메뉴 건너뛰기




Volumn 90, Issue 5, 2016, Pages 2455-2472

Deletion of murid herpesvirus 4 ORF63 affects the trafficking of incoming capsids toward the nucleus

Author keywords

[No Author keywords available]

Indexed keywords

INFLAMMASOME; INTERLEUKIN 1BETA CONVERTING ENZYME; VIRAL PROTEIN;

EID: 84961154099     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02942-15     Document Type: Article
Times cited : (11)

References (61)
  • 1
    • 33644638645 scopus 로고    scopus 로고
    • Pathogenesis of gammaherpesvirus infections
    • Ackermann M. 2006. Pathogenesis of gammaherpesvirus infections. Vet Microbiol 113:211-222. http://dx.doi.org/10.1016/j.vetmic.2005.11.008.
    • (2006) Vet Microbiol , vol.113 , pp. 211-222
    • Ackermann, M.1
  • 2
    • 1642334164 scopus 로고    scopus 로고
    • Persistence of the Epstein-Barr virus and the origins of associated lymphomas
    • Thorley-Lawson DA, Gross A. 2004. Persistence of the Epstein-Barr virus and the origins of associated lymphomas. N Engl J Med 350:1328-1337. http://dx.doi.org/10.1056/NEJMra032015.
    • (2004) N Engl J Med , vol.350 , pp. 1328-1337
    • Thorley-Lawson, D.A.1    Gross, A.2
  • 3
    • 0037721575 scopus 로고    scopus 로고
    • Molecular biology and pathogenesis of Kaposi sarcoma-associated herpesvirus
    • Verma SC, Robertson ES. 2003. Molecular biology and pathogenesis of Kaposi sarcoma-associated herpesvirus. FEMS Microbiol Lett 222:155-163. http://dx.doi.org/10.1016/S0378-1097(03)00261-1.
    • (2003) FEMS Microbiol Lett , vol.222 , pp. 155-163
    • Verma, S.C.1    Robertson, E.S.2
  • 5
    • 4344714976 scopus 로고    scopus 로고
    • Oncogenic gamma-herpesviruses: comparison of viral proteins involved in tumorigenesis
    • Damania B. 2004. Oncogenic gamma-herpesviruses: comparison of viral proteins involved in tumorigenesis. Nat Rev Microbiol 2:656-668. http://dx.doi.org/10.1038/nrmicro958.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 656-668
    • Damania, B.1
  • 6
    • 84912524765 scopus 로고    scopus 로고
    • KSHV targeted therapy: an update on inhibitors of viral lytic replication
    • Coen N, Duraffour S, Snoeck R, Andrei G. 2014. KSHV targeted therapy: an update on inhibitors of viral lytic replication. Viruses 6:4731-4759. http://dx.doi.org/10.3390/v6114731.
    • (2014) Viruses , vol.6 , pp. 4731-4759
    • Coen, N.1    Duraffour, S.2    Snoeck, R.3    Andrei, G.4
  • 7
    • 40649085105 scopus 로고    scopus 로고
    • Unique structures in a tumor herpesvirus revealed by cryo-electron tomography and microscopy
    • Dai W, Jia Q, Bortz E, Shah S, Liu J, Atanasov I, Li X, Taylor KA, Sun R, Zhou ZH. 2008. Unique structures in a tumor herpesvirus revealed by cryo-electron tomography and microscopy. J Struct Biol 161:428-438. http://dx.doi.org/10.1016/j.jsb.2007.10.010.
    • (2008) J Struct Biol , vol.161 , pp. 428-438
    • Dai, W.1    Jia, Q.2    Bortz, E.3    Shah, S.4    Liu, J.5    Atanasov, I.6    Li, X.7    Taylor, K.A.8    Sun, R.9    Zhou, Z.H.10
  • 9
    • 35348826721 scopus 로고    scopus 로고
    • Murine gammaherpesvirus 68 ORF52 encodes a tegument protein required for virion morphogenesis in the cytoplasm
    • Bortz E, Wang L, Jia Q, Wu TT, Whitelegge JP, Deng H, Zhou ZH, Sun R. 2007. Murine gammaherpesvirus 68 ORF52 encodes a tegument protein required for virion morphogenesis in the cytoplasm. J Virol 81: 10137-10150. http://dx.doi.org/10.1128/JVI.01233-06.
