메뉴 건너뛰기




Volumn 376, Issue 2, 2008, Pages 279-289

The HSV-1 tegument protein pUL46 associates with cellular membranes and viral capsids

Author keywords

Envelopment; HSV 1; Membrane association; pUL46; Tegument; UL11; UL37; VP16; VP22; VP5

Indexed keywords

PROTEIN PUL46; PROTEIN VP22; VIRUS PROTEIN;

EID: 44649168714     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2008.03.018     Document Type: Article
Times cited : (40)

References (65)
  • 1
    • 33947368648 scopus 로고    scopus 로고
    • Electron tomography of nascent herpes simplex virus virions
    • Baines J.D., Hsieh C.E., Wills E., Mannella C., and Marko M. Electron tomography of nascent herpes simplex virus virions. J. Virol. 81 (2007) 2726-2735
    • (2007) J. Virol. , vol.81 , pp. 2726-2735
    • Baines, J.D.1    Hsieh, C.E.2    Wills, E.3    Mannella, C.4    Marko, M.5
  • 2
    • 0037384969 scopus 로고    scopus 로고
    • Membrane association of VP22, a herpes simplex virus type 1 tegument protein
    • Brignati M.J., Loomis J.S., Wills J.W., and Courtney R.J. Membrane association of VP22, a herpes simplex virus type 1 tegument protein. J. Virol. 77 (2003) 4888-4898
    • (2003) J. Virol. , vol.77 , pp. 4888-4898
    • Brignati, M.J.1    Loomis, J.S.2    Wills, J.W.3    Courtney, R.J.4
  • 3
    • 0027095747 scopus 로고
    • Membrane-binding properties of filensin, a cytoskeletal protein of the lens fiber cells
    • Brunkener M., and Georgatos S.D. Membrane-binding properties of filensin, a cytoskeletal protein of the lens fiber cells. J. Cell Sci. 103 (1992) 709-718
    • (1992) J. Cell Sci. , vol.103 , pp. 709-718
    • Brunkener, M.1    Georgatos, S.D.2
  • 4
    • 34147100237 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids
    • Bucks M.A., O'Regan K.J., Murphy M.A., Wills J.W., and Courtney R.J. Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids. Virology 10 (2007) 316-324
    • (2007) Virology , vol.10 , pp. 316-324
    • Bucks, M.A.1    O'Regan, K.J.2    Murphy, M.A.3    Wills, J.W.4    Courtney, R.J.5
  • 5
    • 13644249446 scopus 로고    scopus 로고
    • The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids
    • Chi J.H., Harley C.A., Mukhopadhyay A., and Wilson D.W. The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids. J. Gen. Virol. 86 (2005) 253-261
    • (2005) J. Gen. Virol. , vol.86 , pp. 253-261
    • Chi, J.H.1    Harley, C.A.2    Mukhopadhyay, A.3    Wilson, D.W.4
  • 7
    • 0029015321 scopus 로고
    • PREPs: herpes simplex virus type 1-specific particles produced by infected cells when viral DNA replication is blocked
    • Dargan D.J., Patel A.H., and Subak-Sharpe J.H. PREPs: herpes simplex virus type 1-specific particles produced by infected cells when viral DNA replication is blocked. J. Virol. 69 (1995) 4924-4932
    • (1995) J. Virol. , vol.69 , pp. 4924-4932
    • Dargan, D.J.1    Patel, A.H.2    Subak-Sharpe, J.H.3
  • 8
    • 0027511720 scopus 로고
    • Mutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA
    • Desai P., DeLuca N.A., Glorioso J.C., and Person S. Mutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA. J. Virol. 67 (1993) 1357-1364
    • (1993) J. Virol. , vol.67 , pp. 1357-1364
    • Desai, P.1    DeLuca, N.A.2    Glorioso, J.C.3    Person, S.4
  • 9
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • Elliott G., and O'Hare P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88 (1997) 223-233
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 10
    • 0031901219 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules
    • Elliot G., and O'Hare P. Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules. J. Virol. 72 (1998) 6448-6455
