메뉴 건너뛰기




Volumn 89, Issue 3, 2015, Pages 1502-1511

The large tegument protein pUL36 is essential for formation of the capsid vertex-specific component at the capsid-tegument interface of herpes simplex virus 1

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; PROTEIN PUL17; PROTEIN PUL25; PROTEIN PUL36; PROTEIN PUL37; UNCLASSIFIED DRUG; VIRUS PROTEIN; UL36 PROTEIN, HUMAN HERPESVIRUS 1;

EID: 84921453194     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02887-14     Document Type: Article
Times cited : (45)

References (65)
  • 1
    • 84974731299 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • In Knipe DM, Howley PM, Cohen JI, Griffin DE, Lamb RA, Martin MA, Racaniello VR, Roizman B (ed), 6th ed, Lippincott Williams&Wilkins, Philadelphia, PA
    • Roizman B, Knipe DM, Whitley RJ. 2013. Herpes simplex viruses, p 1824-1897. In Knipe DM, Howley PM, Cohen JI, Griffin DE, Lamb RA, Martin MA, Racaniello VR, Roizman B (ed), Fields virology, 6th ed, vol 2. Lippincott Williams&Wilkins, Philadelphia, PA.
    • (2013) Fields virology , vol.2 , pp. 1824-1897
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 2
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret S, Guay G, Lippe R. 2008. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol 82:8605-8618. http://dx.doi.org/10.1128/JVI.00904-08.
    • (2008) J Virol , vol.82 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippe, R.3
  • 3
    • 0030298322 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation
    • Newcomb WW, Homa FL, Thomsen DR, Booy FP, Trus BL, Steven AC, Spencer JV, Brown JC. 1996. Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation. J Mol Biol 263:432-446. http://dx.doi.org/10.1006/jmbi.1996.0587.
    • (1996) J Mol Biol , vol.263 , pp. 432-446
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Booy, F.P.4    Trus, B.L.5    Steven, A.C.6    Spencer, J.V.7    Brown, J.C.8
  • 4
    • 0033919955 scopus 로고    scopus 로고
    • Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus
    • Newcomb WW, Trus BL, Cheng NQ, Steven AC, Sheaffer AK, Tenney DJ, Weller SK, Brown JC. 2000. Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus. J Virol 74:1663-1673. http://dx.doi.org/10.1128/JVI.74.4.1663-1673.2000.
    • (2000) J Virol , vol.74 , pp. 1663-1673
    • Newcomb, W.W.1    Trus, B.L.2    Cheng, N.Q.3    Steven, A.C.4    Sheaffer, A.K.5    Tenney, D.J.6    Weller, S.K.7    Brown, J.C.8
  • 5
    • 0034766951 scopus 로고    scopus 로고
    • The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid
    • Newcomb WW, Juhas RM, Thomsen DR, Homa FL, Burch AD, Weller SK, Brown JC. 2001. The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid. J Virol 75:10923-10932. http://dx.doi.org/10.1128/JVI.75.22.10923-10932.2001.
    • (2001) J Virol , vol.75 , pp. 10923-10932
    • Newcomb, W.W.1    Juhas, R.M.2    Thomsen, D.R.3    Homa, F.L.4    Burch, A.D.5    Weller, S.K.6    Brown, J.C.7
  • 6
    • 7644228864 scopus 로고    scopus 로고
    • Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1
    • Trus BL, Chen NQ, Newcomb WW, Homa FL, Brown JC, Steven AC. 2004. Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1. J Virol 78:12668-12671. http://dx.doi.org/10.1128/JVI.78.22.12668-12671.2004.
