메뉴 건너뛰기




Volumn 86, Issue 15, 2012, Pages 8002-8013

Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN B; GLYCOPROTEIN D; GLYCOPROTEIN H; GLYCOPROTEIN L; UNCLASSIFIED DRUG;

EID: 84864390271     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00690-12     Document Type: Article
Times cited : (20)

References (63)
  • 1
    • 78049513712 scopus 로고    scopus 로고
    • Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB
    • Atanasiu DW, Saw T, Cohen GH, Eisenberg RJ. 2010. Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB. J. Virol. 84:12292-12299.
    • (2010) J. Virol. , vol.84 , pp. 12292-12299
    • Atanasiu, D.W.1    Saw, T.2    Cohen, G.H.3    Eisenberg, R.J.4
  • 2
    • 0029813074 scopus 로고    scopus 로고
    • Glycoprotein gH of pseudorabies virus is essential for penetration and propagation in cell culture and in the nervous system of mice
    • Babic N, et al. 1996. Glycoprotein gH of pseudorabies virus is essential for penetration and propagation in cell culture and in the nervous system of mice. J. Gen. Virol. 77:2277-2285.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2277-2285
    • Babic, N.1
  • 3
    • 34548158909 scopus 로고    scopus 로고
    • Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity
    • Backovic M, Jardetzky TS, Longnecker R. 2007. Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity. J. Virol. 81:9596-9600.
    • (2007) J. Virol. , vol.81 , pp. 9596-9600
    • Backovic, M.1    Jardetzky, T.S.2    Longnecker, R.3
  • 5
    • 78651083181 scopus 로고    scopus 로고
    • Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody
    • Backovic M, et al. 2010. Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody. Proc. Natl. Acad. Sci. U. S. A. 107:22635-22640.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22635-22640
    • Backovic, M.1
  • 6
    • 73949091055 scopus 로고    scopus 로고
    • Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8
    • Chesnokova LS, Nishimura SL, Hutt-Fletcher LM. 2009. Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8. Proc. Natl. Acad. Sci. U. S. A. 106:20464-20469.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20464-20469
    • Chesnokova, L.S.1    Nishimura, S.L.2    Hutt-Fletcher, L.M.3
  • 7
    • 0029934516 scopus 로고    scopus 로고
    • The CXXC motif: imperatives for the formation of native disulfide bonds in the cell
    • Chivers PT, Laboissière MC, Raines RT. 1996. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J. 15:2659-2667.
    • (1996) EMBO J , vol.15 , pp. 2659-2667
    • Chivers, P.T.1    Laboissière, M.C.2    Raines, R.T.3
  • 8
    • 77954385082 scopus 로고    scopus 로고
    • Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL
    • Chowdary TK, et al. 2010. Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL. Nat. Struct. Mol. Biol. 17:882-888.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 882-888
    • Chowdary, T.K.1
  • 9
    • 2442425332 scopus 로고    scopus 로고
    • The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entry
    • Cocchi F, et al. 2004. The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entry. Proc. Natl. Acad. Sci. U. S. A. 101:7445-7450.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 7445-7450
    • Cocchi, F.1
  • 10
  • 11
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 12
    • 0023910143 scopus 로고
    • Excretion of non-infectious virus particles lacking glycoprotein H by a temperature-sensitive mutant of herpes simplex virus type 1 evidence that gH is essential for virion infectivity
    • Desai PJ, Schaffer PA, Minson AC. 1988. Excretion of non-infectious virus particles lacking glycoprotein H by a temperature-sensitive mutant of herpes simplex virus type 1: evidence that gH is essential for virion infectivity. J. Gen. Virol. 69:1147-1156.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1147-1156
    • Desai, P.J.1    Schaffer, P.A.2    Minson, A.C.3
  • 13
    • 34547232297 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane
    • Farnsworth A, et al. 2007. Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane. Proc. Natl. Acad. Sci. U. S. A. 104:10187-10192.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10187-10192
    • Farnsworth, A.1
  • 14
    • 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.