    • (2007) J Virol , vol.81 , pp. 10137-10150
    • Bortz, E.1    Wang, L.2    Jia, Q.3    Wu, T.T.4    Whitelegge, J.P.5    Deng, H.6    Zhou, Z.H.7    Sun, R.8
  • 10
    • 70349751724 scopus 로고    scopus 로고
    • Open reading frame 33 of a gammaherpesvirus encodes a tegument protein essential for virion morphogenesis and egress
    • Guo H, Wang L, Peng L, Zhou ZH, Deng H. 2009. Open reading frame 33 of a gammaherpesvirus encodes a tegument protein essential for virion morphogenesis and egress. J Virol 83:10582-10595. http://dx.doi.org/10.1128/JVI.00497-09.
    • (2009) J Virol , vol.83 , pp. 10582-10595
    • Guo, H.1    Wang, L.2    Peng, L.3    Zhou, Z.H.4    Deng, H.5
  • 11
    • 16244403634 scopus 로고    scopus 로고
    • Murine gammaherpesvirus 68 open reading frame 45 plays an essential role during the immediate-early phase of viral replication
    • Jia Q, Chernishof V, Bortz E, McHardy I, Wu TT, Liao HI, Sun R. 2005. Murine gammaherpesvirus 68 open reading frame 45 plays an essential role during the immediate-early phase of viral replication. J Virol 79: 5129-5141. http://dx.doi.org/10.1128/JVI.79.8.5129-5141.2005.
    • (2005) J Virol , vol.79 , pp. 5129-5141
    • Jia, Q.1    Chernishof, V.2    Bortz, E.3    McHardy, I.4    Wu, T.T.5    Liao, H.I.6    Sun, R.7
  • 12
    • 84896547685 scopus 로고    scopus 로고
    • Murine gammaherpesvirus-68 ORF38 encodes a tegument protein and is packaged into virions during secondary envelopment
    • Shen S, Guo H, Deng H. 2014. Murine gammaherpesvirus-68 ORF38 encodes a tegument protein and is packaged into virions during secondary envelopment. Protein Cell 5:141-150.
    • (2014) Protein Cell , vol.5 , pp. 141-150
    • Shen, S.1    Guo, H.2    Deng, H.3
  • 13
    • 50649120325 scopus 로고    scopus 로고
    • Multiple functions for ORF75c in murid herpesvirus-4 infection
    • Gaspar M, Gill MB, Losing JB, May JS, Stevenson PG. 2008. Multiple functions for ORF75c in murid herpesvirus-4 infection. PLoS One 3:e2781. http://dx.doi.org/10.1371/journal.pone.0002781.
    • (2008) PLoS One , vol.3
    • Gaspar, M.1    Gill, M.B.2    Losing, J.B.3    May, J.S.4    Stevenson, P.G.5
  • 15
    • 58149393193 scopus 로고    scopus 로고
    • Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1
    • Roberts AP, Abaitua F, O'Hare P, McNab D, Rixon FJ, Pasdeloup D. 2009. Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1. J Virol 83:105-116. http://dx.doi.org/10.1128/JVI.01032-08.
    • (2009) J Virol , vol.83 , pp. 105-116
    • Roberts, A.P.1    Abaitua, F.2    O'Hare, P.3    McNab, D.4    Rixon, F.J.5    Pasdeloup, D.6
  • 16
    • 63149186260 scopus 로고    scopus 로고
    • Translocation of incoming pseudorabies virus capsids to the cell nucleus is delayed in the absence of tegument protein pUL37
    • Krautwald M, Fuchs W, Klupp BG, Mettenleiter TC. 2009. Translocation of incoming pseudorabies virus capsids to the cell nucleus is delayed in the absence of tegument protein pUL37. J Virol 83:3389-3396. http://dx.doi.org/10.1128/JVI.02090-08.
    • (2009) J Virol , vol.83 , pp. 3389-3396
    • Krautwald, M.1    Fuchs, W.2    Klupp, B.G.3    Mettenleiter, T.C.4
  • 17
    • 67849102088 scopus 로고    scopus 로고
    • Phenotypic similarities and differences between UL37-deleted pseudorabies virus and herpes simplex virus type 1
    • Leege T, Granzow H, Fuchs W, Klupp BG, Mettenleiter TC. 2009. Phenotypic similarities and differences between UL37-deleted pseudorabies virus and herpes simplex virus type 1. J Gen Virol 90:1560-1568. http://dx.doi.org/10.1099/vir.0.010322-0.