    • (1998) J. Virol. , vol.72 , pp. 6448-6455
    • Elliot, G.1    O'Hare, P.2
  • 11
    • 0028849796 scopus 로고
    • VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells
    • Elliott G., Mouzakitis G., and O'Hare P. VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells. J. Virol. 69 (1995) 7932-7941
    • (1995) J. Virol. , vol.69 , pp. 7932-7941
    • Elliott, G.1    Mouzakitis, G.2    O'Hare, P.3
  • 12
    • 0033032399 scopus 로고    scopus 로고
    • Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22
    • Elliott G., O'Reilly D., and O'Hare P. Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. J. Virol. 73 (1999) 6203-6206
    • (1999) J. Virol. , vol.73 , pp. 6203-6206
    • Elliott, G.1    O'Reilly, D.2    O'Hare, P.3
  • 13
    • 0032247683 scopus 로고    scopus 로고
    • Infection and spread of alphaherpesviruses in the nervous system
    • Enquist L.W., Husak P.J., Banfield B.W., and Smith G.A. Infection and spread of alphaherpesviruses in the nervous system. Adv. Virus Res. 51 (1998) 237-347
    • (1998) Adv. Virus Res. , vol.51 , pp. 237-347
    • Enquist, L.W.1    Husak, P.J.2    Banfield, B.W.3    Smith, G.A.4
  • 14
    • 33845775712 scopus 로고    scopus 로고
    • Cytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gD
    • Farnsworth A., Wisner T.W., and Johnson D.C. Cytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gD. J. Virol. 81 (2007) 319-331
    • (2007) J. Virol. , vol.81 , pp. 319-331
    • Farnsworth, A.1    Wisner, T.W.2    Johnson, D.C.3
  • 15
    • 0036316146 scopus 로고    scopus 로고
    • Physical interaction between envelope glycoproteins E and M of pseudorabies virus and the major tegument protein UL49
    • Fuchs W., Klupp B.G., Granzow H., Hengartner C., Brack A., Mundt A., Enquist L.W., and Mettenleiter T.C. Physical interaction between envelope glycoproteins E and M of pseudorabies virus and the major tegument protein UL49. J. Virol. 76 (2002) 8208-8217
    • (2002) J. Virol. , vol.76 , pp. 8208-8217
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Hengartner, C.4    Brack, A.5    Mundt, A.6    Enquist, L.W.7    Mettenleiter, T.C.8
  • 16
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., and Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93 (1982) 97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 17
    • 0028106296 scopus 로고
    • Intracellular transport of newly synthesized varicella-zoster virus: final envelopment in the trans-Golgi network
    • Gershon A.A., Sherman D.L., Zhu Z., Gabel C.A., Ambron R.T., and Gershon M.D. Intracellular transport of newly synthesized varicella-zoster virus: final envelopment in the trans-Golgi network. J. Virol. 68 (1994) 6372-6390
    • (1994) J. Virol. , vol.68 , pp. 6372-6390
    • Gershon, A.A.1    Sherman, D.L.2    Zhu, Z.3    Gabel, C.A.4    Ambron, R.T.5    Gershon, M.D.6
  • 18
    • 0031048830 scopus 로고    scopus 로고
    • Ultrastructural analysis of the replication cycle of pseudorabies virus in cell culture: a reassessment
    • Granzow H., Weiland F., Jons A., Klupp B.G., Karger A., and Mettenleiter T.C. Ultrastructural analysis of the replication cycle of pseudorabies virus in cell culture: a reassessment. J. Virol. 71 (1997) 2072-2082
    • (1997) J. Virol. , vol.71 , pp. 2072-2082
    • Granzow, H.1    Weiland, F.2    Jons, A.3    Klupp, B.G.4    Karger, A.5    Mettenleiter, T.C.6
  • 20
    • 13944272582 scopus 로고    scopus 로고
    • Entry of pseudorabies virus: an immunogold-labeling study
    • Granzow H., Klupp B.G., and Mettenleiter T.C. Entry of pseudorabies virus: an immunogold-labeling study. J. Virol. 79 (2005) 3200-3205