    • (2004) J Virol , vol.78 , pp. 12668-12671
    • Trus, B.L.1    Chen, N.Q.2    Newcomb, W.W.3    Homa, F.L.4    Brown, J.C.5    Steven, A.C.6
  • 7
    • 78951479560 scopus 로고    scopus 로고
    • Seeing the portal in herpes simplex virus type 1 B capsids
    • Rochat RH, Liu X, Murata K, Nagayama K, Rixon FJ, Chiu W. 2011. Seeing the portal in herpes simplex virus type 1 B capsids. J Virol 85:1871-1874. http://dx.doi.org/10.1128/JVI.01663-10.
    • (2011) J Virol , vol.85 , pp. 1871-1874
    • Rochat, R.H.1    Liu, X.2    Murata, K.3    Nagayama, K.4    Rixon, F.J.5    Chiu, W.6
  • 8
    • 0020678189 scopus 로고
    • Identification and characterization of a herpes simplex virus gene product required for encapsidation of virus DNA
    • Preston VG, Coates JAV, Rixon FJ. 1983. Identification and characterization of a herpes simplex virus gene product required for encapsidation of virus DNA. J Virol 45:1056-1064.
    • (1983) J Virol , vol.45 , pp. 1056-1064
    • Preston, V.G.1    Coates, J.A.V.2    Rixon, F.J.3
  • 9
    • 0037406441 scopus 로고    scopus 로고
    • Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy
    • Heymann JB, Cheng NQ, Newcomb WW, Trus BL, Brown JC, Steven AC. 2003. Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Nat Struct Biol 10:334-341. http://dx.doi.org/10.1038/nsb922.
    • (2003) Nat Struct Biol , vol.10 , pp. 334-341
    • Heymann, J.B.1    Cheng, N.Q.2    Newcomb, W.W.3    Trus, B.L.4    Brown, J.C.5    Steven, A.C.6
  • 10
    • 82355175265 scopus 로고    scopus 로고
    • Herpes simplex virus capsid assembly and DNA packaging: a present and future antiviral drug target
    • Baines JD. 2011. Herpes simplex virus capsid assembly and DNA packaging: a present and future antiviral drug target. Trends Microbiol 19:606-613. http://dx.doi.org/10.1016/j.tim.2011.09.001.
    • (2011) Trends Microbiol , vol.19 , pp. 606-613
    • Baines, J.D.1
  • 11
    • 79955374201 scopus 로고    scopus 로고
    • Residues of the UL25 protein of herpes simplex virus that are required for its stable interaction with capsids
    • Cockrell SK, Huffman JB, Toropova K, Conway JF, Homa FL. 2011. Residues of the UL25 protein of herpes simplex virus that are required for its stable interaction with capsids. J Virol 85:4875-4887. http://dx.doi.org/10.1128/JVI.00242-11.
    • (2011) J Virol , vol.85 , pp. 4875-4887
    • Cockrell, S.K.1    Huffman, J.B.2    Toropova, K.3    Conway, J.F.4    Homa, F.L.5
  • 12
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • Johnson DC, Baines JD. 2011. Herpesviruses remodel host membranes for virus egress. Nat Rev Microbiol 9:382-394. http://dx.doi.org/10.1038/nrmicro2559.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 13
    • 33746318034 scopus 로고    scopus 로고
    • Herpesvirus assembly: a tale of two membranes
    • Mettenleiter TC, Klupp BG, Granzow H. 2006. Herpesvirus assembly: a tale of two membranes. Curr Opin Microbiol 9:423-429. http://dx.doi.org/10.1016/j.mib.2006.06.013.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 423-429
    • Mettenleiter, T.C.1    Klupp, B.G.2    Granzow, H.3
  • 14
    • 68749090845 scopus 로고    scopus 로고
    • Herpesvirus assembly: an update
    • Mettenleiter TC, Klupp BG, Granzow H. 2009. Herpesvirus assembly: an update. Virus Res 143:222-234. http://dx.doi.org/10.1016/j.virusres.2009.03.018.
