메뉴 건너뛰기




Volumn 85, Issue 14, 2011, Pages 7203-7215

Herpes simplex virus 1 pUL34 plays a critical role in cell-to-cell spread of virus in addition to its role in virus replication

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; PROTEIN UL34; TYROSINE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 79960432712     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00262-11     Document Type: Article
Times cited : (38)

References (65)
  • 1
    • 0028229074 scopus 로고
    • An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ
    • Balan, P., et al. 1994. An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ. J. Gen. Virol. 75:1245-1258.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1245-1258
    • Balan, P.1
  • 2
    • 0038467608 scopus 로고    scopus 로고
    • L34 protein
    • L34 protein. J. Virol. 77:7601-7610.
    • (2003) J. Virol. , vol.77 , pp. 7601-7610
    • Bjerke, S.L.1
  • 3
    • 33646018621 scopus 로고    scopus 로고
    • Roles for herpes simplex type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress
    • Bjerke, S. L., and R. Roller. 2006. Roles for herpes simplex type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress. Virology 347(2):261-276.
    • (2006) Virology , vol.347 , Issue.2 , pp. 261-276
    • Bjerke, S.L.1    Roller, R.2
  • 4
    • 0031926378 scopus 로고    scopus 로고
    • The Us9 gene product of pseudorabies virus, an alphaherpesvirus, is a phosphorylated, tail-anchored type II membrane protein
    • Brideau, A. D., B. W. Banfield, and L. W. Enquist. 1998. The Us9 gene product of pseudorabies virus, an alphaherpesvirus, is a phosphorylated, tail-anchored type II membrane protein. J. Virol. 72:4560-4570.
    • (1998) J. Virol. , vol.72 , pp. 4560-4570
    • Brideau, A.D.1    Banfield, B.W.2    Enquist, L.W.3
  • 5
    • 0033989063 scopus 로고    scopus 로고
    • Role of pseudorabies virus Us9, a type II membrane protein, in infection of tissue culture cells and the rat nervous system
    • Brideau, A. D., J. P. Card, and L. W. Enquist. 2000. Role of pseudorabies virus Us9, a type II membrane protein, in infection of tissue culture cells and the rat nervous system. J. Virol. 74:834-845.
    • (2000) J. Virol. , vol.74 , pp. 834-845
    • Brideau, A.D.1    Card, J.P.2    Enquist, L.W.3
  • 6
    • 3242715831 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of a herpesvirus gene in the viral genome context reveals a region essential for virus replication
    • Bubeck, A., et al. 2004. Comprehensive mutational analysis of a herpesvirus gene in the viral genome context reveals a region essential for virus replication. J. Virol. 78:8026-8035.
    • (2004) J. Virol. , vol.78 , pp. 8026-8035
    • Bubeck, A.1
  • 7
    • 0033125379 scopus 로고    scopus 로고
    • Identification and structure of the Marek's disease virus serotype 2 glycoprotein M gene: comparison with glycoprotein M genes of Herpesviridae family
    • Cai, J. S., et al. 1999. Identification and structure of the Marek's disease virus serotype 2 glycoprotein M gene: comparison with glycoprotein M genes of Herpesviridae family. J. Vet. Med. Sci. 61:503-511.
    • (1999) J. Vet. Med. Sci. , vol.61 , pp. 503-511
    • Cai, J.S.1
  • 8
    • 84918724361 scopus 로고
    • Herpesvirus envelopment
    • Darlington, R. W., and L. H. Moss. 1968. Herpesvirus envelopment. J. Virol. 2:49-55.
    • (1968) J. Virol. , vol.2 , pp. 49-55
    • Darlington, R.W.1    Moss, L.H.2
  • 9
    • 0033198645 scopus 로고    scopus 로고
    • Second site mutations in the N terminus of the major capsid protein (VP5) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1
    • Desai, P., and S. Person. 1999. Second site mutations in the N terminus of the major capsid protein (VP5) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1. Virology 261:357-366.
