메뉴 건너뛰기




Volumn 13, Issue 11, 2012, Pages 1443-1449

Herpesviruses Exploit Several Host Compartments for Envelopment

Author keywords

Assembly compartment; CMV; Cytomegalovirus; Egress; Endosomes; ESCRT; Herpesvirus; HSV; Multivesicular bodies; PRV; TGN; VZV

Indexed keywords

CYTOMEGALOVIRUS; HERPES VIRUS; HERPES VIRUS INFECTION; HOST; INTRACELLULAR SPACE; MULTIVESICULAR BODY; NONHUMAN; PRIORITY JOURNAL; REVIEW; VIRION; VIRUS ASSEMBLY; VIRUS CELL INTERACTION; VIRUS ENVELOPE;

EID: 84867232564     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2012.01399.x     Document Type: Review
Times cited : (58)

References (88)
  • 1
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari J, Helenius A. Endosome maturation. EMBO J 2011;30:3481-3500.
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 3
    • 0038339673 scopus 로고    scopus 로고
    • pH of TGN and recycling endosomes of H+/K+-ATPase-transfected HEK-293 cells: implications for pH regulation in the secretory pathway
    • Machen TE, Leigh MJ, Taylor C, Kimura T, Asano S, Moore HP. pH of TGN and recycling endosomes of H+/K+-ATPase-transfected HEK-293 cells: implications for pH regulation in the secretory pathway. Am J Physiol Cell Physiol 2003;285:C205-C214.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Machen, T.E.1    Leigh, M.J.2    Taylor, C.3    Kimura, T.4    Asano, S.5    Moore, H.P.6
  • 4
    • 0031941594 scopus 로고    scopus 로고
    • Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface
    • Demaurex N, Furuya W, D'Souza S, Bonifacino JS, Grinstein S. Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface. J Biol Chem 1998;273:2044-2051.
    • (1998) J Biol Chem , vol.273 , pp. 2044-2051
    • Demaurex, N.1    Furuya, W.2    D'Souza, S.3    Bonifacino, J.S.4    Grinstein, S.5
  • 5
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R, Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 1985;54:631-664.
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 6
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 2009;10:513-525.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 7
    • 79960618381 scopus 로고    scopus 로고
    • Balancing ER dynamics: shaping, bending, severing, and mending membranes
    • Pendin D, McNew JA, Daga A. Balancing ER dynamics: shaping, bending, severing, and mending membranes. Curr Opin Cell Biol 2011;23:435-442.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 435-442
    • Pendin, D.1    McNew, J.A.2    Daga, A.3
  • 8
    • 70350230237 scopus 로고    scopus 로고
    • Membrane traffic within the Golgi apparatus
    • Glick BS, Nakano A. Membrane traffic within the Golgi apparatus. Annu Rev Cell Dev Biol 2009;25:113-132.
    • (2009) Annu Rev Cell Dev Biol , vol.25 , pp. 113-132
    • Glick, B.S.1    Nakano, A.2
  • 9
    • 84857359495 scopus 로고    scopus 로고
    • The intracellular trafficking pathway of transferrin
    • Mayle KM, Le AM, Kamei DT. The intracellular trafficking pathway of transferrin. Biochim Biophys Acta 2012;1820:264-281.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 264-281
    • Mayle, K.M.1    Le, A.M.2    Kamei, D.T.3
  • 10
    • 0021738861 scopus 로고
    • Endosomes and Golgi vesicles in adsorptive and fluid phase endocytosis
    • Gonatas NK, Stieber A, Hickey WF, Herbert SH, Gonatas JO. Endosomes and Golgi vesicles in adsorptive and fluid phase endocytosis. J Cell Biol 1984;99(4 Pt 1):1379-1390.
    • (1984) J Cell Biol , vol.99 , Issue.4 PART 1 , pp. 1379-1390
    • Gonatas, N.K.1    Stieber, A.2    Hickey, W.F.3    Herbert, S.H.4    Gonatas, J.O.5
  • 11
    • 72849149008 scopus 로고    scopus 로고
    • Meeting of conventional and unconventional pathways at the TGN
    • Rémillard-Labrosse G, Lippé R. Meeting of conventional and unconventional pathways at the TGN. Commun Integr Biol 2009;2:434-6.