    • (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
  • 15
    • 0031054450 scopus 로고    scopus 로고
    • Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H
    • Galdiero M, et al. 1997. Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H. J. Virol. 71:2163-2170.
    • (1997) J. Virol. , vol.71 , pp. 2163-2170
    • Galdiero, M.1
  • 16
    • 34447544169 scopus 로고    scopus 로고
    • Evidence for a role of the membrane-proximal region of herpes simplex virus type 1 glycoprotein H in membrane fusion and virus inhibition
    • Galdiero S, et al. 2007. Evidence for a role of the membrane-proximal region of herpes simplex virus type 1 glycoprotein H in membrane fusion and virus inhibition. Chembiochem 8:885-895.
    • (2007) Chembiochem , vol.8 , pp. 885-895
    • Galdiero, S.1
  • 17
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty RJ, Krummenacher C, Cohen GH, Eisenberg RJ, Spear PG. 1998. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280:1618-1620.
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 18
    • 0344197551 scopus 로고    scopus 로고
    • Potency of an experimental DNA vaccine against Aujeszky's disease in pigs
    • Gerdts V, Jöns Mettenleiter ATC. 1999. Potency of an experimental DNA vaccine against Aujeszky's disease in pigs. Vet. Microbiol. 66:1-13.
    • (1999) Vet. Microbiol. , vol.66 , pp. 1-13
    • Gerdts, V.1    Jöns Mettenleiter, A.T.C.2
  • 19
    • 33746824162 scopus 로고    scopus 로고
    • Hydrophobic a-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion
    • Gianni T, Fato R, Bergamini C, Lenaz G, Campadelli-Fiume G. 2006. Hydrophobic a-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion. J. Virol. 80:8190-8198.
    • (2006) J. Virol. , vol.80 , pp. 8190-8198
    • Gianni, T.1    Fato, R.2    Bergamini, C.3    Lenaz, G.4    Campadelli-Fiume, G.5
  • 20
    • 67650566358 scopus 로고    scopus 로고
    • Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain
    • Gianni T, Amasio M, Campadelli-Fiume G. 2009. Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain. J. Biol. Chem. 284:17370-17382.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17370-17382
    • Gianni, T.1    Amasio, M.2    Campadelli-Fiume, G.3
  • 21
    • 33845723594 scopus 로고    scopus 로고
    • Glycoprotein L disruption reveals two functional forms of the murine gammaherpesvirus 68 glycoprotein H
    • Gillet L, May JS, Colaco S, Stevenson PG. 2007. Glycoprotein L disruption reveals two functional forms of the murine gammaherpesvirus 68 glycoprotein H. J. Virol. 81:280-291.
    • (2007) J. Virol. , vol.81 , pp. 280-291
    • Gillet, L.1    May, J.S.2    Colaco, S.3    Stevenson, P.G.4
  • 22
    • 67449093075 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops
    • Hannah BP, et al. 2009. Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops. J. Virol. 83:6825-6836.
    • (2009) J. Virol. , vol.83 , pp. 6825-6836
    • Hannah, B.P.1
  • 23
    • 33746005904 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein B from herpes simplex virus 1
    • Heldwein EE, et al. 2006. Crystal structure of glycoprotein B from herpes simplex virus 1. Science 313:217-220.
    • (2006) Science , vol.313 , pp. 217-220
    • Heldwein, E.E.1
  • 24
    • 0026026623 scopus 로고
    • Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity
    • Herold BC, WuDunn D, Soltys N, Spear PG. 1991. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol. 65:1090-1098.
    • (1991) J. Virol. , vol.65 , pp. 1090-1098
    • Herold, B.C.1    WuDunn, D.2    Soltys, N.3    Spear, P.G.4
  • 25
    • 0026525542 scopus 로고
    • A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoproteinH(gH) and affects normal folding and surface expression of gH
    • Hutchinson L, et al. 1992. A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoproteinH(gH) and affects normal folding and surface expression of gH. J. Virol. 66:2240-2250.