    • (2005) J. Virol. , vol.79 , pp. 3200-3205
    • Granzow, H.1    Klupp, B.G.2    Mettenleiter, T.C.3
  • 21
    • 0346367068 scopus 로고    scopus 로고
    • The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo
    • Gross S.T., Harley C.A., and Wilson D.W. The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo. Virology 317 (2003) 1-12
    • (2003) Virology , vol.317 , pp. 1-12
    • Gross, S.T.1    Harley, C.A.2    Wilson, D.W.3
  • 22
    • 0035154361 scopus 로고    scopus 로고
    • Characterization of herpes simplex virus-containing organelles by subcellular fractionation: role for organelle acidification in assembly of infectious particles
    • Harley C.A., Dasgupta A., and Wilson D.W. Characterization of herpes simplex virus-containing organelles by subcellular fractionation: role for organelle acidification in assembly of infectious particles. J. Virol. 75 (2001) 1236-1251
    • (2001) J. Virol. , vol.75 , pp. 1236-1251
    • Harley, C.A.1    Dasgupta, A.2    Wilson, D.W.3
  • 23
    • 0016264832 scopus 로고
    • Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains
    • Heine J.W., Honess R.W., Cassai E., and Roizman B. Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J. Virol. 14 (1974) 640-651
    • (1974) J. Virol. , vol.14 , pp. 640-651
    • Heine, J.W.1    Honess, R.W.2    Cassai, E.3    Roizman, B.4
  • 24
    • 0035031534 scopus 로고    scopus 로고
    • Ebola virus VP40-induced particle formation and association with the lipid bilayer
    • Jasenosky L.D., Neumann G., Lukashevic I., and Kawaoka Y. Ebola virus VP40-induced particle formation and association with the lipid bilayer. J. Virol. 75 (2001) 5205-5214
    • (2001) J. Virol. , vol.75 , pp. 5205-5214
    • Jasenosky, L.D.1    Neumann, G.2    Lukashevic, I.3    Kawaoka, Y.4
  • 25
    • 18144387577 scopus 로고    scopus 로고
    • Structural basis for the physiological temperature dependence of the association of VP16 with the cytoplasmic tail of herpes simplex virus glycoprotein H
    • Kamen D.E., Gross S.T., Girvin M.E., and Wilson D.W. Structural basis for the physiological temperature dependence of the association of VP16 with the cytoplasmic tail of herpes simplex virus glycoprotein H. J. Virol. 79 (2005) 6134-6141
    • (2005) J. Virol. , vol.79 , pp. 6134-6141
    • Kamen, D.E.1    Gross, S.T.2    Girvin, M.E.3    Wilson, D.W.4
  • 26
    • 0033734819 scopus 로고    scopus 로고
    • Synthesis, subcellular localization and VP16 interaction of the herpes simplex virus type 2 UL46 gene product
    • Kato K., Daikoku T., Goshima F., Kume H., Yamaki K., and Nishiyama Y. Synthesis, subcellular localization and VP16 interaction of the herpes simplex virus type 2 UL46 gene product. Arch. Virol. 145 (2000) 2149-2162
    • (2000) Arch. Virol. , vol.145 , pp. 2149-2162
    • Kato, K.1    Daikoku, T.2    Goshima, F.3    Kume, H.4    Yamaki, K.5    Nishiyama, Y.6
  • 27
    • 0019119354 scopus 로고
    • Herpes simplex virus phosphoproteins. II. Characterization of the virion protein kinase and of the polypeptides phosphorylated in the virion
    • Lemaster S., and Roizman B. Herpes simplex virus phosphoproteins. II. Characterization of the virion protein kinase and of the polypeptides phosphorylated in the virion. J. Virol. 35 (1980) 798-811
    • (1980) J. Virol. , vol.35 , pp. 798-811
    • Lemaster, S.1    Roizman, B.2
  • 28
    • 0035194288 scopus 로고    scopus 로고
    • Intracellular trafficking of the UL11 tegument protein of herpes simplex virus type 1
    • Loomis J.S., Bowzard J.B., Courtney R.J., and Wills J.W. Intracellular trafficking of the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 75 (2001) 12209-12219