    • (2009) Commun Integr Biol , vol.2 , pp. 434-436
    • Rémillard-Labrosse, G.1    Lippé, R.2
  • 12
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino JS, Rojas R. Retrograde transport from endosomes to the trans-Golgi network. Nat Rev Mol Cell Biol 2006;7:568-579.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 13
    • 70450223884 scopus 로고    scopus 로고
    • Multiple routes of protein transport from endosomes to the trans Golgi network
    • Pfeffer SR. Multiple routes of protein transport from endosomes to the trans Golgi network. FEBS Lett 2009;583:3811-3816.
    • (2009) FEBS Lett , vol.583 , pp. 3811-3816
    • Pfeffer, S.R.1
  • 14
    • 45849124923 scopus 로고    scopus 로고
    • Endosomal sorting and signalling: an emerging role for sorting nexins
    • Cullen PJ. Endosomal sorting and signalling: an emerging role for sorting nexins. Nat Rev Mol Cell Biol 2008;9:574-582.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 574-582
    • Cullen, P.J.1
  • 15
    • 79960184162 scopus 로고    scopus 로고
    • Recent advances in retromer biology
    • McGough IJ, Cullen PJ. Recent advances in retromer biology. Traffic 2011;12:963-971.
    • (2011) Traffic , vol.12 , pp. 963-971
    • McGough, I.J.1    Cullen, P.J.2
  • 16
    • 33644822448 scopus 로고    scopus 로고
    • Viral interactions with the cytoskeleton: a hitchhiker's guide to the cell
    • Radtke K, Döhner K, Sodeik B. Viral interactions with the cytoskeleton: a hitchhiker's guide to the cell. Cell Microbiol 2006;8:387-400.
    • (2006) Cell Microbiol , vol.8 , pp. 387-400
    • Radtke, K.1    Döhner, K.2    Sodeik, B.3
  • 17
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S, Krijnse-Locker J. Modification of intracellular membrane structures for virus replication. Nat Rev Microbiol 2008;6:363-374.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 18
    • 0001551701 scopus 로고    scopus 로고
    • Herpesviridae
    • Fields BN, Knipe DM, Howley PM, editors., 3rd edn. Philadelphia: Lippincott-Raven Publishers
    • Roizman B. Herpesviridae. In: Fields BN, Knipe DM, Howley PM, editors. Fileds Virology, 3rd edn. Philadelphia: Lippincott-Raven Publishers; 1996, pp. 2221-2230.
    • (1996) Fileds Virology , pp. 2221-2230
    • Roizman, B.1
  • 19
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret S, Guay G, Lippé R. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol 2008;82:8605-8618.
    • (2008) J Virol , vol.82 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippé, R.3
  • 20
    • 84867231810 scopus 로고    scopus 로고
    • Deciphering novel host-herpesvirus interactions by virion proteomics
    • Lippé R. Deciphering novel host-herpesvirus interactions by virion proteomics. Front Microbiol 2012;3:1-14.
    • (2012) Front Microbiol , vol.3 , pp. 1-14
    • Lippé, R.1
  • 21
    • 79955661336 scopus 로고    scopus 로고
    • Actin in herpesvirus infection
    • Roberts KL, Baines JD. Actin in herpesvirus infection. Viruses 2011;3:336-346.
    • (2011) Viruses , vol.3 , pp. 336-346
    • Roberts, K.L.1    Baines, J.D.2
  • 22
    • 80052188114 scopus 로고    scopus 로고
    • Coupling viruses to dynein and kinesin-1
    • Dodding MP, Way M. Coupling viruses to dynein and kinesin-1. EMBO J 2011;30:3527-3539.
    • (2011) EMBO J , vol.30 , pp. 3527-3539
    • Dodding, M.P.1    Way, M.2
  • 23
    • 33748948262 scopus 로고    scopus 로고
    • Reconstitution of herpes simplex virus type 1 nuclear capsid egress in vitro
    • Rémillard-Labrosse G, Guay G, Lippé R. Reconstitution of herpes simplex virus type 1 nuclear capsid egress in vitro. J Virol 2006;80:9741-9753.