    • (1992) J. Virol. , vol.66 , pp. 2240-2250
    • Hutchinson, L.1
  • 26
    • 75449089945 scopus 로고    scopus 로고
    • Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry
    • Jackson JO, Lin E, Spear PG, Longnecker R. 2010. Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry. J. Virol. 84:2038-2046.
    • (2010) J. Virol. , vol.84 , pp. 2038-2046
    • Jackson, J.O.1    Lin, E.2    Spear, P.G.3    Longnecker, R.4
  • 27
    • 0035158723 scopus 로고    scopus 로고
    • Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread
    • Johnson DC, Webb M, Wisner TW, Brunetti C. 2001. Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread. J. Virol. 75:821-833.
    • (2001) J. Virol. , vol.75 , pp. 821-833
    • Johnson, D.C.1    Webb, M.2    Wisner, T.W.3    Brunetti, C.4
  • 28
    • 0342711242 scopus 로고    scopus 로고
    • Green fluorescent protein expressed by recombinant pseudorabies virus as an in vivo marker for viral replication
    • Jöns A, Mettenleiter TC. 1997. Green fluorescent protein expressed by recombinant pseudorabies virus as an in vivo marker for viral replication. J. Virol. Methods 66:283-292.
    • (1997) J. Virol. Methods , vol.66 , pp. 283-292
    • Jöns, A.1    Mettenleiter, T.C.2
  • 29
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec J, Loureiro S, Abrescia NG, Stuart DI, Jones IM. 2008. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 15:1024-1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 30
    • 0000525742 scopus 로고
    • A comparison of herpes simplex and pseudorabies viruses
    • Kaplan AS, Vatter AE. 1959. A comparison of herpes simplex and pseudorabies viruses. Virology 7:394-407.
    • (1959) Virology , vol.7 , pp. 394-407
    • Kaplan, A.S.1    Vatter, A.E.2
  • 31
  • 32
    • 33748942530 scopus 로고    scopus 로고
    • Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion
    • Kirschner AN, Omerovic J, Popov B, Longnecker R, Jardetzky TS. 2006. Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion. J. Virol. 80:9444-9454.
    • (2006) J. Virol. , vol.80 , pp. 9444-9454
    • Kirschner, A.N.1    Omerovic, J.2    Popov, B.3    Longnecker, R.4    Jardetzky, T.S.5
  • 33
    • 0030848485 scopus 로고    scopus 로고
    • Pseudorabies virus glycoprotein L is necessary for virus infectivity but dispensable for virion localization of glycoprotein H
    • Klupp BG, Fuchs W, Weiland E, Mettenleiter TC. 1997. Pseudorabies virus glycoprotein L is necessary for virus infectivity but dispensable for virion localization of glycoprotein H. J. Virol. 71:7687-7695.
    • (1997) J. Virol. , vol.71 , pp. 7687-7695
    • Klupp, B.G.1    Fuchs, W.2    Weiland, E.3    Mettenleiter, T.C.4
  • 34
    • 0033015078 scopus 로고    scopus 로고
    • Glycoprotein gL-independent infectivity of pseudorabies virus is mediated by a gD-gH fusion protein
    • Klupp BG, Mettenleiter TC. 1999. Glycoprotein gL-independent infectivity of pseudorabies virus is mediated by a gD-gH fusion protein. J. Virol. 73:3014-3022.
    • (1999) J. Virol. , vol.73 , pp. 3014-3022
    • Klupp, B.G.1    Mettenleiter, T.C.2
  • 35
    • 0033928392 scopus 로고    scopus 로고
    • Pseudorabies virus glycoprotein M inhibits membrane fusion
    • Klupp BG, Nixdorf R, Mettenleiter TC. 2000. Pseudorabies virus glycoprotein M inhibits membrane fusion. J. Virol. 74:6760-6768.
    • (2000) J. Virol. , vol.74 , pp. 6760-6768
    • Klupp, B.G.1    Nixdorf, R.2    Mettenleiter, T.C.3
  • 37
    • 45749112586 scopus 로고    scopus 로고
    • Glycoproteins required for entry are not necessary for egress of pseudorabies virus
    • Klupp BG, Altenschmidt J, Granzow H, Fuchs W, Mettenleiter TC. 2008. Glycoproteins required for entry are not necessary for egress of pseudorabies virus. J. Virol. 82:6299-6309.