    • (2001) J. Virol. , vol.75 , pp. 12209-12219
    • Loomis, J.S.1    Bowzard, J.B.2    Courtney, R.J.3    Wills, J.W.4
  • 29
    • 0142092454 scopus 로고    scopus 로고
    • Binding partners for the UL11 tegument protein of herpes simplex virus type 1
    • Loomis J.S., Courtney R.J., and Wills J.W. Binding partners for the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 77 (2003) 11417-11424
    • (2003) J. Virol. , vol.77 , pp. 11417-11424
    • Loomis, J.S.1    Courtney, R.J.2    Wills, J.W.3
  • 30
    • 33750353962 scopus 로고    scopus 로고
    • Packaging determinants in the UL11 tegument protein of herpes simplex virus type 1
    • Loomis J.S., Courtney R.J., and Wills J.W. Packaging determinants in the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 80 (2006) 10534-10541
    • (2006) J. Virol. , vol.80 , pp. 10534-10541
    • Loomis, J.S.1    Courtney, R.J.2    Wills, J.W.3
  • 31
    • 0026046947 scopus 로고
    • Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell
    • Merdes A., Brunkener M., Horstmann H., and Georgatos S.D. Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell. J. Cell Biol. 115 (1991) 397-410
    • (1991) J. Cell Biol. , vol.115 , pp. 397-410
    • Merdes, A.1    Brunkener, M.2    Horstmann, H.3    Georgatos, S.D.4
  • 32
    • 0033631564 scopus 로고    scopus 로고
    • Aujeszky's disease (pseudorabies) virus: the virus and molecular pathogenesis-state of the art, June 1999
    • Mettenleiter T.C. Aujeszky's disease (pseudorabies) virus: the virus and molecular pathogenesis-state of the art, June 1999. Vet. Res. 31 (2000) 99-115
    • (2000) Vet. Res. , vol.31 , pp. 99-115
    • Mettenleiter, T.C.1
  • 33
    • 0036148284 scopus 로고    scopus 로고
    • Herpesvirus assembly and egress
    • Mettenleiter T.C. Herpesvirus assembly and egress. J. Virol. 76 (2002) 1537-1547
    • (2002) J. Virol. , vol.76 , pp. 1537-1547
    • Mettenleiter, T.C.1
  • 34
    • 9644268172 scopus 로고    scopus 로고
    • Budding events in herpesvirus morphogenesis
    • Mettenleiter T.C. Budding events in herpesvirus morphogenesis. Virus Res. 106 (2004) 167-180
    • (2004) Virus Res. , vol.106 , pp. 167-180
    • Mettenleiter, T.C.1
  • 35
    • 0031816798 scopus 로고    scopus 로고
    • Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument
    • Morrison E.E., Wang Y.F., and Meredith D.M. Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. J. Virol. 72 (1998) 7108-7114
    • (1998) J. Virol. , vol.72 , pp. 7108-7114
    • Morrison, E.E.1    Wang, Y.F.2    Meredith, D.M.3
  • 36
    • 0033919401 scopus 로고    scopus 로고
    • Evidence that herpes simplex virus VP16 is required for viral egress downstream of the initial envelopment event
    • Mossman K.L., Sherburne R., Lavery C., Duncan J., and Smiley J.R. Evidence that herpes simplex virus VP16 is required for viral egress downstream of the initial envelopment event. J. Virol. 74 (2000) 6287-6299
    • (2000) J. Virol. , vol.74 , pp. 6287-6299
    • Mossman, K.L.1    Sherburne, R.2    Lavery, C.3    Duncan, J.4    Smiley, J.R.5
  • 37
    • 33749476250 scopus 로고    scopus 로고
    • The amino terminus of the herpes simplex virus 1 protein vhs mediates membrane association and tegument incorporation
    • Mukhopadhyay A., Lee G.E., and Wilson D.W. The amino terminus of the herpes simplex virus 1 protein vhs mediates membrane association and tegument incorporation. J. Virol. 80 (2006) 10117-10127
    • (2006) J. Virol. , vol.80 , pp. 10117-10127
    • Mukhopadhyay, A.1    Lee, G.E.2    Wilson, D.W.3
  • 39
    • 33144465751 scopus 로고    scopus 로고
    • Herpes simplex virus tegument protein VP16 is a component of primary enveloped virions