    • (1999) Virology , vol.261 , pp. 357-366
    • Desai, P.1    Person, S.2
  • 10
    • 0028089018 scopus 로고
    • Herpes simplex virus glycoproteins E and I facilitate cell-to-cell spread in vivo and across junctions of cultured cells
    • Dingwell, K. S., et al. 1994. Herpes simplex virus glycoproteins E and I facilitate cell-to-cell spread in vivo and across junctions of cultured cells. J. Virol. 68:834-845.
    • (1994) J. Virol. , vol.68 , pp. 834-845
    • Dingwell, K.S.1
  • 11
    • 0028849767 scopus 로고
    • Glycoproteins E and I facilitate neuron-to-neuron spread of herpes simplex virus
    • Dingwell, K. S., L. C. Doering, and D. C. Johnson. 1995. Glycoproteins E and I facilitate neuron-to-neuron spread of herpes simplex virus. J. Virol. 69: 7087-7098.
    • (1995) J. Virol. , vol.69 , pp. 7087-7098
    • Dingwell, K.S.1    Doering, L.C.2    Johnson, D.C.3
  • 12
    • 0031690758 scopus 로고    scopus 로고
    • The herpes simplex virus gE-gI complex facilitates cell-to-cell spread and binds to components of cell junctions
    • Dingwell, K. S., and D. C. Johnson. 1998. The herpes simplex virus gE-gI complex facilitates cell-to-cell spread and binds to components of cell junctions. J. Virol. 72:8933-8942.
    • (1998) J. Virol. , vol.72 , pp. 8933-8942
    • Dingwell, K.S.1    Johnson, D.C.2
  • 13
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 14
    • 0014286962 scopus 로고
    • Characteristics of herpes simplex virus strains differing in their effect on social behavior of infected cells
    • Ejercito, P. M., E. D. Kieff, and B. Roizman. 1968. Characteristics of herpes simplex virus strains differing in their effect on social behavior of infected cells. J. Gen. Virol. 2:357-364.
    • (1968) J. Gen. Virol. , vol.2 , pp. 357-364
    • Ejercito, P.M.1    Kieff, E.D.2    Roizman, B.3
  • 15
    • 20044384534 scopus 로고    scopus 로고
    • BFRF1 of Epstein-Barr virus is essential for efficient primary viral envelopment and egress
    • Farina, A., et al. 2005. BFRF1 of Epstein-Barr virus is essential for efficient primary viral envelopment and egress. J. Virol. 79:3703-3712.
    • (2005) J. Virol. , vol.79 , pp. 3703-3712
    • Farina, A.1
  • 16
    • 33645221124 scopus 로고    scopus 로고
    • Herpes simplex virus gE/gI must accumulate in the trans-Golgi network at early times and then redistribute to cell junctions to promote cell-cell spread
    • Farnsworth, A., and D. C. Johnson. 2006. Herpes simplex virus gE/gI must accumulate in the trans-Golgi network at early times and then redistribute to cell junctions to promote cell-cell spread. J. Virol. 80:3167-3179.
    • (2006) J. Virol. , vol.80 , pp. 3167-3179
    • Farnsworth, A.1    Johnson, D.C.2
  • 17
    • 0026556674 scopus 로고
    • Construction and properties of a mutant herpes simplex virus type 1 with glycoprotein H coding sequences deleted
    • Forrester, A., et al. 1992. Construction and properties of a mutant herpes simplex virus type 1 with glycoprotein H coding sequences deleted. J. Virol. 66:341-348.
    • (1992) J. Virol. , vol.66 , pp. 341-348
    • Forrester, A.1
  • 18
    • 0036133234 scopus 로고    scopus 로고
    • The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions
    • Fuchs, W., B. G. Klupp, H. Granzow, N. Osterrieder, and T. C. Mettenleiter. 2002. The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions. J. Virol. 76:364-378.
    • (2002) J. Virol. , vol.76 , pp. 364-378
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Osterrieder, N.4    Mettenleiter, T.C.5
  • 19
    • 20044393307 scopus 로고    scopus 로고
    • Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: interactions with BFRF1 and with the nuclear lamina
    • Gonnella, R., et al. 2005. Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: interactions with BFRF1 and with the nuclear lamina. J. Virol. 79:3713-3727.