    • (2008) J. Virol. , vol.82 , pp. 6299-6309
    • Klupp, B.G.1    Altenschmidt, J.2    Granzow, H.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 38
    • 0344080584 scopus 로고    scopus 로고
    • The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm
    • Kopp M, et al. 2003. The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm. J. Virol. 77:5339-5351.
    • (2003) J. Virol. , vol.77 , pp. 5339-5351
    • Kopp, M.1
  • 39
    • 58149502561 scopus 로고    scopus 로고
    • Effects of simultaneous deletion of pUL11 and glycoprotein M on virion maturation of herpes simplex virus type 1
    • Leege T, et al. 2009. Effects of simultaneous deletion of pUL11 and glycoprotein M on virion maturation of herpes simplex virus type 1. J. Virol. 83:896-907.
    • (2009) J. Virol. , vol.83 , pp. 896-907
    • Leege, T.1
  • 40
    • 84857831938 scopus 로고    scopus 로고
    • Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry
    • Lété C, Machiels B, Stevenson PG, Vanderplasschen A, Gillet L. 2012. Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry. J. Virol. 86:2653-2664.
    • (2012) J. Virol. , vol.86 , pp. 2653-2664
    • Lété, C.1    Machiels, B.2    Stevenson, P.G.3    Vanderplasschen, A.4    Gillet, L.5
  • 41
    • 34548778580 scopus 로고    scopus 로고
    • Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B
    • Lin E, Spear PG. 2007. Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B. Proc. Natl. Acad. Sci. U. S. A. 104:13140-13145.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 13140-13145
    • Lin, E.1    Spear, P.G.2
  • 42
    • 78651074196 scopus 로고    scopus 로고
    • Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex
    • Matsuura H, Kirschner AN, Longnecker R, Jardetzky TS. 2010. Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex. Proc. Natl. Acad. Sci. U. S. A. 107:22641-22646.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22641-22646
    • Matsuura, H.1    Kirschner, A.N.2    Longnecker, R.3    Jardetzky, T.S.4
  • 43
    • 0024411795 scopus 로고
    • Glycoprotein gIII deletion mutants of pseudorabies virus are impaired in virus entry
    • Mettenleiter TC. 1989. Glycoprotein gIII deletion mutants of pseudorabies virus are impaired in virus entry. Virology 171:623-625.
    • (1989) Virology , vol.171 , pp. 623-625
    • Mettenleiter, T.C.1
  • 44
    • 0029967665 scopus 로고    scopus 로고
    • Glycoprotein D-negative pseudorabies virus can spread transneuronally via direct neuron-to-neuron transmission in its natural host, the pig, but not after additional inactivation of gE or gI
    • Mulder W, et al. 1996. Glycoprotein D-negative pseudorabies virus can spread transneuronally via direct neuron-to-neuron transmission in its natural host, the pig, but not after additional inactivation of gE or gI. J. Virol. 70:2191-2200.
    • (1996) J. Virol. , vol.70 , pp. 2191-2200
    • Mulder, W.1
  • 45
    • 0033942487 scopus 로고    scopus 로고
    • Effects of truncation of the carboxy terminus of pseudorabies virus glycoprotein B on infectivity
    • Nixdorf R, Klupp BG, Karger A, Mettenleiter TC. 2000. Effects of truncation of the carboxy terminus of pseudorabies virus glycoprotein B on infectivity. J. Virol. 74:7137-7145.
    • (2000) J. Virol. , vol.74 , pp. 7137-7145
    • Nixdorf, R.1    Klupp, B.G.2    Karger, A.3    Mettenleiter, T.C.4
  • 46
    • 0024390820 scopus 로고
    • Construction of large DNA segments in Escherichia coli
    • O'Connor M, Peifer M, Bender W. 1989. Construction of large DNA segments in Escherichia coli. Science 244:1307-1312.