    • (2006) J Virol , vol.80 , pp. 9741-9753
    • Rémillard-Labrosse, G.1    Guay, G.2    Lippé, R.3
  • 24
    • 50149097733 scopus 로고    scopus 로고
    • Nuclear pore composition and gating in herpes simplex virus-infected cells
    • Hofemeister H, O'Hare P. Nuclear pore composition and gating in herpes simplex virus-infected cells. J Virol 2008;82:8392-8399.
    • (2008) J Virol , vol.82 , pp. 8392-8399
    • Hofemeister, H.1    O'Hare, P.2
  • 26
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • Johnson DC, Baines JD. Herpesviruses remodel host membranes for virus egress. Nat Rev Microbiol 2011;9:382-394.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 27
    • 21644443202 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress
    • Turcotte S, Letellier J, Lippé R. Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress. J Virol 2005;79:8847-8860.
    • (2005) J Virol , vol.79 , pp. 8847-8860
    • Turcotte, S.1    Letellier, J.2    Lippé, R.3
  • 28
    • 43949089146 scopus 로고    scopus 로고
    • Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1
    • Sugimoto K, Uema M, Sagara H, Tanaka M, Sata T, Hashimoto Y, Kawaguchi Y. Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1. J Virol 2008;82:5198-5211.
    • (2008) J Virol , vol.82 , pp. 5198-5211
    • Sugimoto, K.1    Uema, M.2    Sagara, H.3    Tanaka, M.4    Sata, T.5    Hashimoto, Y.6    Kawaguchi, Y.7
  • 29
    • 0024784576 scopus 로고
    • Transformation of Golgi membrane into the envelope of herpes simplex virus in rat anterior pituitary cells
    • Komuro M, Tajima M, Kato K. Transformation of Golgi membrane into the envelope of herpes simplex virus in rat anterior pituitary cells. Eur J Cell Biol 1989;50:398-406.
    • (1989) Eur J Cell Biol , vol.50 , pp. 398-406
    • Komuro, M.1    Tajima, M.2    Kato, K.3
  • 31
    • 0028106296 scopus 로고
    • Intracellular transport of newly synthesized varicella-zoster virus: final envelopment in the trans-Golgi network
    • Gershon AA, Sherman DL, Zhu Z, Gabel CA, Ambron RT, Gershon MD. Intracellular transport of newly synthesized varicella-zoster virus: final envelopment in the trans-Golgi network. J Virol 1994;68:6372-6390.
    • (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
  • 32
    • 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 BG, Karger A, Mettenleiter TC. Ultrastructural analysis of the replication cycle of pseudorabies virus in cell culture: a reassessment. J Virol 1997;71:2072-2082.
    • (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
  • 33
    • 0028269719 scopus 로고
    • The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei
    • van Genderen IL, Brandimarti R, Torrisi MR, Campadelli G, van Meer G. The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei. Virology 1994;200:831-836.
    • (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
  • 34
    • 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 CA, Dasgupta A, Wilson DW. Characterization of herpes simplex virus-containing organelles by subcellular fractionation: role for organelle acidification in assembly of infectious particles. J Virol 2001;75:1236-1251.
    • (2001) J Virol , vol.75 , pp. 1236-1251
    • Harley, C.A.1    Dasgupta, A.2    Wilson, D.W.3
  • 35
    • 77955515275 scopus 로고    scopus 로고
    • Virion incorporation of the herpes simplex virus type 1 tegument protein VP22 is facilitated by trans-Golgi network localization and is independent of interaction with glycoprotein E
    • O'Regan KJ, Brignati MJ, Murphy MA, Bucks MA, Courtney RJ. Virion incorporation of the herpes simplex virus type 1 tegument protein VP22 is facilitated by trans-Golgi network localization and is independent of interaction with glycoprotein E. Virology 2010;405:176-192.
    • (2010) Virology , vol.405 , pp. 176-192
    • O'Regan, K.J.1    Brignati, M.J.2    Murphy, M.A.3    Bucks, M.A.4    Courtney, R.J.5
  • 36
    • 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 TN, Johnson DC. 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 2001;75:1928-1940.
    • (2001) J Virol , vol.75 , pp. 1928-1940
    • McMillan, T.N.1    Johnson, D.C.2
  • 37
    • 8644252674 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 glycoprotein K and the UL20 protein are interdependent for intracellular trafficking and trans-Golgi network localization
    • Foster TP, Melancon JM, Olivier TL, Kousoulas KG. Herpes simplex virus type 1 glycoprotein K and the UL20 protein are interdependent for intracellular trafficking and trans-Golgi network localization. J Virol 2004;78:13262-13277.