    • Naldinho-Souto R., Browne H., and Minson T. Herpes simplex virus tegument protein VP16 is a component of primary enveloped virions. J. Virol. 80 (2006) 2582-2584
    • (2006) J. Virol. , vol.80 , pp. 2582-2584
    • Naldinho-Souto, R.1    Browne, H.2    Minson, T.3
  • 40
    • 0031987325 scopus 로고    scopus 로고
    • UL13 protein kinase of herpes simplex virus 1 complexes with glycoprotein E and mediates the phosphorylation of the viral Fc receptor: glycoproteins E and I
    • Ng T.I., Ogle W.O., and Roizman B. UL13 protein kinase of herpes simplex virus 1 complexes with glycoprotein E and mediates the phosphorylation of the viral Fc receptor: glycoproteins E and I. Virology 241 (1998) 37-48
    • (1998) Virology , vol.241 , pp. 37-48
    • Ng, T.I.1    Ogle, W.O.2    Roizman, B.3
  • 41
    • 4444331960 scopus 로고    scopus 로고
    • Formation of aggresome-like structures in herpes simplex virus type 2-infected cells and a potential role in virus assembly
    • Nozawa N., Yamauchi Y., Ohtsuka K., Kawaguchi Y., and Nishiyama Y. Formation of aggresome-like structures in herpes simplex virus type 2-infected cells and a potential role in virus assembly. Exp. Cell Res. 299 (2004) 486-497
    • (2004) Exp. Cell Res. , vol.299 , pp. 486-497
    • Nozawa, N.1    Yamauchi, Y.2    Ohtsuka, K.3    Kawaguchi, Y.4    Nishiyama, Y.5
  • 42
    • 33845985558 scopus 로고    scopus 로고
    • A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE)
    • O'Regan K.J., Bucks M.A., Murphy M.A., Wills J.W., and Courtney R.J. A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE). Virology 358 (2006) 192-200
    • (2006) Virology , vol.358 , pp. 192-200
    • O'Regan, K.J.1    Bucks, M.A.2    Murphy, M.A.3    Wills, J.W.4    Courtney, R.J.5
  • 43
    • 0031818787 scopus 로고    scopus 로고
    • Study of subcellular localization of membrane-bound choline acetyltransferase in Drosophila central nervous system and its association with membranes
    • Pahud G., Salem G., van de Goor J., Medilanski J., Pellegrinelli N., and Eder-Colli L. Study of subcellular localization of membrane-bound choline acetyltransferase in Drosophila central nervous system and its association with membranes. Eur. J. Neurosci. 10 (1998) 1644-1653
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1644-1653
    • Pahud, G.1    Salem, G.2    van de Goor, J.3    Medilanski, J.4    Pellegrinelli, N.5    Eder-Colli, L.6
  • 44
    • 0032029782 scopus 로고    scopus 로고
    • Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C)
    • Person S., and Desai P. Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C). Virology 242 (1998) 193-203
    • (1998) Virology , vol.242 , pp. 193-203
    • Person, S.1    Desai, P.2
  • 45
    • 33846505946 scopus 로고    scopus 로고
    • Packaging of the virion host shutoff (Vhs) protein of herpes simplex virus: two forms of the vhs polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virions
    • Read G.S., and Patterson M. Packaging of the virion host shutoff (Vhs) protein of herpes simplex virus: two forms of the vhs polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virions. J. Virol. 81 (2007) 1148-1161
    • (2007) J. Virol. , vol.81 , pp. 1148-1161
    • Read, G.S.1    Patterson, M.2
  • 46
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott-Raven, Philadelphia
    • Roizman B., and Sears A.E. Herpes simplex viruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology (2001), Lippincott-Raven, Philadelphia 2399-2459
    • (2001) Fields Virology , pp. 2399-2459
    • Roizman, B.1    Sears, A.E.2
  • 47
    • 0033989064 scopus 로고    scopus 로고
    • Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: characterization of a potential site of virus assembly
    • Sanchez V., Greis K.D., Sztul E., and Britt W.J. Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: characterization of a potential site of virus assembly. J. Virol. 74 (2000) 975-986
    • (2000) J. Virol. , vol.74 , pp. 975-986
    • Sanchez, V.1    Greis, K.D.2    Sztul, E.3    Britt, W.J.4
  • 48
    • 0028855672 scopus 로고
    • The UL37 protein of herpes simplex virus type 1 is associated with the tegument of purified virions
    • Schmitz J.B., Albright A.G., Kinchington P.R., and Jenkins F.J. The UL37 protein of herpes simplex virus type 1 is associated with the tegument of purified virions. Virology 206 (1995) 1055-1065
    • (1995) Virology , vol.206 , pp. 1055-1065
    • Schmitz, J.B.1    Albright, A.G.2    Kinchington, P.R.3    Jenkins, F.J.4
  • 49
    • 0035024157 scopus 로고    scopus 로고
    • Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment-> deenvelopment-> reenvelopment pathway
    • Skepper J.N., Whiteley A., Browne H., and Minson A. Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment-> deenvelopment-> reenvelopment pathway. J. Virol. 75 (2001) 5697-5702
    • (2001) J. Virol. , vol.75 , pp. 5697-5702
    • Skepper, J.N.1    Whiteley, A.2    Browne, H.3    Minson, A.4
  • 50
    • 0000337275 scopus 로고
    • Relationship between the envelope and the infectivity of herpes simplex virus
    • Smith K.O. Relationship between the envelope and the infectivity of herpes simplex virus. Proc. Soc. Exp. Biol. Med. 115 (1964) 814-816
    • (1964) Proc. Soc. Exp. Biol. Med. , vol.115 , pp. 814-816
    • Smith, K.O.1
  • 51
    • 0026100629 scopus 로고
    • Identification and characterization of a novel non-infectious herpes simplex virus-related particle
    • Szilagyi J.F., and Cunningham C. Identification and characterization of a novel non-infectious herpes simplex virus-related particle. J. Gen. Virol. 72 (1991) 661-668
    • (1991) J. Gen. Virol. , vol.72 , pp. 661-668
    • Szilagyi, J.F.1    Cunningham, C.2
  • 52
    • 0028269719 scopus 로고
    • The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei
    • van Genderen I.L., Brandimarti R., Torrisi M.R., Campadelli G., and van Meer G. The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei. Virology 200 (1994) 831-836
    • (1994) Virology , vol.200 , pp. 831-836
    • van Genderen, I.L.1    Brandimarti, R.2    Torrisi, M.R.3    Campadelli, G.4    van Meer, G.5
  • 54
    • 33644759363 scopus 로고    scopus 로고
    • The alpha-TIF (VP16) homologue (ETIF) of equine herpesvirus 1 is essential for secondary envelopment and virus egress
    • von Einem J., Schumacher D., O'Callaghan D.J., and Osterrieder N. The alpha-TIF (VP16) homologue (ETIF) of equine herpesvirus 1 is essential for secondary envelopment and virus egress. J. Virol. 80 (2006) 2609-2620
    • (2006) J. Virol. , vol.80 , pp. 2609-2620
    • von Einem, J.1    Schumacher, D.2    O'Callaghan, D.J.3    Osterrieder, N.4
  • 56
    • 0026083301 scopus 로고
    • Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress
    • Whealy M.E., Card J.P., Meade R.P., Robbins A.K., and Enquist L.W. Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress. J. Virol. 65 (1991) 1066-1081
    • (1991) J. Virol. , vol.65 , pp. 1066-1081
    • Whealy, M.E.1    Card, J.P.2    Meade, R.P.3    Robbins, A.K.4    Enquist, L.W.5
  • 57
    • 0032829388 scopus 로고    scopus 로고
    • Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network
    • Whiteley A., Bruun B., Minson T., and Browne H. Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network. J. Virol. 73 (1999) 9515-9520
