruses. Adv Virus Res. 1970;16: 99–134. 4924992
    • (1970) Adv Virus Res , vol.16 , pp. 99-134
    • Bancroft, J.B.1
  • 52
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy
    • Speir JA, Munshi S, Wang GJ, Baker TS, Johnson JE, Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure. 1995;3: 63–78. 7743132
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Munshi, S.2    Wang, G.J.3    Baker, T.S.4    Johnson, J.E.5
  • 53
    • 33644995225 scopus 로고    scopus 로고
    • The role of subunit hinges and molecular "switches" in the control of viral capsid polymorphism
    • Tang JH, Johnson JM, Dryden KA, Young MJ, Zlotnick A, Johnson JE, The role of subunit hinges and molecular "switches" in the control of viral capsid polymorphism. J Struct Biol. 2006;154: 59–67. 16495083
    • (2006) J Struct Biol , vol.154 , pp. 59-67
    • Tang, J.H.1    Johnson, J.M.2    Dryden, K.A.3    Young, M.J.4    Zlotnick, A.5    Johnson, J.E.6
  • 54
    • 46449089671 scopus 로고    scopus 로고
    • An improved SUMO fusion protein system for effective production of native proteins
    • Lee CD, Sun HC, Hu SM, Chiu CF, Homhuan A, Liang SM, et al. An improved SUMO fusion protein system for effective production of native proteins. Protein Sci. 2008;17: 1241–1248. doi: 10.1110/ps.035188.108 18467498
    • (2008) Protein Sci , vol.17 , pp. 1241-1248
    • Lee, C.D.1    Sun, H.C.2    Hu, S.M.3    Chiu, C.F.4    Homhuan, A.5    Liang, S.M.6
  • 55
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol. 1997;276: 307–326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 25144433340 scopus 로고    scopus 로고
    • Ab initio crystal structure determination of spherical viruses that exhibit a centrosymmetric location in the unit cell
    • Taka J, Naitow H, Yoshimura M, Miyazaki N, Nakagawa A, Tsukihara T, Ab initio crystal structure determination of spherical viruses that exhibit a centrosymmetric location in the unit cell. Acta Crystallogr D Biol Crystallogr. 2005;61: 1099–1106. 16041075
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 1099-1106
    • Taka, J.1    Naitow, H.2    Yoshimura, M.3    Miyazaki, N.4    Nakagawa, A.5    Tsukihara, T.6
  • 58
    • 0001681837 scopus 로고
    • Molecular replacement method at low resolution: optimum strategy and intrinsic limitations as determined by calculations on icosahedral virus models
    • Rayment I, Molecular replacement method at low resolution: optimum strategy and intrinsic limitations as determined by calculations on icosahedral virus models. Acta Crystallogr A. 1983;39: 102–116.
    • (1983) Acta Crystallogr A , vol.39 , pp. 102-116
    • Rayment, I.1
  • 67
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A, Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc. 2008;3: 1171–1179. doi: 10.1038/nprot.2008.91 18600222
    • (2008) Nat Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 70
    • 0032810512 scopus 로고    scopus 로고
    • Establishment and characterization of a continuous cell line (GF-1) derived from grouper, Epinephelus coioides (Hamilton): a cell line susceptible to grouper nervous necrosis virus (GNNV)
    • Chi SC, Hu WW, Lo BJ, Establishment and characterization of a continuous cell line (GF-1) derived from grouper, Epinephelus coioides (Hamilton): a cell line susceptible to grouper nervous necrosis virus (GNNV). J Fish Dis. 1999;22: 173–182.
    • (1999) J Fish Dis , vol.22 , pp. 173-182
    • Chi, S.C.1    Hu, W.W.2    Lo, B.J.3
  • 71
    • 79952339481 scopus 로고    scopus 로고
    • Real-time quantitative pcr assay for monitoring of nervous necrosis virus infection in grouper aquaculture
    • Kuo HC, Wang TY, Chen PP, Chen YM, Chuang HC, Chen TY, Real-time quantitative pcr assay for monitoring of nervous necrosis virus infection in grouper aquaculture. J Clin Microbiol. 2011;49: 1090–1096. doi: 10.1128/JCM.01016-10 21233077
    • (2011) J Clin Microbiol , vol.49 , pp. 1090-1096
    • Kuo, H.C.1    Wang, T.Y.2    Chen, P.P.3    Chen, Y.M.4    Chuang, H.C.5    Chen, T.Y.6
  • 72
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S, MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol. 2011;28: 2731–2739. doi: 10.1093/molbev/msr121 21546353
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.