    • (2004) J Virol , vol.78 , pp. 13262-13277
    • Foster, T.P.1    Melancon, J.M.2    Olivier, T.L.3    Kousoulas, K.G.4
  • 38
    • 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. Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures. J Virol 2008;82:11354-11361.
    • (2008) J Virol , vol.82 , pp. 11354-11361
    • Desai, P.1    Sexton, G.L.2    Huang, E.3    Person, S.4
  • 39
    • 9944249048 scopus 로고    scopus 로고
    • Alphaherpesvirus glycoprotein M causes the relocalization of plasma membrane proteins
    • Crump CM, Bruun B, Bell S, Pomeranz LE, Minson T, Browne HM. Alphaherpesvirus glycoprotein M causes the relocalization of plasma membrane proteins. J Gen Virol 2004;85(Pt 12):3517-3527.
    • (2004) J Gen Virol , vol.85 , Issue.PART 12 , pp. 3517-3527
    • Crump, C.M.1    Bruun, B.2    Bell, S.3    Pomeranz, L.E.4    Minson, T.5    Browne, H.M.6
  • 40
    • 0032889509 scopus 로고    scopus 로고
    • Intracellular traffic of herpes simplex virus glycoprotein gE: characterization of the sorting signals required for its trans-Golgi network localization
    • Alconada A, Bauer U, Sodeik B, Hoflack B. Intracellular traffic of herpes simplex virus glycoprotein gE: characterization of the sorting signals required for its trans-Golgi network localization. J Virol 1999;73:377-387.
    • (1999) J Virol , vol.73 , pp. 377-387
    • Alconada, A.1    Bauer, U.2    Sodeik, B.3    Hoflack, B.4
  • 41
    • 0345742558 scopus 로고    scopus 로고
    • Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity
    • Beitia Ortiz de Zarate I, Kaelin K, Rozenberg F. Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity. J Virol 2004;78:1540-1551.
    • (2004) J Virol , vol.78 , pp. 1540-1551
    • Beitia Ortiz de Zarate, I.1    Kaelin, K.2    Rozenberg, F.3
  • 42
    • 3543069876 scopus 로고    scopus 로고
    • Internalization of pseudorabies virus glycoprotein B is mediated by an interaction between the YQRL motif in its cytoplasmic domain and the clathrin-associated AP-2 adaptor complex
    • Van Minnebruggen G, Favoreel HW, Nauwynck HJ. Internalization of pseudorabies virus glycoprotein B is mediated by an interaction between the YQRL motif in its cytoplasmic domain and the clathrin-associated AP-2 adaptor complex. J Virol 2004;78:8852-8859.
    • (2004) J Virol , vol.78 , pp. 8852-8859
    • Van Minnebruggen, G.1    Favoreel, H.W.2    Nauwynck, H.J.3
  • 43
    • 0032976556 scopus 로고    scopus 로고
    • Mutation of the YXXL endocytosis motif in the cytoplasmic tail of pseudorabies virus gE
    • Tirabassi RS, Enquist LW. Mutation of the YXXL endocytosis motif in the cytoplasmic tail of pseudorabies virus gE. J Virol 1999;73:2717-2728.
    • (1999) J Virol , vol.73 , pp. 2717-2728
    • Tirabassi, R.S.1    Enquist, L.W.2
  • 44
    • 18744405385 scopus 로고    scopus 로고
    • Pseudorabies virus glycoprotein gD contains a functional endocytosis motif that acts in concert with an endocytosis motif in gB to drive internalization of antibody-antigen complexes from the surface of infected monocytes
    • Ficinska J, Van Minnebruggen G, Nauwynck HJ, Bienkowska-Szewcz K, Favoreel HW. Pseudorabies virus glycoprotein gD contains a functional endocytosis motif that acts in concert with an endocytosis motif in gB to drive internalization of antibody-antigen complexes from the surface of infected monocytes. J Virol 2005;79:7248-7254.