    • (2009) Virus Res , vol.143 , pp. 222-234
    • Mettenleiter, T.C.1    Klupp, B.G.2    Granzow, H.3
  • 15
    • 35148834647 scopus 로고    scopus 로고
    • Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies
    • Calistri A, Sette P, Salata C, Cancellotti E, Forghieri C, Cornin A, Goettlinger H, Campadelli-Fiume G, Palu G, Parolin C. 2007. Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies. J Virol 81:11468-11478. http://dx.doi.org/10.1128/JVI.01364-07.
    • (2007) J Virol , vol.81 , pp. 11468-11478
    • Calistri, A.1    Sette, P.2    Salata, C.3    Cancellotti, E.4    Forghieri, C.5    Cornin, A.6    Goettlinger, H.7    Campadelli-Fiume, G.8    Palu, G.9    Parolin, C.10
  • 16
    • 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. 2009. Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. J Virol 83:11254-11264. http://dx.doi.org/10.1128/JVI.00574-09.
    • (2009) J Virol , vol.83 , pp. 11254-11264
    • Pawliczek, T.1    Crump, C.M.2
  • 17
    • 84867232564 scopus 로고    scopus 로고
    • Herpesviruses exploit several host compartments for envelopment
    • Henaff D, Radtke K, Lippe R. 2012. Herpesviruses exploit several host compartments for envelopment. Traffic 13:1443-1449. http://dx.doi.org/10.1111/j.1600-0854.2012.01399.x.
    • (2012) Traffic , vol.13 , pp. 1443-1449
    • Henaff, D.1    Radtke, K.2    Lippe, R.3
  • 18
    • 84868587398 scopus 로고    scopus 로고
    • Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus
    • Hollinshead M, Johns HL, Sayers CL, Gonzalez-Lopez C, Smith GL, Elliott G. 2012. Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus. EMBO J 31:4204-4220. http://dx.doi.org/10.1038/emboj.2012.262.
    • (2012) EMBO J , vol.31 , pp. 4204-4220
    • Hollinshead, M.1    Johns, H.L.2    Sayers, C.L.3    Gonzalez-Lopez, C.4    Smith, G.L.5    Elliott, G.6
  • 19
    • 0026551804 scopus 로고
    • Assembly of enveloped tegument structures (L-particles) can occur independently of virion maturation in herpes-simplex virus type 1-infected cells
    • Rixon FJ, Addison C, McLauchlan J. 1992. Assembly of enveloped tegument structures (L-particles) can occur independently of virion maturation in herpes-simplex virus type 1-infected cells. J Gen Virol 73:277-284. http://dx.doi.org/10.1099/0022-1317-73-2-277.
    • (1992) J Gen Virol , vol.73 , pp. 277-284
    • Rixon, F.J.1    Addison, C.2    McLauchlan, J.3
  • 20
    • 58149393193 scopus 로고    scopus 로고
    • Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1
    • Roberts APE, Abaitua F, O'Hare P, McNab D, Rixon FJ, Pasdeloup D. 2009. Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1. J Virol 83:105-116. http://dx.doi.org/10.1128/JVI.01032-08.
    • (2009) J Virol , vol.83 , pp. 105-116
    • Roberts, A.P.E.1    Abaitua, F.2    O'Hare, P.3    McNab, D.4    Rixon, F.J.5    Pasdeloup, D.6
  • 21
    • 0026100629 scopus 로고
    • Identification and characterization of a novel non-infectious herpes simplex virus-related particle
    • Szilágyi JF, Cunningham C. 1991. Identification and characterization of a novel non-infectious herpes simplex virus-related particle. J Gen Virol 72:661-668. http://dx.doi.org/10.1099/0022-1317-72-3-661.
    • (1991) J Gen Virol , vol.72 , pp. 661-668
    • Szilágyi, J.F.1    Cunningham, C.2
  • 22
    • 0028068631 scopus 로고
    • The herpes simplex virus type 1 UL37 gene-product is a component of virus particles
    • McLauchlan J, Liefkens K, Stow ND. 1994. The herpes simplex virus type 1 UL37 gene-product is a component of virus particles. J Gen Virol 75:2047-2052. http://dx.doi.org/10.1099/0022-1317-75-8-2047.