    • (2009) J Gen Virol , vol.90 , pp. 1560-1568
    • Leege, T.1    Granzow, H.2    Fuchs, W.3    Klupp, B.G.4    Mettenleiter, T.C.5
  • 18
    • 0034849764 scopus 로고    scopus 로고
    • Pseudorabies virus UL37 gene product is involved in secondary envelopment
    • Klupp BG, Granzow H, Mundt E, Mettenleiter TC. 2001. Pseudorabies virus UL37 gene product is involved in secondary envelopment. J Virol 75:8927-8936. http://dx.doi.org/10.1128/JVI.75.19.8927-8936.2001.
    • (2001) J Virol , vol.75 , pp. 8927-8936
    • Klupp, B.G.1    Granzow, H.2    Mundt, E.3    Mettenleiter, T.C.4
  • 19
    • 0034785814 scopus 로고    scopus 로고
    • A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation
    • Desai P, Sexton GL, McCaffery JM, Person S. 2001. A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation. J Virol 75:10259-10271. http://dx.doi.org/10.1128/JVI.75.21.10259-10271.2001.
    • (2001) J Virol , vol.75 , pp. 10259-10271
    • Desai, P.1    Sexton, G.L.2    McCaffery, J.M.3    Person, S.4
  • 20
    • 0019266011 scopus 로고
    • Isolation of five strains of herpesviruses from two species of free living small rodents
    • Blaskovic D, Stancekova M, Svobodova J, Mistrikova J. 1980. Isolation of five strains of herpesviruses from two species of free living small rodents. Acta Virol 24:468.
    • (1980) Acta Virol , vol.24 , pp. 468
    • Blaskovic, D.1    Stancekova, M.2    Svobodova, J.3    Mistrikova, J.4
  • 22
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797. http://dx.doi.org/10.1093/nar/gkh340.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 23
    • 36448960843 scopus 로고    scopus 로고
    • PFRES: protein fold classification by using evolutionary information and predicted secondary structure
    • Chen K, Kurgan L. 2007. PFRES: protein fold classification by using evolutionary information and predicted secondary structure. Bioinformatics 23:2843-2850. http://dx.doi.org/10.1093/bioinformatics/btm475.
    • (2007) Bioinformatics , vol.23 , pp. 2843-2850
    • Chen, K.1    Kurgan, L.2
  • 24
    • 46449128812 scopus 로고    scopus 로고
    • Prediction of protein structural class using novel evolutionary collocation-based sequence representation
    • Chen K, Kurgan LA, Ruan J. 2008. Prediction of protein structural class using novel evolutionary collocation-based sequence representation. J Comput Chem 29:1596-1604. http://dx.doi.org/10.1002/jcc.20918.
    • (2008) J Comput Chem , vol.29 , pp. 1596-1604
    • Chen, K.1    Kurgan, L.A.2    Ruan, J.3
  • 25
    • 35448954064 scopus 로고    scopus 로고
    • Prediction of protein secondary structure content for the twilight zone sequences
    • Homaeian L, Kurgan LA, Ruan J, Cios KJ, Chen K. 2007. Prediction of protein secondary structure content for the twilight zone sequences. Proteins 69:486-498. http://dx.doi.org/10.1002/prot.21527.
    • (2007) Proteins , vol.69 , pp. 486-498
    • Homaeian, L.1    Kurgan, L.A.2    Ruan, J.3    Cios, K.J.4    Chen, K.5
  • 26
    • 0033912858 scopus 로고    scopus 로고
    • Cloning and mutagenesis of the murine gammaherpesvirus 68 genome as an infectious bacterial artificial chromosome
    • Adler H, Messerle M, Wagner M, Koszinowski UH. 2000. Cloning and mutagenesis of the murine gammaherpesvirus 68 genome as an infectious bacterial artificial chromosome. J Virol 74:6964-6974. http://dx.doi.org/10.1128/JVI.74.15.6964-6974.2000.
    • (2000) J Virol , vol.74 , pp. 6964-6974
    • Adler, H.1    Messerle, M.2    Wagner, M.3    Koszinowski, U.H.4
  • 28
    • 37149005032 scopus 로고    scopus 로고
    • Antibody evasion by the N terminus of murid herpesvirus-4 glycoprotein B
    • Gillet L, Stevenson PG. 2007. Antibody evasion by the N terminus of murid herpesvirus-4 glycoprotein B.EMBOJ 26:5131-5142. http://dx.doi.org/10.1038/sj.emboj.7601925.