    • (2005) J Virol , vol.79 , pp. 7248-7254
    • Ficinska, J.1    Van Minnebruggen, G.2    Nauwynck, H.J.3    Bienkowska-Szewcz, K.4    Favoreel, H.W.5
  • 45
    • 0033937217 scopus 로고    scopus 로고
    • Trafficking of varicella-zoster virus glycoprotein gI: T(338)-dependent retention in the trans-Golgi network, secretion, and mannose 6-phosphate-inhibitable uptake of the ectodomain
    • Wang ZH, Gershon MD, Lungu O, Zhu Z, Gershon AA. Trafficking of varicella-zoster virus glycoprotein gI: T(338)-dependent retention in the trans-Golgi network, secretion, and mannose 6-phosphate-inhibitable uptake of the ectodomain. J Virol 2000;74:6600-6613.
    • (2000) J Virol , vol.74 , pp. 6600-6613
    • Wang, Z.H.1    Gershon, M.D.2    Lungu, O.3    Zhu, Z.4    Gershon, A.A.5
  • 46
    • 0037379221 scopus 로고    scopus 로고
    • A functional YNKI motif in the short cytoplasmic tail of varicella-zoster virus glycoprotein gH mediates clathrin-dependent and antibody-independent endocytosis
    • Pasieka TJ, Maresova L, Grose C. A functional YNKI motif in the short cytoplasmic tail of varicella-zoster virus glycoprotein gH mediates clathrin-dependent and antibody-independent endocytosis. J Virol 2003;77:4191-4204.
    • (2003) J Virol , vol.77 , pp. 4191-4204
    • Pasieka, T.J.1    Maresova, L.2    Grose, C.3
  • 47
    • 0030901199 scopus 로고    scopus 로고
    • Endocytosis and recycling of varicella-zoster virus Fc receptor glycoprotein gE: internalization mediated by a YXXL motif in the cytoplasmic tail
    • Olson JK, Grose C. Endocytosis and recycling of varicella-zoster virus Fc receptor glycoprotein gE: internalization mediated by a YXXL motif in the cytoplasmic tail. J Virol 1997;71:4042-4054.
    • (1997) J Virol , vol.71 , pp. 4042-4054
    • Olson, J.K.1    Grose, C.2
  • 48
    • 0028971193 scopus 로고
    • Envelopment of varicella-zoster virus: targeting of viral glycoproteins to the trans-Golgi network
    • Zhu Z, Gershon MD, Hao Y, Ambron RT, Gabel CA, Gershon AA. Envelopment of varicella-zoster virus: targeting of viral glycoproteins to the trans-Golgi network. J Virol 1995;69:7951-7959.
    • (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
  • 49
    • 0029794452 scopus 로고    scopus 로고
    • Targeting of glycoprotein I (gE) of varicella-zoster virus to the trans-Golgi network by an AYRV sequence and an acidic amino acid-rich patch in the cytosolic domain of the molecule
    • Zhu Z, Hao Y, Gershon MD, Ambron RT, Gershon AA. Targeting of glycoprotein I (gE) of varicella-zoster virus to the trans-Golgi network by an AYRV sequence and an acidic amino acid-rich patch in the cytosolic domain of the molecule. J Virol 1996;70:6563-6575.
    • (1996) J Virol , vol.70 , pp. 6563-6575
    • Zhu, Z.1    Hao, Y.2    Gershon, M.D.3    Ambron, R.T.4    Gershon, A.A.5
  • 50
    • 0029858530 scopus 로고    scopus 로고
    • A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network
    • Alconada A, Bauer U, Hoflack B. A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network. EMBO J 1996;15:6096-6110.
    • (1996) EMBO J , vol.15 , pp. 6096-6110
    • Alconada, A.1    Bauer, U.2    Hoflack, B.3
  • 51
    • 0035918969 scopus 로고    scopus 로고
    • VZV gB endocytosis and Golgi localization are mediated by YXXphi motifs in its cytoplasmic domain
    • Heineman TC, Hall SL. VZV gB endocytosis and Golgi localization are mediated by YXXphi motifs in its cytoplasmic domain. Virology 2001;285:42-49.
    • (2001) Virology , vol.285 , pp. 42-49
    • Heineman, T.C.1    Hall, S.L.2
  • 52
    • 33646038897 scopus 로고    scopus 로고
    • The why's of Y-based motifs in alphaherpesvirus envelope proteins
    • Favoreel HW. The why's of Y-based motifs in alphaherpesvirus envelope proteins. Virus Res 2006;117:202-208.