    • (1989) Science , vol.244 , pp. 1307-1312
    • O'Connor, M.1    Peifer, M.2    Bender, W.3
  • 47
    • 11444255131 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 glycoprotein H binds to alphavbeta3 integrins
    • Parry C, Bell S, Minson T, Browne H. 2005. Herpes simplex virus type 1 glycoprotein H binds to alphavbeta3 integrins. J. Gen. Virol. 86:7-10.
    • (2005) J. Gen. Virol. , vol.86 , pp. 7-10
    • Parry, C.1    Bell, S.2    Minson, T.3    Browne, H.4
  • 48
    • 58249131528 scopus 로고    scopus 로고
    • Protection of chickens against H5N1 highly pathogenic avian influenza virus infection by live vaccination with infectious laryngotracheitis virus recombinants expressing H5 hemagglutinin and N1 neuraminidase
    • Pavlova SP, Veits J, Keil GM, Mettenleiter TC, Fuchs W. 2009. Protection of chickens against H5N1 highly pathogenic avian influenza virus infection by live vaccination with infectious laryngotracheitis virus recombinants expressing H5 hemagglutinin and N1 neuraminidase. Vaccine 27:773-785.
    • (2009) Vaccine , vol.27 , pp. 773-785
    • Pavlova, S.P.1    Veits, J.2    Keil, G.M.3    Mettenleiter, T.C.4    Fuchs, W.5
  • 49
    • 15244353552 scopus 로고    scopus 로고
    • Herpes simplex virus entry mediator associates in infected cells in a complex with viral proteins gD and at least gH
    • Perez-Romero P, Perez A, Capul A, Montgomery R, Fuller AO. 2005. Herpes simplex virus entry mediator associates in infected cells in a complex with viral proteins gD and at least gH. J. Virol. 79:4540-4544.
    • (2005) J. Virol. , vol.79 , pp. 4540-4544
    • Perez-Romero, P.1    Perez, A.2    Capul, A.3    Montgomery, R.4    Fuller, A.O.5
  • 50
    • 0026072796 scopus 로고
    • Pseudorabies virus glycoproteins gII and gp50 are essential for virus penetration
    • Rauh I, Mettenleiter TC. 1991. Pseudorabies virus glycoproteins gII and gp50 are essential for virus penetration. J. Virol. 65:5348-5356.
    • (1991) J. Virol. , vol.65 , pp. 5348-5356
    • Rauh, I.1    Mettenleiter, T.C.2
  • 51
    • 0017837667 scopus 로고
    • The genome of simian virus 40
    • Reddy VB, et al. 1978. The genome of simian virus 40. Science 200:494-502.
    • (1978) Science , vol.200 , pp. 494-502
    • Reddy, V.B.1
  • 52
    • 58149487663 scopus 로고    scopus 로고
    • Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis
    • Reimer JJ, Backovic M, Deshpande CG, Jardetzky T, Longnecker R. 2009. Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis. J. Virol. 83:734-747.
    • (2009) J. Virol. , vol.83 , pp. 734-747
    • Reimer, J.J.1    Backovic, M.2    Deshpande, C.G.3    Jardetzky, T.4    Longnecker, R.5
  • 53
    • 34249950342 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • Knipe DM, Howley PM (ed), 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Roizman B, Knipe DM, Whitney RJ. 2007. Herpes simplex viruses, p 2501-2601. In Knipe DM, Howley PM (ed), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 2501-2601
    • Roizman, B.1    Knipe, D.M.2    Whitney, R.J.3
  • 54
    • 0027502727 scopus 로고
    • A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H
    • Roop C, Hutchinson L, Johnson DC. 1993. A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H. J. Virol. 67:2285-2297.
    • (1993) J. Virol. , vol.67 , pp. 2285-2297
    • Roop, C.1    Hutchinson, L.2    Johnson, D.C.3
  • 55
    • 0034800140 scopus 로고    scopus 로고
    • Glycoprotein D-independent infectivity of pseudorabies virus results in an alteration of in vivo host range and correlates with mutations in glycoproteins B and H
    • Schmidt J, Gerdts V, Beyer J, Klupp BG, Mettenleiter TC. 2001. Glycoprotein D-independent infectivity of pseudorabies virus results in an alteration of in vivo host range and correlates with mutations in glycoproteins B and H. J. Virol. 75:10054-10064.