    • (1994) J Gen Virol , vol.75 , pp. 2047-2052
    • McLauchlan, J.1    Liefkens, K.2    Stow, N.D.3
  • 23
    • 55549112567 scopus 로고    scopus 로고
    • Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures
    • Desai P, Sexton GL, Huang E, Person S. 2008. Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures. J Virol 82:11354-11361. http://dx.doi.org/10.1128/JVI.00956-08.
    • (2008) J Virol , vol.82 , pp. 11354-11361
    • Desai, P.1    Sexton, G.L.2    Huang, E.3    Person, S.4
  • 24
    • 22544438727 scopus 로고    scopus 로고
    • Determination of interactions between tegument proteins of herpes simplex virus type 1
    • Vittone V, Diefenbach E, Triffett D, Douglas MW, Cunningham AL, Diefenbach RJ. 2005. Determination of interactions between tegument proteins of herpes simplex virus type 1. J Virol 79:9566-9571. http://dx.doi.org/10.1128/JVI.79.15.9566-9571.2005.
    • (2005) J Virol , vol.79 , pp. 9566-9571
    • Vittone, V.1    Diefenbach, E.2    Triffett, D.3    Douglas, M.W.4    Cunningham, A.L.5    Diefenbach, R.J.6
  • 25
    • 35349025922 scopus 로고    scopus 로고
    • Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1/2) mediate binding of tegument protein pUL37
    • Mijatov B, Cunningham AL, Diefenbach RJ. 2007. Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1/2) mediate binding of tegument protein pUL37. Virology 368:26-31. http://dx.doi.org/10.1016/j.virol.2007.07.005.
    • (2007) Virology , vol.368 , pp. 26-31
    • Mijatov, B.1    Cunningham, A.L.2    Diefenbach, R.J.3
  • 26
    • 0034466764 scopus 로고    scopus 로고
    • A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells
    • Desai PJ. 2000. A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells. J Virol 74:11608-11618. http://dx.doi.org/10.1128/JVI.74.24.11608-11618.2000.
    • (2000) J Virol , vol.74 , pp. 11608-11618
    • Desai, P.J.1
  • 27
    • 0034785814 scopus 로고    scopus 로고
    • A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation
    • Desai P, Sexton GL, McCaffery JM, Person S. 2001. A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation. J Virol 75:10259-10271. http://dx.doi.org/10.1128/JVI.75.21.10259-10271.2001.
    • (2001) J Virol , vol.75 , pp. 10259-10271
    • Desai, P.1    Sexton, G.L.2    McCaffery, J.M.3    Person, S.4
  • 28
    • 0345471494 scopus 로고    scopus 로고
    • Visualization of tegument-capsid interactions andDNAin intact herpes simplex virus type 1 virions
    • Zhou ZH, Chen DH, Jakana J, Rixon FJ, Chiu W. 1999. Visualization of tegument-capsid interactions andDNAin intact herpes simplex virus type 1 virions. J Virol 73:3210-3218.
    • (1999) J Virol , vol.73 , pp. 3210-3218
    • Zhou, Z.H.1    Chen, D.H.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5
  • 30
    • 84868153297 scopus 로고    scopus 로고
    • Atail-like assembly at the portal vertex in intact herpes simplex type-1 virions
    • Schmid MF, Hecksel CW, Rochat RH, Bhella D, Chiu W, Rixon FJ. 2012. Atail-like assembly at the portal vertex in intact herpes simplex type-1 virions. PLoS Pathog 8:e1002961. http://dx.doi.org/10.1371/journal.ppat.1002961.