    • (2007) EMBOJ , vol.26 , pp. 5131-5142
    • Gillet, L.1    Stevenson, P.G.2
  • 29
    • 38349165377 scopus 로고    scopus 로고
    • Isolation and characterisation of a ruminant alphaherpesvirus closely related to bovine herpesvirus 1 in a free-ranging red deer
    • Thiry J, Widen F, Gregoire F, Linden A, Belak S, Thiry E. 2007. Isolation and characterisation of a ruminant alphaherpesvirus closely related to bovine herpesvirus 1 in a free-ranging red deer. BMC Vet Res 3:26. http://dx.doi.org/10.1186/1746-6148-3-26.
    • (2007) BMC Vet Res , vol.3 , pp. 26
    • Thiry, J.1    Widen, F.2    Gregoire, F.3    Linden, A.4    Belak, S.5    Thiry, E.6
  • 31
    • 84862239242 scopus 로고    scopus 로고
    • A post-assembly genome-improvement toolkit (PAGIT) to obtain annotated genomes from contigs
    • Swain MT, Tsai IJ, Assefa SA, Newbold C, Berriman M, Otto TD. 2012. A post-assembly genome-improvement toolkit (PAGIT) to obtain annotated genomes from contigs. Nat Protoc 7:1260-1284. http://dx.doi.org/10.1038/nprot.2012.068.
    • (2012) Nat Protoc , vol.7 , pp. 1260-1284
    • Swain, M.T.1    Tsai, I.J.2    Assefa, S.A.3    Newbold, C.4    Berriman, M.5    Otto, T.D.6
  • 32
    • 84862591603 scopus 로고    scopus 로고
    • Toward almost closed genomes with GapFiller
    • Boetzer M, Pirovano W. 2012. Toward almost closed genomes with GapFiller. Genome Biol 13:R56. http://dx.doi.org/10.1186/gb-2012-13-6-r56.
    • (2012) Genome Biol , vol.13 , pp. R56
    • Boetzer, M.1    Pirovano, W.2
  • 34
    • 33845723594 scopus 로고    scopus 로고
    • Glycoprotein L disruption reveals two functional forms of the murine gammaherpes-virus 68 glycoprotein H
    • Gillet L, May JS, Colaco S, Stevenson PG. 2007. Glycoprotein L disruption reveals two functional forms of the murine gammaherpes-virus 68 glycoprotein H. J Virol 81:280-291. http://dx.doi.org/10.1128/JVI.01616-06.
    • (2007) J Virol , vol.81 , pp. 280-291
    • Gillet, L.1    May, J.S.2    Colaco, S.3    Stevenson, P.G.4
  • 35
    • 78650645593 scopus 로고    scopus 로고
    • The bovine herpesvirus 4 Bo10 gene encodes a nonessential viral envelope protein that regulates viral tropism through both positive and negative effects
    • Machiels B, Lete C, de Fays K, Mast J, Dewals B, Stevenson PG, Vanderplasschen A, Gillet L. 2011. The bovine herpesvirus 4 Bo10 gene encodes a nonessential viral envelope protein that regulates viral tropism through both positive and negative effects. J Virol 85:1011-1024. http://dx.doi.org/10.1128/JVI.01092-10.
    • (2011) J Virol , vol.85 , pp. 1011-1024
    • Machiels, B.1    Lete, C.2    de Fays, K.3    Mast, J.4    Dewals, B.5    Stevenson, P.G.6    Vanderplasschen, A.7    Gillet, L.8
  • 36
    • 24644521162 scopus 로고    scopus 로고
    • Ultrastructural changes of the tracheal epithelium after vaccination of day-old chickens with the La Sota strain of Newcastle disease virus
    • Mast J, Nanbru C, van den Berg T, Meulemans G. 2005. Ultrastructural changes of the tracheal epithelium after vaccination of day-old chickens with the La Sota strain of Newcastle disease virus. Vet Pathol 42:559-565. http://dx.doi.org/10.1354/vp.42-5-559.