    • (2005) J. Virol. , vol.79 , pp. 3713-3727
    • Gonnella, R.1
  • 20
    • 33845461933 scopus 로고    scopus 로고
    • Linker insertion mutations in the herpes simplex virus type 1 UL28 gene: effects on UL28 interaction with UL15 and UL33 and identification of a second-site mutation in the UL15 gene that suppresses a lethal UL28 mutation
    • Jacobson, J. G., K. Yang, J. D. Baines, and F. L. Homa. 2006. Linker insertion mutations in the herpes simplex virus type 1 UL28 gene: effects on UL28 interaction with UL15 and UL33 and identification of a second-site mutation in the UL15 gene that suppresses a lethal UL28 mutation. J. Virol. 80:12312-12323.
    • (2006) J. Virol. , vol.80 , pp. 12312-12323
    • Jacobson, J.G.1    Yang, K.2    Baines, J.D.3    Homa, F.L.4
  • 21
    • 0023252169 scopus 로고
    • Identification of a novel herpes simplex virus type 1-induced glycoprotein which complexes with gE and binds immunoglobulin
    • Johnson, D. C., and V. Feenstra. 1987. Identification of a novel herpes simplex virus type 1-induced glycoprotein which complexes with gE and binds immunoglobulin. J. Virol. 61:2208-2216.
    • (1987) J. Virol. , vol.61 , pp. 2208-2216
    • Johnson, D.C.1    Feenstra, V.2
  • 22
    • 0023834392 scopus 로고
    • Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI
    • Johnson, D. C., M. C. Frame, M. W. Ligas, A. M. Cross, and N. D. Stow. 1988. Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI. J. Virol. 62:1347-1354.
    • (1988) J. Virol. , vol.62 , pp. 1347-1354
    • Johnson, D.C.1    Frame, M.C.2    Ligas, M.W.3    Cross, A.M.4    Stow, N.D.5
  • 23
    • 0019918329 scopus 로고
    • Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells
    • Johnson, D. C., and P. G. Spear. 1982. Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells. J. Virol. 43:1102-1112.
    • (1982) J. Virol. , vol.43 , pp. 1102-1112
    • Johnson, D.C.1    Spear, P.G.2
  • 24
    • 34249844954 scopus 로고    scopus 로고
    • Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins
    • Klupp, B. G., et al. 2007. Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins. Proc. Natl. Acad. Sci. U. S. A. 104:7241-7246.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7241-7246
    • Klupp, B.G.1
  • 25
    • 0033775156 scopus 로고    scopus 로고
    • Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product
    • Klupp, B. G., H. Granzow, and T. C. Mettenleiter. 2000. Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product. J. Virol. 74:10063-10073.
    • (2000) J. Virol. , vol.74 , pp. 10063-10073
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 26
    • 1542289787 scopus 로고    scopus 로고
    • The Epstein-Barr virus BFRF1 and BFLF2 proteins interact and coexpression alters their cellular localization
    • Lake, C. M., and L. M. Hutt-Fletcher. 2004. The Epstein-Barr virus BFRF1 and BFLF2 proteins interact and coexpression alters their cellular localization. Virology 320:99-106.
    • (2004) Virology , vol.320 , pp. 99-106
    • Lake, C.M.1    Hutt-Fletcher, L.M.2
  • 27
    • 34648822335 scopus 로고    scopus 로고
    • Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3
    • Leach, N., et al. 2007. Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3. J. Virol. 81:10792-10803.
    • (2007) J. Virol. , vol.81 , pp. 10792-10803
    • Leach, N.1
  • 28
    • 55549097836 scopus 로고    scopus 로고
    • Mapping short DNA sequencing reads and calling variants using mapping quality scores
    • Li, H., J. Ruan, and R. Durbin. 2008. Mapping short DNA sequencing reads and calling variants using mapping quality scores. Genome Res. 18:1851-1858.