    • (2012) PLoS Pathog , vol.8
    • Schmid, M.F.1    Hecksel, C.W.2    Rochat, R.H.3    Bhella, D.4    Chiu, W.5    Rixon, F.J.6
  • 31
    • 0033587536 scopus 로고    scopus 로고
    • Three-dimensional visualization of tegument/capsid interactions in the intact human cytomegalovirus
    • Chen DH, Jiang H, Lee M, Liu FY, Zhou ZH. 1999. Three-dimensional visualization of tegument/capsid interactions in the intact human cytomegalovirus. Virology 260:10-16. http://dx.doi.org/10.1006/viro.1999.9791.
    • (1999) Virology , vol.260 , pp. 10-16
    • Chen, D.H.1    Jiang, H.2    Lee, M.3    Liu, F.Y.4    Zhou, Z.H.5
  • 32
    • 0033045991 scopus 로고    scopus 로고
    • Capsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites
    • Trus BL, Gibson W, Cheng NQ, Steven AC. 1999. Capsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites. J Virol 73:2181-2192.
    • (1999) J Virol , vol.73 , pp. 2181-2192
    • Trus, B.L.1    Gibson, W.2    Cheng, N.Q.3    Steven, A.C.4
  • 34
    • 84883422214 scopus 로고    scopus 로고
    • The smallest capsid protein mediates binding of the essential tegument protein pp150 to stabilize DNAcontaining capsids in human cytomegalovirus
    • Dai X, Yu X, Gong H, Jiang X, Abenes G, Liu H, Shivakoti S, Britt WJ, Zhu H, Liu F, Zhou ZH. 2013. The smallest capsid protein mediates binding of the essential tegument protein pp150 to stabilize DNAcontaining capsids in human cytomegalovirus. PLoS Pathog 9(8): e1003525. http://dx.doi.org/10.1371/journal.ppat.1003525.
    • (2013) PLoS Pathog , vol.9 , Issue.8
    • Dai, X.1    Yu, X.2    Gong, H.3    Jiang, X.4    Abenes, G.5    Liu, H.6    Shivakoti, S.7    Britt, W.J.8    Zhu, H.9    Liu, F.10    Zhou, Z.H.11
  • 35
    • 84907979342 scopus 로고    scopus 로고
    • Organization of capsidassociated tegument components in Kaposi's sarcoma-associated herpesvirus
    • Dai X, Gong D, Wu T-T, Sun R, Zhou ZH. 2014. Organization of capsidassociated tegument components in Kaposi's sarcoma-associated herpesvirus. J Virol 88:12694-12702. http://dx.doi.org/10.1128/JVI.01509-14.
    • (2014) J Virol , vol.88 , pp. 12694-12702
    • Dai, X.1    Gong, D.2    Wu, T.-T.3    Sun, R.4    Zhou, Z.H.5
  • 36
    • 34248583632 scopus 로고    scopus 로고
    • Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-filled HSV-1 capsids
    • Trus BL, Newcomb WW, Cheng NQ, Cardone G, Marekov L, Horna FL, Brown JC, Steven AC. 2007. Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-filled HSV-1 capsids. Mol Cell 26:479-489. http://dx.doi.org/10.1016/j.molcel.2007.04.010.
    • (2007) Mol Cell , vol.26 , pp. 479-489
    • Trus, B.L.1    Newcomb, W.W.2    Cheng, N.Q.3    Cardone, G.4    Marekov, L.5    Horna, F.L.6    Brown, J.C.7    Steven, A.C.8
  • 37
    • 77349090419 scopus 로고    scopus 로고
    • Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton
    • Conway JF, Cockrell SK, Copeland AM, Newcomb WW, Brown JC, Homa FL. 2010. Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton. J Mol Biol 397:575-586. http://dx.doi.org/10.1016/j.jmb.2010.01.043.