    • (2005) Vet Pathol , vol.42 , pp. 559-565
    • Mast, J.1    Nanbru, C.2    van den Berg, T.3    Meulemans, G.4
  • 37
    • 84861114181 scopus 로고    scopus 로고
    • Virion endocytosis is a major target for murid herpesvirus-4 neutralization
    • Glauser DL, Gillet L, Stevenson PG. 2012. Virion endocytosis is a major target for murid herpesvirus-4 neutralization. J Gen Virol 93:1316-1327. http://dx.doi.org/10.1099/vir.0.040790-0.
    • (2012) J Gen Virol , vol.93 , pp. 1316-1327
    • Glauser, D.L.1    Gillet, L.2    Stevenson, P.G.3
  • 38
    • 14744272167 scopus 로고    scopus 로고
    • Glycoprotein M is an essential lytic replication protein of the murine gammaherpesvirus 68
    • May JS, Colaco S, Stevenson PG. 2005. Glycoprotein M is an essential lytic replication protein of the murine gammaherpesvirus 68. J Virol 79: 3459-3467. http://dx.doi.org/10.1128/JVI.79.6.3459-3467.2005.
    • (2005) J Virol , vol.79 , pp. 3459-3467
    • May, J.S.1    Colaco, S.2    Stevenson, P.G.3
  • 39
    • 33751394229 scopus 로고    scopus 로고
    • Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice
    • Gillet L, Gill MB, Colaco S, Smith CM, Stevenson PG. 2006. Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice. J Gen Virol 87:3515-3527. http://dx.doi.org/10.1099/vir.0.82313-0.
    • (2006) J Gen Virol , vol.87 , pp. 3515-3527
    • Gillet, L.1    Gill, M.B.2    Colaco, S.3    Smith, C.M.4    Stevenson, P.G.5
  • 40
    • 84866914719 scopus 로고    scopus 로고
    • Myeloid infection links epithelial and B cell tropisms of murid herpesvirus-4
    • Frederico B, Milho R, May JS, Gillet L, Stevenson PG. 2012. Myeloid infection links epithelial and B cell tropisms of murid herpesvirus-4. PLoS Pathog 8:e1002935. http://dx.doi.org/10.1371/journal.ppat.1002935.
    • (2012) PLoS Pathog , vol.8
    • Frederico, B.1    Milho, R.2    May, J.S.3    Gillet, L.4    Stevenson, P.G.5
  • 41
    • 77950463338 scopus 로고    scopus 로고
    • Pathogenesis of a model gammaherpesvirus in a natural host
    • Hughes DJ, Kipar A, Sample JT, Stewart JP. 2010. Pathogenesis of a model gammaherpesvirus in a natural host. J Virol 84:3949-3961. http://dx.doi.org/10.1128/JVI.02085-09.
    • (2010) J Virol , vol.84 , pp. 3949-3961
    • Hughes, D.J.1    Kipar, A.2    Sample, J.T.3    Stewart, J.P.4
  • 44
    • 84857831938 scopus 로고    scopus 로고
    • Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry
    • Lété C, Machiels B, Stevenson PG, Vanderplasschen A, Gillet L. 2012. Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry. J Virol 86:2653-2664. http://dx.doi.org/10.1128/JVI.06238-11.
    • (2012) J Virol , vol.86 , pp. 2653-2664
    • Lété, C.1    Machiels, B.2    Stevenson, P.G.3    Vanderplasschen, A.4    Gillet, L.5
  • 45
    • 80051721138 scopus 로고    scopus 로고
    • A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization
    • Glauser DL, Kratz AS, Gillet L, Stevenson PG. 2011. A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization. J Gen Virol 92:2020-2033. http://dx.doi.org/10.1099/vir.0.032177-0.
    • (2011) J Gen Virol , vol.92 , pp. 2020-2033
    • Glauser, D.L.1    Kratz, A.S.2    Gillet, L.3    Stevenson, P.G.4
  • 46
    • 45949085102 scopus 로고    scopus 로고
    • Glycoprotein B switches conformation during murid herpesvirus 4 entry
    • Gillet L, Colaco S, Stevenson PG. 2008. Glycoprotein B switches conformation during murid herpesvirus 4 entry. J Gen Virol 89:1352-1363. http://dx.doi.org/10.1099/vir.0.83519-0.