    • (2008) Genome Res , vol.18 , pp. 1851-1858
    • Li, H.1    Ruan, J.2    Durbin, R.3
  • 29
    • 14744280502 scopus 로고    scopus 로고
    • Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein
    • Liang, L., and J. D. Baines. 2005. Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein. J. Virol. 79:3797-3806.
    • (2005) J. Virol. , vol.79 , pp. 3797-3806
    • Liang, L.1    Baines, J.D.2
  • 30
    • 0023906081 scopus 로고
    • A herpes simplex virus mutant in which glycoprotein D sequences are replaced by β galactosidase sequences binds to but is unable to penetrate into cells
    • Ligas, M. W., and D. C. Johnson. 1988. A herpes simplex virus mutant in which glycoprotein D sequences are replaced by β galactosidase sequences binds to but is unable to penetrate into cells. J. Virol. 62:1486-1494.
    • (1988) J. Virol. , vol.62 , pp. 1486-1494
    • Ligas, M.W.1    Johnson, D.C.2
  • 31
    • 0023180043 scopus 로고
    • Clustering of genes dispensable for growth in culture in the S component of the HSV-1 genome
    • Longnecker, R., and B. Roizman. 1987. Clustering of genes dispensable for growth in culture in the S component of the HSV-1 genome. Science 236: 573-576.
    • (1987) Science , vol.236 , pp. 573-576
    • Longnecker, R.1    Roizman, B.2
  • 32
    • 33645980333 scopus 로고    scopus 로고
    • Functional domains of murine cytomegalovirus nuclear egress protein M53/p38
    • Lötzerich, M., Z. Ruzsics, and U. H. Koszinowski. 2006. Functional domains of murine cytomegalovirus nuclear egress protein M53/p38. J. Virol. 80:73-84.
    • (2006) J. Virol. , vol.80 , pp. 73-84
    • Lötzerich, M.1    Ruzsics, Z.2    Koszinowski, U.H.3
  • 33
    • 35148896264 scopus 로고    scopus 로고
    • Pseudorabies virus Us9 directs axonal sorting of viral capsids
    • Lyman, M. G., B. Feierbach, D. Curanovic, M. Bisher, and L. W. Enquist. 2007. Pseudorabies virus Us9 directs axonal sorting of viral capsids. J. Virol. 81:11363-11371.
    • (2007) J. Virol. , vol.81 , pp. 11363-11371
    • Lyman, M.G.1    Feierbach, B.2    Curanovic, D.3    Bisher, M.4    Enquist, L.W.5
  • 34
    • 67650465605 scopus 로고    scopus 로고
    • Comparison of the pseudorabies virus Us9 protein with homologs from other veterinary and human alphaherpesviruses
    • Lyman, M. G., C. D. Kemp, M. P. Taylor, and L. W. Enquist. 2009. Comparison of the pseudorabies virus Us9 protein with homologs from other veterinary and human alphaherpesviruses. J. Virol. 83:6978-6986.
    • (2009) J. Virol. , vol.83 , pp. 6978-6986
    • Lyman, M.G.1    Kemp, C.D.2    Taylor, M.P.3    Enquist, L.W.4
  • 35
    • 0034092676 scopus 로고    scopus 로고
    • Allele-specific suppression as a tool to study protein-protein interactions in bacteria
    • Manson, M. 2000. Allele-specific suppression as a tool to study protein-protein interactions in bacteria. Methods 20:18-34.
    • (2000) Methods , vol.20 , pp. 18-34
    • Manson, M.1
  • 36
    • 69249219334 scopus 로고    scopus 로고
    • Anterograde spread of herpes simplex virus type 1 requires glycoprotein E and glycoprotein I but not Us9
    • McGraw, H. M., S. Awasthi, J. A. Wojcechowskyj, and H. M. Friedman. 2009. Anterograde spread of herpes simplex virus type 1 requires glycoprotein E and glycoprotein I but not Us9. J. Virol. 83:8315-8326.