    • (2010) J Mol Biol , vol.397 , pp. 575-586
    • Conway, J.F.1    Cockrell, S.K.2    Copeland, A.M.3    Newcomb, W.W.4    Brown, J.C.5    Homa, F.L.6
  • 38
    • 79960400096 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL17 protein is the second constituent of the capsid vertex-specific component required for DNA packaging and retention
    • Toropova K, Huffman JB, Homa FL, Conway JF. 2011. The herpes simplex virus 1 UL17 protein is the second constituent of the capsid vertex-specific component required for DNA packaging and retention. J Virol 85:7513-7522. http://dx.doi.org/10.1128/JVI.00837-11.
    • (2011) J Virol , vol.85 , pp. 7513-7522
    • Toropova, K.1    Huffman, J.B.2    Homa, F.L.3    Conway, J.F.4
  • 39
    • 84883272572 scopus 로고    scopus 로고
    • Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins
    • Homa FL, Huffman JB, Toropova K, Lopez HR, Makhov AM, Conway JF. 2013. Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins. J Mol Biol 425:3415-3428. http://dx.doi.org/10.1016/j.jmb.2013.06.034.
    • (2013) J Mol Biol , vol.425 , pp. 3415-3428
    • Homa, F.L.1    Huffman, J.B.2    Toropova, K.3    Lopez, H.R.4    Makhov, A.M.5    Conway, J.F.6
  • 40
    • 84861375995 scopus 로고    scopus 로고
    • The UL36 tegument protein of herpes simplex virus 1 has a composite binding site at the capsid vertices
    • Cardone G, Newcomb WW, Cheng N, Wingfield PT, Trus BL, Brown JC, Steven AC. 2012. The UL36 tegument protein of herpes simplex virus 1 has a composite binding site at the capsid vertices. J Virol 86:4058-4064. http://dx.doi.org/10.1128/JVI.00012-12.
    • (2012) J Virol , vol.86 , pp. 4058-4064
    • Cardone, G.1    Newcomb, W.W.2    Cheng, N.3    Wingfield, P.T.4    Trus, B.L.5    Brown, J.C.6    Steven, A.C.7
  • 41
    • 0028151168 scopus 로고
    • Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy
    • Zhou ZH, Prasad BVV, Jakana J, Rixon FJ, Chiu W. 1994. Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy. J Mol Biol 242:456-469. http://dx.doi.org/10.1006/jmbi.1994.1594.
    • (1994) J Mol Biol , vol.242 , pp. 456-469
    • Zhou, Z.H.1    Prasad, B.V.V.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5
  • 42
    • 0033986875 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 UL34 gene product is required for viral envelopment
    • Roller RJ, Zhou YP, Schnetzer R, Ferguson J, DeSalvo D. 2000. Herpes simplex virus type 1 UL34 gene product is required for viral envelopment. J Virol 74:117-129. http://dx.doi.org/10.1128/JVI.74.1.117-129.2000.
    • (2000) J Virol , vol.74 , pp. 117-129
    • Roller, R.J.1    Zhou, Y.P.2    Schnetzer, R.3    Ferguson, J.4    DeSalvo, D.5
  • 44
    • 10644290789 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments
    • Thurlow JK, Rixon FJ, Murphy M, Targett-Adams P, Hughes M, Preston VG. 2005. The herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments. J Virol 79:150-158. http://dx.doi.org/10.1128/JVI.79.1.150-158.2005.
    • (2005) J Virol , vol.79 , pp. 150-158
    • Thurlow, J.K.1    Rixon, F.J.2    Murphy, M.3    Targett-Adams, P.4    Hughes, M.5    Preston, V.G.6
  • 45
    • 43949107502 scopus 로고    scopus 로고
    • Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein
    • Abaitua F, O'Hare P. 2008. Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein. J Virol 82:5234-5244. http://dx.doi.org/10.1128/JVI.02497-07.
    • (2008) J Virol , vol.82 , pp. 5234-5244
    • Abaitua, F.1    O'Hare, P.2
  • 46
    • 0028057836 scopus 로고
    • Retention of the herpes simplex virus type 1 (HSV-1) UL37 protein on single-stranded DNA columns requires the HSV-1 ICP8 protein
    • Shelton LS, Albright AG, Ruyechan WT, Jenkins FJ. 1994. Retention of the herpes simplex virus type 1 (HSV-1) UL37 protein on single-stranded DNA columns requires the HSV-1 ICP8 protein. J Virol 68:521-525.