    • (2001) J. Virol , vol.75 , pp. 10054-10064
    • Schmidt, J.1    Gerdts, V.2    Beyer, J.3    Klupp, B.G.4    Mettenleiter, T.C.5
  • 56
    • 18244427809 scopus 로고    scopus 로고
    • Bovine herpesvirus 1 requires glycoproteinH for infectivity and direct spreading and glycoproteins gH(W450) and gB for glycoprotein D-independent cell-to-cell spread
    • Schröder C, Keil GM. 1999. Bovine herpesvirus 1 requires glycoproteinH for infectivity and direct spreading and glycoproteins gH(W450) and gB for glycoprotein D-independent cell-to-cell spread. J. Gen. Virol. 80:57-61.
    • (1999) J. Gen. Virol. , vol.80 , pp. 57-61
    • Schröder, C.1    Keil, G.M.2
  • 57
    • 0034712723 scopus 로고    scopus 로고
    • A self-recombining bacterial artificial chromosome and its application for analysis of herpesvirus pathogenesis
    • Smith GA, Enquist LW. 2000. A self-recombining bacterial artificial chromosome and its application for analysis of herpesvirus pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 97:4873-4878.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4873-4878
    • Smith, G.A.1    Enquist, L.W.2
  • 58
    • 0141632878 scopus 로고    scopus 로고
    • Herpesvirus entry: an update
    • Spear PG, Longnecker R. 2003. Herpesvirus entry: an update. J. Virol. 77:10179-10185.
    • (2003) J. Virol. , vol.77 , pp. 10179-10185
    • Spear, P.G.1    Longnecker, R.2
  • 59
    • 0023201475 scopus 로고
    • Replication and virulence of pseudorabies virus mutants lacking glycoprotein gX
    • Thomsen DR, Marchioli CC, Yancey RJ, Jr, Post LE. 1987. Replication and virulence of pseudorabies virus mutants lacking glycoprotein gX. J. Virol. 61:229-232.
    • (1987) J. Virol. , vol.61 , pp. 229-232
    • Thomsen, D.R.1    Marchioli, C.C.2    Yancey Jr., R.J.3    Post, L.E.4
  • 60
    • 0031963977 scopus 로고    scopus 로고
    • Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system
    • Turner A, Bruun B, Minson T, Browne H. 1998. Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system. J. Virol. 72: 873-875.
    • (1998) J. Virol. , vol.72 , pp. 873-875
    • Turner, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 61
    • 0025163940 scopus 로고
    • Identification of two genes in the unique short region of pseudorabies virus; comparison with herpes simplex virus and varicella-zoster virus
    • van Zijl M, van der Gulden H, de Wind N, Gielkens A, Berns A. 1990. Identification of two genes in the unique short region of pseudorabies virus; comparison with herpes simplex virus and varicella-zoster virus. J. Gen. Virol. 71:1747-1755.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1747-1755
    • van Zijl, M.1    van der Gulden, H.2    de Wind, N.3    Gielkens, A.4    Berns, A.5
  • 62
    • 81055145260 scopus 로고    scopus 로고
    • Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism
    • Vleck SE, et al. 2011. Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism. Proc. Natl. Acad. Sci. U. S. A. 108:18412-18417.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 18412-18417
    • Vleck, S.E.1
  • 63
    • 0028046624 scopus 로고
    • Mutations in the cytoplasmic tail of herpes simplex virus glycoprotein H suppress cell fusion by a syncytial strain
    • Wilson DW, Davis-Poynter N, Minson AC. 1994. Mutations in the cytoplasmic tail of herpes simplex virus glycoprotein H suppress cell fusion by a syncytial strain. J. Virol. 68:6985-6993.
    • (1994) J. Virol. , vol.68 , pp. 6985-6993
    • Wilson, D.W.1    Davis-Poynter, N.2    Minson, A.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.