    • (2009) J. Virol. , vol.83 , pp. 8315-8326
    • McGraw, H.M.1    Awasthi, S.2    Wojcechowskyj, J.A.3    Friedman, H.M.4
  • 37
    • 0035138826 scopus 로고    scopus 로고
    • Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions
    • McMillan, T. N., and D. C. Johnson. 2001. Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions. J. Virol. 75:1928-1940.
    • (2001) J. Virol. , vol.75 , pp. 1928-1940
    • McMillan, T.N.1    Johnson, D.C.2
  • 38
    • 34247642597 scopus 로고    scopus 로고
    • Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein
    • Morris, J. B., H. Hofemeister, and P. O'Hare. 2007. Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein. J. Virol. 81:4429-4437.
    • (2007) J. Virol. , vol.81 , pp. 4429-4437
    • Morris, J.B.1    Hofemeister, H.2    O'Hare, P.3
  • 39
    • 34249939914 scopus 로고    scopus 로고
    • Us3 of herpes simplex type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells
    • Mou, F., T. Forest, and J. D. Baines. 2007. Us3 of herpes simplex type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells. J. Virol. 81:6459-6470.
    • (2007) J. Virol. , vol.81 , pp. 6459-6470
    • Mou, F.1    Forest, T.2    Baines, J.D.3
  • 40
    • 65349156839 scopus 로고    scopus 로고
    • Phosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids
    • Mou, F., E. Wills, and J. D. Baines. 2009. Phosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids. J. Virol. 83:5181-5191.
    • (2009) J. Virol. , vol.83 , pp. 5181-5191
    • Mou, F.1    Wills, E.2    Baines, J.D.3
  • 41
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi, W., J. Haas, M. Wagner, G. Krohne, and U. H. Koszinowski. 2002. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 297:854-857.
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 42
    • 78651245790 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 strain KOS carries a defective US9 and a mutated US8A gene
    • Negatsch, A., T. C. Mettenleiter, and W. Fuchs. 2011. Herpes simplex virus type 1 strain KOS carries a defective US9 and a mutated US8A gene. J. Gen. Virol. 92:167-172.
    • (2011) J. Gen. Virol. , vol.92 , pp. 167-172
    • Negatsch, A.1    Mettenleiter, T.C.2    Fuchs, W.3
  • 43
    • 0036389915 scopus 로고    scopus 로고
    • The equine herpesvirus 1 UL34 gene product is involved in an early step in virus egress and can be efficiently replaced by a UL34-GFP fusion protein
    • Neubauer, A., J. Rudolph, C. Brandmuller, F. T. Just, and N. Osterrieder. 2002. The equine herpesvirus 1 UL34 gene product is involved in an early step in virus egress and can be efficiently replaced by a UL34-GFP fusion protein. Virology 300:189-204.
    • (2002) Virology , vol.300 , pp. 189-204
    • Neubauer, A.1    Rudolph, J.2    Brandmuller, C.3    Just, F.T.4    Osterrieder, N.5
  • 44
    • 0014282895 scopus 로고
    • Electron microscopy of herpes simplex virus. II. Sequence of development
    • Nii, S., C. Morgan, and H. M. Rose. 1968. Electron microscopy of herpes simplex virus. II. Sequence of development. J. Virol. 2:517-536.
    • (1968) J. Virol. , vol.2 , pp. 517-536
    • Nii, S.1    Morgan, C.2    Rose, H.M.3
  • 45
    • 33645961583 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B
    • Park, R., and J. Baines. 2006. Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B. J. Virol. 80:494-504.
    • (2006) J. Virol. , vol.80 , pp. 494-504
    • Park, R.1    Baines, J.2
  • 46
    • 77956019599 scopus 로고    scopus 로고
    • Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation
    • Popa, M., et al. 2010. Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation. J. Virol. 84:9035-9046.
    • (2010) J. Virol. , vol.84 , pp. 9035-9046
    • Popa, M.1
  • 47
    • 2442697760 scopus 로고    scopus 로고
    • Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes UL31 and UL34
    • Reynolds, A. E., L. Liang, and J. D. Baines. 2004. Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes UL31 and UL34. J. Virol. 78:5564-5575.