    • (1994) J Virol , vol.68 , pp. 521-525
    • Shelton, L.S.1    Albright, A.G.2    Ruyechan, W.T.3    Jenkins, F.J.4
  • 47
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • Heymann JB, Belnap DM. 2007. Bsoft: image processing and molecular modeling for electron microscopy. J Struct Biol 157:3-18. http://dx.doi.org/10.1016/j.jsb.2006.06.006.
    • (2007) J Struct Biol , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 48
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, Radermacher M, Penczek P, Zhu J, Li YH, Ladjadj M, Leith A. 1996. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116:190-199. http://dx.doi.org/10.1006/jsbi.1996.0030.
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.H.5    Ladjadj, M.6    Leith, A.7
  • 49
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker TS, Cheng RH. 1996. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J Struct Biol 116:120-130. http://dx.doi.org/10.1006/jsbi.1996.0020.
    • (1996) J Struct Biol , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 50
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther RA, Amos LA, Finch JT, Derosier DJ, Klug A. 1970. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature 226:421-425. http://dx.doi.org/10.1038/226421a0.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    Derosier, D.J.4    Klug, A.5
  • 51
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles-the uncommon line
    • Fuller SD, Butcher SJ, Cheng RH, Baker TS. 1996. Three-dimensional reconstruction of icosahedral particles-the uncommon line. J Struct Biol 116:48-55. http://dx.doi.org/10.1006/jsbi.1996.0009.
    • (1996) J Struct Biol , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 53
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W. 1999. EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128:82-97. http://dx.doi.org/10.1006/jsbi.1999.4174.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 54
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions
    • Pintilie GD, Zhang J, Goddard TD, Chiu W, Gossard DC. 2010. Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J Struct Biol 170:427-438. http://dx.doi.org/10.1016/j.jsb.2010.03.007.
    • (2010) J Struct Biol , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 55
    • 73949127977 scopus 로고    scopus 로고
    • The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2)
    • Ko DH, Cunningham AL, Diefenbach RJ. 2010. The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2). J Virol 84:1397-1405. http://dx.doi.org/10.1128/JVI.01721-09.
    • (2010) J Virol , vol.84 , pp. 1397-1405
    • Ko, D.H.1    Cunningham, A.L.2    Diefenbach, R.J.3
  • 56
    • 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, Klupp BG, Granzow H, Osterrieder N, Mettenleiter TC. 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. http://dx.doi.org/10.1128/JVI.76.1.364-378.2002.
    • (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
  • 57
    • 0036333663 scopus 로고    scopus 로고
    • Ultrastructural localization of the herpes simplex virus type 1 U(L)31, U(L)34, and U(S)3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids
    • Reynolds AE, Wills EG, Roller RJ, Ryckman BJ, Baines JD. 2002. Ultrastructural localization of the herpes simplex virus type 1 U(L)31, U(L)34, and U(S)3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. J Virol 76:8939-8952. http://dx.doi.org/10.1128/JVI.76.17.8939-8952.2002.
    • (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
  • 58
    • 32944480977 scopus 로고    scopus 로고
    • The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport
    • Luxton GWG, Lee JIH, Haverlock-Moyns S, Schober JM, Smith GA. 2006. The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport. J Virol 80:201-209. http://dx.doi.org/10.1128/JVI.80.1.201-209.2006.
    • (2006) J Virol , vol.80 , pp. 201-209
    • Luxton, G.W.G.1    Lee, J.I.H.2    Haverlock-Moyns, S.3    Schober, J.M.4    Smith, G.A.5
  • 59
    • 34147100237 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids
    • Bucks MA, O'Regan KJ, Murphy MA, Wills JW, Courtney RJ. 2007. Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids. Virology 361:316-324. http://dx.doi.org/10.1016/j.virol.2006.11.031.
