메뉴 건너뛰기




Volumn 17, Issue 9, 2016, Pages 965-975

Herpesvirus Entry into Host Cells Mediated by Endosomal Low pH

Author keywords

endocytosis; endosomes; gB; herpes simplex viruses; herpesviruses; low pH; viral entry

Indexed keywords

GLYCOPROTEIN B; HYBRID PROTEIN; VIRUS PROTEIN;

EID: 84981194477     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12408     Document Type: Review
Times cited : (77)

References (111)
  • 2
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison SC. Viral membrane fusion. Nat Struct Mol Biol 2008;15:690–698.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 690-698
    • Harrison, S.C.1
  • 3
    • 84974731299 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • In, Knipe DM, Howley PM, editors., 6th edn., Lippincott Williams & Wilkins, Philadelphia, Pennsylvania
    • Roizman B, Knipe DM, Whitley RJ. Herpes simplex viruses. In: Knipe DM, Howley PM, editors. Fields Virology, 6th edn. Lippincott Williams & Wilkins, Philadelphia, Pennsylvania; 2013, pp. 1823–1897.
    • (2013) Fields Virology , pp. 1823-1897
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 4
    • 84942088799 scopus 로고    scopus 로고
    • Recent insights into the structure, regulation, and function of the V-ATPases
    • Cotter K, Stransky L, McGuire C, Forgac M. Recent insights into the structure, regulation, and function of the V-ATPases. Trends Biochem Sci 2015;40:611–622.
    • (2015) Trends Biochem Sci , vol.40 , pp. 611-622
    • Cotter, K.1    Stransky, L.2    McGuire, C.3    Forgac, M.4
  • 5
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta ES, Ebersold M, Garrett W, Pypaert M, Mellman I. Activation of lysosomal function during dendritic cell maturation. Science 2003;299:1400–1403.
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 6
    • 84883442790 scopus 로고    scopus 로고
    • Regulation of luminal acidification by the V-ATPase
    • Breton S, Brown D. Regulation of luminal acidification by the V-ATPase. Physiology (Bethesda) 2013;28:318–329.
    • (2013) Physiology (Bethesda) , vol.28 , pp. 318-329
    • Breton, S.1    Brown, D.2
  • 7
    • 84878463876 scopus 로고    scopus 로고
    • Multiscale perspectives of virus entry via endocytosis
    • Barrow E, Nicola AV, Liu J. Multiscale perspectives of virus entry via endocytosis. Virol J 2013;10:177.
    • (2013) Virol J , vol.10 , pp. 177
    • Barrow, E.1    Nicola, A.V.2    Liu, J.3
  • 8
    • 0018853517 scopus 로고
    • On the entry of Semliki forest virus into BHK-21 cells
    • Helenius A, Kartenbeck J, Simons K, Fries E. On the entry of Semliki forest virus into BHK-21 cells. J Cell Biol 1980;84:404–420.
    • (1980) J Cell Biol , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3    Fries, E.4
  • 9
    • 0021040946 scopus 로고
    • Lysosomes revisited
    • de Duve C. Lysosomes revisited. Eur J Biochem 1983;137:391–397.
    • (1983) Eur J Biochem , vol.137 , pp. 391-397
    • de Duve, C.1
  • 10
    • 0021331201 scopus 로고
    • Metabolic products of microorganisms. 224. Bafilomycins, a new group of macrolide antibiotics. Production, isolation, chemical structure and biological activity
    • Werner G, Hagenmaier H, Drautz H, Baumgartner A, Zahner H. Metabolic products of microorganisms. 224. Bafilomycins, a new group of macrolide antibiotics. Production, isolation, chemical structure and biological activity. J Antibiot (Tokyo) 1984;37:110–117.
    • (1984) J Antibiot (Tokyo) , vol.37 , pp. 110-117
    • Werner, G.1    Hagenmaier, H.2    Drautz, H.3    Baumgartner, A.4    Zahner, H.5
  • 11
    • 0011913143 scopus 로고
    • Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman EJ, Siebers A, Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci USA 1988;85:7972–7976.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 12
    • 0027978351 scopus 로고
    • Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase
    • Zhang J, Feng Y, Forgac M. Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase. J Biol Chem 1994;269:23518–23523.
    • (1994) J Biol Chem , vol.269 , pp. 23518-23523
    • Zhang, J.1    Feng, Y.2    Forgac, M.3
  • 14
    • 84857369888 scopus 로고    scopus 로고
    • Viral and cellular contributions to herpes simplex virus entry into the cell