    • (2004) J. Virol. , vol.78 , pp. 5564-5575
    • Reynolds, A.E.1    Liang, L.2    Baines, J.D.3
  • 48
    • 0034892972 scopus 로고    scopus 로고
    • L34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids
    • L34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids. J. Virol. 75:8803-8817.
    • (2001) J. Virol. , vol.75 , pp. 8803-8817
    • Reynolds, A.E.1
  • 49
    • 0036333663 scopus 로고    scopus 로고
    • Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids
    • Reynolds, A. E., E. G. Wills, R. J. Roller, B. J. Ryckman, and J. D. Baines. 2002. Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. J. Virol. 76:8939-8952.
    • (2002) J. Virol. , vol.76 , pp. 8939-8952
    • Reynolds, A.E.1    Wills, E.G.2    Roller, R.J.3    Ryckman, B.J.4    Baines, J.D.5
  • 50
    • 77950466161 scopus 로고    scopus 로고
    • Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids
    • Roller, R. J., S. L. Bjerke, A. C. Haugo, and S. Hanson. 2010. Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids. J. Virol. 84:3921-3934.
    • (2010) J. Virol. , vol.84 , pp. 3921-3934
    • Roller, R.J.1    Bjerke, S.L.2    Haugo, A.C.3    Hanson, S.4
  • 52
    • 0027502727 scopus 로고
    • A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells and its particles lack glycoprotein H
    • Roop, C., L. Hutchinson, and D. C. Johnson. 1993. A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells and its particles lack glycoprotein H. J. Virol. 67:2285-2297.
    • (1993) J. Virol. , vol.67 , pp. 2285-2297
    • Roop, C.1    Hutchinson, L.2    Johnson, D.C.3
  • 53
    • 34249828989 scopus 로고    scopus 로고
    • Random screening for dominant-negative mutants of the cytomegalovirus nuclear egress protein M50
    • Rupp, B., et al. 2007. Random screening for dominant-negative mutants of the cytomegalovirus nuclear egress protein M50. J. Virol. 81:5508-5517.
    • (2007) J. Virol. , vol.81 , pp. 5508-5517
    • Rupp, B.1
  • 54
    • 0346365295 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 primary envelopment: UL34 protein modification and the US3-UL34 catalytic relationship
    • Ryckman, B. J., and R. J. Roller. 2004. Herpes simplex virus type 1 primary envelopment: UL34 protein modification and the US3-UL34 catalytic relationship. J. Virol. 78:399-412.
    • (2004) J. Virol. , vol.78 , pp. 399-412
    • Ryckman, B.J.1    Roller, R.J.2
  • 55
    • 42449094941 scopus 로고    scopus 로고
    • Identification and characterization of the product encoded by ORF69 of Kaposi's sarcoma-associated herpesvirus
    • Santarelli, R., et al. 2008. Identification and characterization of the product encoded by ORF69 of Kaposi's sarcoma-associated herpesvirus. J. Virol. 82:4562-4572.
    • (2008) J. Virol. , vol.82 , pp. 4562-4572
    • Santarelli, R.1
  • 56
    • 33751234823 scopus 로고    scopus 로고
    • Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay
    • Schnee, M., Z. Ruzsics, A. Bubeck, and U. H. Koszinowski. 2006. Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay. J. Virol. 80:11658-11666.
    • (2006) J. Virol. , vol.80 , pp. 11658-11666
    • Schnee, M.1    Ruzsics, Z.2    Bubeck, A.3    Koszinowski, U.H.4
  • 57
    • 0034892692 scopus 로고    scopus 로고
    • Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection
    • Scott, E. S., and P. O'Hare. 2001. Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection. J. Virol. 75:1818-1830.
    • (2001) J. Virol. , vol.75 , pp. 1818-1830
    • Scott, E.S.1    O'Hare, P.2
  • 58
    • 26444466028 scopus 로고    scopus 로고
    • Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection
    • Simpson-Holley, M., R. C. Colgrove, G. Nalepa, J. W. Harper, and D. M. Knipe. 2005. Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection. J. Virol. 79:12840-12851.