    • (2007) Virology , vol.361 , pp. 316-324
    • Bucks, M.A.1    O'Regan, K.J.2    Murphy, M.A.3    Wills, J.W.4    Courtney, R.J.5
  • 60
    • 84861303783 scopus 로고    scopus 로고
    • The C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virus
    • Schipke J, Pohlmann A, Diestel R, Binz A, Rudolph K, Nagel C-H, Bauerfeind R, Sodeik B. 2012. The C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virus. J Virol 86:3682-3700. http://dx.doi.org/10.1128/JVI.06432-11.
    • (2012) J Virol , vol.86 , pp. 3682-3700
    • Schipke, J.1    Pohlmann, A.2    Diestel, R.3    Binz, A.4    Rudolph, K.5    Nagel, C.-H.6    Bauerfeind, R.7    Sodeik, B.8
  • 61
    • 79955447065 scopus 로고    scopus 로고
    • Nucleocapsid structure, assembly and DNA packaging of herpes simplex virus
    • In Weller SK (ed), Caister Academic Press, Wymondham, United Kingdom
    • Conway JF, Homa FL. 2011. Nucleocapsid structure, assembly and DNA packaging of herpes simplex virus, p 175-193. In Weller SK (ed), Alphaherpesviruses: molecular virology. Caister Academic Press, Wymondham, United Kingdom.
    • (2011) Alphaherpesviruses: molecular virology , pp. 175-193
    • Conway, J.F.1    Homa, F.L.2
  • 62
    • 84863606066 scopus 로고    scopus 로고
    • Nuclear egress of pseudorabies virus capsids is enhanced by a subspecies of the large tegument protein that is lost upon cytoplasmic maturation
    • Leelawong M, Lee JI, Smith GA. 2012. Nuclear egress of pseudorabies virus capsids is enhanced by a subspecies of the large tegument protein that is lost upon cytoplasmic maturation. J Virol 86:6303-6314. http://dx.doi.org/10.1128/JVI.07051-11.
    • (2012) J Virol , vol.86 , pp. 6303-6314
    • Leelawong, M.1    Lee, J.I.2    Smith, G.A.3
  • 63
    • 35448946916 scopus 로고    scopus 로고
    • The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins
    • Coller KE, Lee JIH, Ueda A, Smith GA. 2007. The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. J Virol 81:11790-11797. http://dx.doi.org/10.1128/JVI.01113-07.
    • (2007) J Virol , vol.81 , pp. 11790-11797
    • Coller, K.E.1    Lee, J.I.H.2    Ueda, A.3    Smith, G.A.4
  • 64
    • 67449089967 scopus 로고    scopus 로고
    • Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25
    • Pasdeloup D, Blondel D, Isidro AL, Rixon FJ. 2009. Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. J Virol 83:6610-6623. http://dx.doi.org/10.1128/JVI.02655-08.
    • (2009) J Virol , vol.83 , pp. 6610-6623
    • Pasdeloup, D.1    Blondel, D.2    Isidro, A.L.3    Rixon, F.J.4
  • 65
    • 33144488410 scopus 로고    scopus 로고
    • Structural characterization of the UL25 DNApackaging protein from herpes simplex virus type 1
    • Bowman BR, Welschhans RL, Jayaram H, Stow ND, Preston VG, Quiocho FA. 2006. Structural characterization of the UL25 DNApackaging protein from herpes simplex virus type 1. J Virol 80:2309-2317. http://dx.doi.org/10.1128/JVI.80.5.2309-2317.2006.
    • (2006) J Virol , vol.80 , pp. 2309-2317
    • Bowman, B.R.1    Welschhans, R.L.2    Jayaram, H.3    Stow, N.D.4    Preston, V.G.5    Quiocho, F.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.