    • (2006) Virus Res , vol.117 , pp. 202-208
    • Favoreel, H.W.1
  • 53
    • 0029949793 scopus 로고    scopus 로고
    • An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress
    • Browne H, Bell S, Minson T, Wilson DW. An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress. J Virol 1996;70:4311-4316.
    • (1996) J Virol , vol.70 , pp. 4311-4316
    • Browne, H.1    Bell, S.2    Minson, T.3    Wilson, D.W.4
  • 54
    • 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, Browne H. Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network. J Virol 1999;73:9515-9520.
    • (1999) J Virol , vol.73 , pp. 9515-9520
    • Whiteley, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 55
    • 0026083301 scopus 로고
    • Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress
    • Whealy ME, Card JP, Meade RP, Robbins AK, Enquist LW. Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress. J Virol 1991;65:1066-1081.
    • (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
  • 56
    • 67649891816 scopus 로고    scopus 로고
    • Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane
    • Rémillard-Labrosse G, Mihai C, Duron J, Guay G, Lippé R. Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane. Traffic 2009;10:1074-1083.
    • (2009) Traffic , vol.10 , pp. 1074-1083
    • Rémillard-Labrosse, G.1    Mihai, C.2    Duron, J.3    Guay, G.4    Lippé, R.5
  • 57
    • 77956845138 scopus 로고    scopus 로고
    • Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins
    • Roberts KL, Baines JD. Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins. J Virol 2010;84:9889-9896.
    • (2010) J Virol , vol.84 , pp. 9889-9896
    • Roberts, K.L.1    Baines, J.D.2
  • 59
    • 34447265020 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4
    • Crump CM, Yates C, Minson T. Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4. J Virol 2007;81:7380-7387.
    • (2007) J Virol , vol.81 , pp. 7380-7387
    • Crump, C.M.1    Yates, C.2    Minson, T.3
  • 61
    • 79955460678 scopus 로고    scopus 로고
    • Early induction of autophagy in human fibroblasts after infection with human cytomegalovirus or herpes simplex virus 1
    • McFarlane S, Aitken J, Sutherland JS, Nicholl MJ, Preston VG, Preston CM. Early induction of autophagy in human fibroblasts after infection with human cytomegalovirus or herpes simplex virus 1. J Virol 2011;85:4212-4221.
    • (2011) J Virol , vol.85 , pp. 4212-4221
    • McFarlane, S.1    Aitken, J.2    Sutherland, J.S.3    Nicholl, M.J.4    Preston, V.G.5    Preston, C.M.6
  • 63
    • 77955239270 scopus 로고    scopus 로고
    • Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites
    • Zoppino FC, Militello RD, Slavin I, Alvarez C, Colombo MI. Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites. Traffic 2010;11:1246-1261.
    • (2010) Traffic , vol.11 , pp. 1246-1261
    • Zoppino, F.C.1    Militello, R.D.2    Slavin, I.3    Alvarez, C.4    Colombo, M.I.5
  • 64
    • 79961195618 scopus 로고    scopus 로고
    • Analysis of Rab GTPase-activating proteins indicates that Rab1a/b and Rab43 are important for herpes simplex virus 1 secondary envelopment
    • Zenner HL, Yoshimura S, Barr FA, Crump CM. Analysis of Rab GTPase-activating proteins indicates that Rab1a/b and Rab43 are important for herpes simplex virus 1 secondary envelopment. J Virol 2011;85:8012-8021.
    • (2011) J Virol , vol.85 , pp. 8012-8021
    • Zenner, H.L.1    Yoshimura, S.2    Barr, F.A.3    Crump, C.M.4
  • 65
    • 36048964024 scopus 로고    scopus 로고
    • Analysis of the role of autophagy in replication of herpes simplex virus in cell culture
    • Alexander DE, Ward SL, Mizushima N, Levine B, Leib DA. Analysis of the role of autophagy in replication of herpes simplex virus in cell culture. J Virol 2007;81:12128-12134.
    • (2007) J Virol , vol.81 , pp. 12128-12134
    • Alexander, D.E.1    Ward, S.L.2    Mizushima, N.3    Levine, B.4    Leib, D.A.5
  • 66
    • 70350322311 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression
    • Pawliczek T, Crump CM. Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. J Virol 2009;83:11254-11264.