    • (2008) J Gen Virol , vol.89 , pp. 1352-1363
    • Gillet, L.1    Colaco, S.2    Stevenson, P.G.3
  • 47
    • 50949098291 scopus 로고    scopus 로고
    • The murid herpesvirus-4 gL regulates an entry-associated conformation change in gH
    • Gillet L, Colaco S, Stevenson PG. 2008. The murid herpesvirus-4 gL regulates an entry-associated conformation change in gH. PLoS One 3:e2811. http://dx.doi.org/10.1371/journal.pone.0002811.
    • (2008) PLoS One , vol.3
    • Gillet, L.1    Colaco, S.2    Stevenson, P.G.3
  • 48
    • 80052188114 scopus 로고    scopus 로고
    • Coupling viruses to dynein and kinesin-1
    • Dodding MP, Way M. 2011. Coupling viruses to dynein and kinesin-1. EMBO J 30:3527-3539. http://dx.doi.org/10.1038/emboj.2011.283.
    • (2011) EMBO J , vol.30 , pp. 3527-3539
    • Dodding, M.P.1    Way, M.2
  • 49
    • 84899072550 scopus 로고    scopus 로고
    • Crystal structure of the herpesvirus inner tegument protein UL37 supports its essential role in control of viral trafficking
    • Pitts JD, Klabis J, Richards AL, Smith GA, Heldwein EE. 2014. Crystal structure of the herpesvirus inner tegument protein UL37 supports its essential role in control of viral trafficking. J Virol 88:5462-5473. http://dx.doi.org/10.1128/JVI.00163-14.
    • (2014) J Virol , vol.88 , pp. 5462-5473
    • Pitts, J.D.1    Klabis, J.2    Richards, A.L.3    Smith, G.A.4    Heldwein, E.E.5
  • 50
    • 84862955208 scopus 로고    scopus 로고
    • Microtubule-and dynein-dependent nuclear trafficking of rhesus rhadinovirus in rhesus fibroblasts
    • Zhang W, Greene W, Gao SJ. 2012. Microtubule-and dynein-dependent nuclear trafficking of rhesus rhadinovirus in rhesus fibroblasts. J Virol 86:599-604. http://dx.doi.org/10.1128/JVI.06129-11.
    • (2012) J Virol , vol.86 , pp. 599-604
    • Zhang, W.1    Greene, W.2    Gao, S.J.3
  • 51
    • 11144224272 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus
    • Naranatt PP, Krishnan HH, Smith MS, Chandran B. 2005. Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus. J Virol 79:1191-1206. http://dx.doi.org/10.1128/JVI.79.2.1191-1206.2005.
    • (2005) J Virol , vol.79 , pp. 1191-1206
    • Naranatt, P.P.1    Krishnan, H.H.2    Smith, M.S.3    Chandran, B.4
  • 52
    • 84874742572 scopus 로고    scopus 로고
    • Herpesvirus tegument protein pUL37 interacts with dystonin/BPAG1 to promote capsid transport on microtubules during egress
    • Pasdeloup D, McElwee M, Beilstein F, Labetoulle M, Rixon FJ. 2013. Herpesvirus tegument protein pUL37 interacts with dystonin/BPAG1 to promote capsid transport on microtubules during egress. J Virol 87:2857-2867. http://dx.doi.org/10.1128/JVI.02676-12.
    • (2013) J Virol , vol.87 , pp. 2857-2867
    • Pasdeloup, D.1    McElwee, M.2    Beilstein, F.3    Labetoulle, M.4    Rixon, F.J.5
  • 53
    • 84886924682 scopus 로고    scopus 로고
    • Dystonin/BPAG1 promotes plus-end-directed transport of herpes simplex virus 1 capsids on microtubules during entry
    • McElwee M, Beilstein F, Labetoulle M, Rixon FJ, Pasdeloup D. 2013. Dystonin/BPAG1 promotes plus-end-directed transport of herpes simplex virus 1 capsids on microtubules during entry. J Virol 87:11008-11018. http://dx.doi.org/10.1128/JVI.01633-13.
    • (2013) J Virol , vol.87 , pp. 11008-11018
    • McElwee, M.1    Beilstein, F.2    Labetoulle, M.3    Rixon, F.J.4    Pasdeloup, D.5
  • 54
    • 77956283203 scopus 로고    scopus 로고
    • Inner tegument protein pUL37 of herpes simplex virus type 1 is involved in directing capsids to the trans-Golgi network for envelopment
    • Pasdeloup D, Beilstein F, Roberts AP, McElwee M, McNab D, Rixon FJ. 2010. Inner tegument protein pUL37 of herpes simplex virus type 1 is involved in directing capsids to the trans-Golgi network for envelopment. J Gen Virol 91:2145-2151. http://dx.doi.org/10.1099/vir.0.022053-0.