    • (1999) J. Virol. , vol.73 , pp. 9515-9520
    • Whiteley, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 58
    • 0036237175 scopus 로고    scopus 로고
    • Rapid directional translocations in virus replication
    • Willard M. Rapid directional translocations in virus replication. J. Virol. 76 (2002) 5220-5232
    • (2002) J. Virol. , vol.76 , pp. 5220-5232
    • Willard, M.1
  • 59
    • 32944467134 scopus 로고    scopus 로고
    • The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro
    • Wolfstein A., Nagel C.H., Radtke K., Dohner K., Allan V.J., and Sodeik B. The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro. Traffic 7 (2006) 227-237
    • (2006) Traffic , vol.7 , pp. 227-237
    • Wolfstein, A.1    Nagel, C.H.2    Radtke, K.3    Dohner, K.4    Allan, V.J.5    Sodeik, B.6
  • 60
    • 0026552585 scopus 로고
    • Association of ICP0 but not ICP27 with purified virions of herpes simplex virus type 1
    • Yao F., and Courtney R.J. Association of ICP0 but not ICP27 with purified virions of herpes simplex virus type 1. J. Virol. 66 (1992) 2709-2716
    • (1992) J. Virol. , vol.66 , pp. 2709-2716
    • Yao, F.1    Courtney, R.J.2
  • 61
    • 0027476811 scopus 로고
    • Herpes simplex virus type 1 UL46 and UL47 deletion mutants lack VP11 and VP12 or VP13 and VP14, respectively, and exhibit altered viral thymidine kinase expression
    • Zhang Y., and McKnight J.L. Herpes simplex virus type 1 UL46 and UL47 deletion mutants lack VP11 and VP12 or VP13 and VP14, respectively, and exhibit altered viral thymidine kinase expression. J. Virol. 67 (1993) 1482-1492
    • (1993) J. Virol. , vol.67 , pp. 1482-1492
    • Zhang, Y.1    McKnight, J.L.2
  • 62
    • 0025170765 scopus 로고
    • The protein kinase encoded in the short unique region of pseudorabies virus: description of the gene and identification of its product in virions and in infected cells
    • Zhang G., Stevens R., and Leader D.P. The protein kinase encoded in the short unique region of pseudorabies virus: description of the gene and identification of its product in virions and in infected cells. J. Gen. Virol. 71 (1990) 1757-1765
    • (1990) J. Gen. Virol. , vol.71 , pp. 1757-1765
    • Zhang, G.1    Stevens, R.2    Leader, D.P.3
  • 63
    • 0026025699 scopus 로고
    • Role of herpes simplex virus type 1 UL46 and UL47 in alpha TIF-mediated transcriptional induction: characterization of three viral deletion mutants
    • Zhang Y., Sirko D.A., and McKnight J.L. Role of herpes simplex virus type 1 UL46 and UL47 in alpha TIF-mediated transcriptional induction: characterization of three viral deletion mutants. J. Virol. 65 (1991) 829-841
    • (1991) J. Virol. , vol.65 , pp. 829-841
    • Zhang, Y.1    Sirko, D.A.2    McKnight, J.L.3
  • 64
    • 0027948545 scopus 로고
    • Chemical cross-linking of virion envelope and tegument proteins of herpes simplex virus type 1
    • Zhu Q., and Courtney R.J. Chemical cross-linking of virion envelope and tegument proteins of herpes simplex virus type 1. Virology 204 (1994) 590-599
    • (1994) Virology , vol.204 , pp. 590-599
    • Zhu, Q.1    Courtney, R.J.2
  • 65
    • 0028971193 scopus 로고
    • Envelopment of varicella-zoster virus: targeting of viral glycoproteins to the trans-Golgi network
    • Zhu Z., Gershon M.D., Hao Y., Ambron R.T., Gabel C.A., and Gershon A.A. Envelopment of varicella-zoster virus: targeting of viral glycoproteins to the trans-Golgi network. J. Virol. 69 (1995) 7951-7959
    • (1995) J. Virol. , vol.69 , pp. 7951-7959
    • Zhu, Z.1    Gershon, M.D.2    Hao, Y.3    Ambron, R.T.4    Gabel, C.A.5    Gershon, A.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.