    • (2009) J Virol , vol.83 , pp. 11254-11264
    • Pawliczek, T.1    Crump, C.M.2
  • 67
    • 39149132089 scopus 로고    scopus 로고
    • ESCRT complexes and the biogenesis of multivesicular bodies
    • Hurley JH. ESCRT complexes and the biogenesis of multivesicular bodies. Curr Opin Cell Biol 2008;20:4-11.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 4-11
    • Hurley, J.H.1
  • 68
    • 46049099346 scopus 로고    scopus 로고
    • Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding
    • Kieffer C, Skalicky JJ, Morita E, De Domenico I, Ward DM, Kaplan J, Sundquist WI. Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding. Dev Cell 2008;15:62-73.
    • (2008) Dev Cell , vol.15 , pp. 62-73
    • Kieffer, C.1    Skalicky, J.J.2    Morita, E.3    De Domenico, I.4    Ward, D.M.5    Kaplan, J.6    Sundquist, W.I.7
  • 70
    • 70349748558 scopus 로고    scopus 로고
    • Human cytomegalovirus exploits ESCRT machinery in the process of virion maturation
    • Tandon R, AuCoin DP, Mocarski ES. Human cytomegalovirus exploits ESCRT machinery in the process of virion maturation. J Virol 2009;83:10797-10807.
    • (2009) J Virol , vol.83 , pp. 10797-10807
    • Tandon, R.1    AuCoin, D.P.2    Mocarski, E.S.3
  • 71
    • 79952860790 scopus 로고    scopus 로고
    • The tegument protein UL71 of human cytomegalovirus is involved in late envelopment and affects multivesicular bodies
    • Schauflinger M, Fischer D, Schreiber A, Chevillotte M, Walther P, Mertens T, von Einem J. The tegument protein UL71 of human cytomegalovirus is involved in late envelopment and affects multivesicular bodies. J Virol 2011;85:3821-3832.
    • (2011) J Virol , vol.85 , pp. 3821-3832
    • Schauflinger, M.1    Fischer, D.2    Schreiber, A.3    Chevillotte, M.4    Walther, P.5    Mertens, T.6    von Einem, J.7
  • 73
    • 0034027177 scopus 로고    scopus 로고
    • Human cytomegalovirus pp28 (UL99) localizes to a cytoplasmic compartment which overlaps the endoplasmic reticulum-golgi-intermediate compartment
    • Sanchez V, Sztul E, Britt WJ. Human cytomegalovirus pp28 (UL99) localizes to a cytoplasmic compartment which overlaps the endoplasmic reticulum-golgi-intermediate compartment. J Virol 2000;74:3842-3851.
    • (2000) J Virol , vol.74 , pp. 3842-3851
    • Sanchez, V.1    Sztul, E.2    Britt, W.J.3
  • 74
    • 0037369083 scopus 로고    scopus 로고
    • Envelopment of human cytomegalovirus occurs by budding into Golgi-derived vacuole compartments positive for gB, Rab 3, trans-golgi network 46, and mannosidase II
    • Homman-Loudiyi M, Hultenby K, Britt W, Soderberg-Naucler C. Envelopment of human cytomegalovirus occurs by budding into Golgi-derived vacuole compartments positive for gB, Rab 3, trans-golgi network 46, and mannosidase II. J Virol 2003;77:3191-3203.
    • (2003) J Virol , vol.77 , pp. 3191-3203
    • Homman-Loudiyi, M.1    Hultenby, K.2    Britt, W.3    Soderberg-Naucler, C.4
  • 75
    • 77950605680 scopus 로고    scopus 로고
    • Human cytomegalovirus final envelopment on membranes containing both trans-Golgi network and endosomal markers
    • Cepeda V, Esteban M, Fraile-Ramos A. Human cytomegalovirus final envelopment on membranes containing both trans-Golgi network and endosomal markers. Cell Microbiol 2010;12:386-404.