    • (2010) J Gen Virol , vol.91 , pp. 2145-2151
    • Pasdeloup, D.1    Beilstein, F.2    Roberts, A.P.3    McElwee, M.4    McNab, D.5    Rixon, F.J.6
  • 55
    • 0036191216 scopus 로고    scopus 로고
    • Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein
    • Klupp BG, Fuchs W, Granzow H, Nixdorf R, Mettenleiter TC. 2002. Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein. J Virol 76:3065-3071. http://dx.doi.org/10.1128/JVI.76.6.3065-3071.2002.
    • (2002) J Virol , vol.76 , pp. 3065-3071
    • Klupp, B.G.1    Fuchs, W.2    Granzow, H.3    Nixdorf, R.4    Mettenleiter, T.C.5
  • 56
    • 35349025922 scopus 로고    scopus 로고
    • Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1/2) mediate binding of tegument protein pUL37
    • Mijatov B, Cunningham AL, Diefenbach RJ. 2007. Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1/2) mediate binding of tegument protein pUL37. Virology 368:26-31. http://dx.doi.org/10.1016/j.virol.2007.07.005.
    • (2007) Virology , vol.368 , pp. 26-31
    • Mijatov, B.1    Cunningham, A.L.2    Diefenbach, R.J.3
  • 57
    • 22544438727 scopus 로고    scopus 로고
    • Determination of interactions between tegument proteins of herpes simplex virus type 1
    • Vittone V, Diefenbach E, Triffett D, Douglas MW, Cunningham AL, Diefenbach RJ. 2005. Determination of interactions between tegument proteins of herpes simplex virus type 1. J Virol 79:9566-9571. http://dx.doi.org/10.1128/JVI.79.15.9566-9571.2005.
    • (2005) J Virol , vol.79 , pp. 9566-9571
    • Vittone, V.1    Diefenbach, E.2    Triffett, D.3    Douglas, M.W.4    Cunningham, A.L.5    Diefenbach, R.J.6
  • 58
    • 55549112567 scopus 로고    scopus 로고
    • Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures
    • Desai P, Sexton GL, Huang E, Person S. 2008. Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures. J Virol 82:11354-11361. http://dx.doi.org/10.1128/JVI.00956-08.
    • (2008) J Virol , vol.82 , pp. 11354-11361
    • Desai, P.1    Sexton, G.L.2    Huang, E.3    Person, S.4
  • 59
    • 84863777040 scopus 로고    scopus 로고
    • Computational analysis predicts the Kaposi's sarcoma-associated herpesvirus tegument protein ORF63 to be alpha helical
    • Boyle JP, Monie TP. 2012. Computational analysis predicts the Kaposi's sarcoma-associated herpesvirus tegument protein ORF63 to be alpha helical. Proteins 80:2063-2070.
    • (2012) Proteins , vol.80 , pp. 2063-2070
    • Boyle, J.P.1    Monie, T.P.2
  • 60
    • 84861209836 scopus 로고    scopus 로고
    • Multiple interferon stimulated genes synergize with the zinc finger antiviral protein to mediate anti-alphavirus activity
    • Karki S, Li MM, Schoggins JW, Tian S, Rice CM, MacDonald MR. 2012. Multiple interferon stimulated genes synergize with the zinc finger antiviral protein to mediate anti-alphavirus activity. PLoS One 7:e37398. http://dx.doi.org/10.1371/journal.pone.0037398.
    • (2012) PLoS One , vol.7
    • Karki, S.1    Li, M.M.2    Schoggins, J.W.3    Tian, S.4    Rice, C.M.5    MacDonald, M.R.6
  • 61
    • 84925877578 scopus 로고    scopus 로고
    • The A, B, Cs of herpesvirus capsids
    • Tandon R, Mocarski ES, Conway JF. 2015. The A, B, Cs of herpesvirus capsids. Viruses 7:899-914. http://dx.doi.org/10.3390/v7030899.
    • (2015) Viruses , vol.7 , pp. 899-914
    • Tandon, R.1    Mocarski, E.S.2    Conway, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.