    • (2005) J. Virol. , vol.79 , pp. 12840-12851
    • Simpson-Holley, M.1    Colgrove, R.C.2    Nalepa, G.3    Harper, J.W.4    Knipe, D.M.5
  • 59
    • 2442719000 scopus 로고    scopus 로고
    • Herpes simplex virus 1 UL31 and UL34 promote the late maturation of viral replication compartments to the nuclear periphery
    • Simpson-Holley, M., J. Baines, R. Roller, and D. Knipe. 2004. Herpes simplex virus 1 UL31 and UL34 promote the late maturation of viral replication compartments to the nuclear periphery. J. Virol. 78:5591-5600.
    • (2004) J. Virol. , vol.78 , pp. 5591-5600
    • Simpson-Holley, M.1    Baines, J.2    Roller, R.3    Knipe, D.4
  • 60
    • 55249103906 scopus 로고    scopus 로고
    • Herpes simplex virus gE/gI and US9 proteins promote transport of both capsids and virion glycoproteins in neuronal axons
    • Snyder, A., K. Polcicova, and D. C. Johnson. 2008. Herpes simplex virus gE/gI and US9 proteins promote transport of both capsids and virion glycoproteins in neuronal axons. J. Virol. 82:10613-10624.
    • (2008) J. Virol. , vol.82 , pp. 10613-10624
    • Snyder, A.1    Polcicova, K.2    Johnson, D.C.3
  • 61
    • 77951457573 scopus 로고    scopus 로고
    • Sequence variability in clinical and laboratory isolates of herpes simplex virus 1 reveals new mutations
    • Szpara, M. L., L. Parsons, and L. W. Enquist. 2010. Sequence variability in clinical and laboratory isolates of herpes simplex virus 1 reveals new mutations. J. Virol. 84:5303-5313.
    • (2010) J. Virol. , vol.84 , pp. 5303-5313
    • Szpara, M.L.1    Parsons, L.2    Enquist, L.W.3
  • 62
    • 33645053126 scopus 로고    scopus 로고
    • Two-step Red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli
    • Tischer, B. K., J. von Einem, B. Kaufer, and N. Osterrieder. 2006. Two-step Red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli. Biotechniques 40:191-197.
    • (2006) Biotechniques , vol.40 , pp. 191-197
    • Tischer, B.K.1    von Einem, J.2    Kaufer, B.3    Osterrieder, N.4
  • 63
    • 0035921429 scopus 로고    scopus 로고
    • A conserved alpha-herpesvirus protein necessary for axonal localization of viral membrane proteins
    • Tomishima, M. J., and L. W. Enquist. 2001. A conserved alpha-herpesvirus protein necessary for axonal localization of viral membrane proteins. J. Cell Biol. 154:741-752.
    • (2001) J. Cell Biol. , vol.154 , pp. 741-752
    • Tomishima, M.J.1    Enquist, L.W.2
  • 64
    • 0033954180 scopus 로고    scopus 로고
    • The extra-cellular domain of herpes simplex virus gE is sufficient for accumulation at cell junctions but not for cell-to-cell spread
    • Wisner, T., C. Brunetti, K. Dingwell, and D. C. Johnson. 2000. The extra-cellular domain of herpes simplex virus gE is sufficient for accumulation at cell junctions but not for cell-to-cell spread. J. Virol. 74:2278-2287.
    • (2000) J. Virol. , vol.74 , pp. 2278-2287
    • Wisner, T.1    Brunetti, C.2    Dingwell, K.3    Johnson, D.C.4
  • 65
    • 0034989005 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 UL34 protein requires UL31 protein for its relocation to the internal nuclear membrane in transfected cells
    • Yamauchi, Y., et al. 2001. Herpes simplex virus type 2 UL34 protein requires UL31 protein for its relocation to the internal nuclear membrane in transfected cells. J. Gen. Virol. 82:1423-1428.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1423-1428
    • Yamauchi, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.