    • (2010) Cell Microbiol , vol.12 , pp. 386-404
    • Cepeda, V.1    Esteban, M.2    Fraile-Ramos, A.3
  • 76
    • 79955966742 scopus 로고    scopus 로고
    • A role for the SNARE protein syntaxin 3 in human cytomegalovirus morphogenesis
    • Cepeda V, Fraile-Ramos A. A role for the SNARE protein syntaxin 3 in human cytomegalovirus morphogenesis. Cell Microbiol 2011;13:846-858.
    • (2011) Cell Microbiol , vol.13 , pp. 846-858
    • Cepeda, V.1    Fraile-Ramos, A.2
  • 77
    • 80053359163 scopus 로고    scopus 로고
    • Melanosomes on the move: a model to understand organelle dynamics
    • Hume AN, Seabra MC. Melanosomes on the move: a model to understand organelle dynamics. Biochem Soc Trans 2011;39:1191-1196.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1191-1196
    • Hume, A.N.1    Seabra, M.C.2
  • 79
    • 70350391655 scopus 로고    scopus 로고
    • HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein FIP4
    • Krzyzaniak MA, Mach M, Britt WJ. HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein FIP4. Traffic 2009;10:1439-1457.
    • (2009) Traffic , vol.10 , pp. 1439-1457
    • Krzyzaniak, M.A.1    Mach, M.2    Britt, W.J.3
  • 80
    • 0141565125 scopus 로고    scopus 로고
    • Role of PACS-1 in trafficking of human cytomegalovirus glycoprotein B and virus production
    • Crump CM, Hung CH, Thomas L, Wan L, Thomas G. Role of PACS-1 in trafficking of human cytomegalovirus glycoprotein B and virus production. J Virol 2003;77:11105-11113.
    • (2003) J Virol , vol.77 , pp. 11105-11113
    • Crump, C.M.1    Hung, C.H.2    Thomas, L.3    Wan, L.4    Thomas, G.5
  • 81
    • 79955407758 scopus 로고    scopus 로고
    • A role for the small GTPase Rab6 in assembly of human cytomegalovirus
    • Indran SV, Britt WJ. A role for the small GTPase Rab6 in assembly of human cytomegalovirus. J Virol 2011;85:5213-5129.
    • (2011) J Virol , vol.85 , pp. 5213-5129
    • Indran, S.V.1    Britt, W.J.2
  • 85
    • 79958109316 scopus 로고    scopus 로고
    • Spatial relationships between markers for secretory and endosomal machinery in human cytomegalovirus-infected cells versus those in uninfected cells
    • Das S, Pellett PE. Spatial relationships between markers for secretory and endosomal machinery in human cytomegalovirus-infected cells versus those in uninfected cells. J Virol 2011;85:5864-5879.
    • (2011) J Virol , vol.85 , pp. 5864-5879
    • Das, S.1    Pellett, P.E.2
  • 86
    • 0028857923 scopus 로고
    • Redistribution of microtubules and Golgi apparatus in herpes simplex virus-infected cells and their role in viral exocytosis
    • Avitabile E, Di Gaeta S, Torrisi MR, Ward PL, Roizman B, Campadelli-Fiume G. Redistribution of microtubules and Golgi apparatus in herpes simplex virus-infected cells and their role in viral exocytosis. J Virol 1995;69:7472-7482.
    • (1995) J Virol , vol.69 , pp. 7472-7482
    • Avitabile, E.1    Di Gaeta, S.2    Torrisi, M.R.3    Ward, P.L.4    Roizman, B.5    Campadelli-Fiume, G.6
  • 87
    • 0027511479 scopus 로고
    • Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1
    • Campadelli G, Brandimarti R, Di Lazzaro C, Ward PL, Roizman B, Torrisi MR. Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1. Proc Natl Acad Sci U S A 1993;90:2798-2802.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2798-2802
    • Campadelli, G.1    Brandimarti, R.2    Di Lazzaro, C.3    Ward, P.L.4    Roizman, B.5    Torrisi, M.R.6
  • 88
    • 79953315804 scopus 로고    scopus 로고
    • Herpes simplex virus dances with amyloid precursor protein while exiting the cell
    • Cheng SB, Ferland P, Webster P, Bearer EL. Herpes simplex virus dances with amyloid precursor protein while exiting the cell. PLoS One 2011;6:e17966.
    • (2011) PLoS One , vol.6
    • Cheng, S.B.1    Ferland, P.2    Webster, P.3    Bearer, E.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.