    • Campadelli-Fiume G, Menotti L, Avitabile E, Gianni T. Viral and cellular contributions to herpes simplex virus entry into the cell. Curr Opin Virol 2012;2:28–36.
    • (2012) Curr Opin Virol , vol.2 , pp. 28-36
    • Campadelli-Fiume, G.1    Menotti, L.2    Avitabile, E.3    Gianni, T.4
  • 15
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: a structural view of the herpesvirus entry machinery
    • Connolly SA, Jackson JO, Jardetzky TS, Longnecker R. Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol 2011;9:369–381.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 16
    • 0034883314 scopus 로고    scopus 로고
    • Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry
    • Shukla D, Spear PG. Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry. J Clin Invest 2001;108:503–510.
    • (2001) J Clin Invest , vol.108 , pp. 503-510
    • Shukla, D.1    Spear, P.G.2
  • 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. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 1998;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
    • 0031797729 scopus 로고    scopus 로고
    • The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells
    • Cocchi F, Menotti L, Mirandola P, Lopez M, Campadelli-Fiume G. The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells. J Virol 1998;72:9992–10002.
    • (1998) J Virol , vol.72 , pp. 9992-10002
    • Cocchi, F.1    Menotti, L.2    Mirandola, P.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 19
    • 0033519211 scopus 로고    scopus 로고
    • Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein
    • Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y. Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein. J Cell Biol 1999;145:539–549.
    • (1999) J Cell Biol , vol.145 , pp. 539-549
    • Takahashi, K.1    Nakanishi, H.2    Miyahara, M.3    Mandai, K.4    Satoh, K.5    Satoh, A.6    Nishioka, H.7    Aoki, J.8    Nomoto, A.9    Mizoguchi, A.10    Takai, Y.11
  • 20
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • Montgomery RI, Warner MS, Lum BJ, Spear PG. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 1996;87:427–436.
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 21
    • 0023705653 scopus 로고
    • Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion
    • Cai WH, Gu B, Person S. Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion. J Virol 1988;62:2596–2604.
    • (1988) J Virol , vol.62 , pp. 2596-2604
    • Cai, W.H.1    Gu, B.2    Person, S.3
  • 22
    • 0023906081 scopus 로고
    • A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells
    • Ligas MW, Johnson DC. A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells. J Virol 1988;62:1486–1494.
    • (1988) J Virol , vol.62 , pp. 1486-1494
    • Ligas, M.W.1    Johnson, D.C.2
  • 23
    • 0026556674 scopus 로고
    • Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted
    • Forrester A, Farrell H, Wilkinson G, Kaye J, Davis-Poynter N, Minson T. Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted. J Virol 1992;66:341–348.
    • (1992) J Virol , vol.66 , pp. 341-348
    • Forrester, A.1    Farrell, H.2    Wilkinson, G.3    Kaye, J.4    Davis-Poynter, N.5    Minson, T.6
  • 24
    • 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. A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H. J Virol 1993;67:2285–2297.
    • (1993) J Virol , vol.67 , pp. 2285-2297
    • Roop, C.1    Hutchinson, L.2    Johnson, D.C.3
  • 25
    • 3142719117 scopus 로고    scopus 로고
    • Cellular and viral requirements for rapid endocytic entry of herpes simplex virus
    • Nicola AV, Straus SE. Cellular and viral requirements for rapid endocytic entry of herpes simplex virus. J Virol 2004;78:7508–7517.
    • (2004) J Virol , vol.78 , pp. 7508-7517
    • Nicola, A.V.1    Straus, S.E.2
  • 26
    • 0028089018 scopus 로고
    • Herpes simplex virus glycoproteins E and I facilitate cell-to-cell spread in vivo and across junctions of cultured cells
    • Dingwell KS, Brunetti CR, Hendricks RL, Tang Q, Tang M, Rainbow AJ, Johnson DC. Herpes simplex virus glycoproteins E and I facilitate cell-to-cell spread in vivo and across junctions of cultured cells. J Virol 1994;68:834–845.
    • (1994) J Virol , vol.68 , pp. 834-845
    • Dingwell, K.S.1    Brunetti, C.R.2    Hendricks, R.L.3    Tang, Q.4    Tang, M.5    Rainbow, A.J.6    Johnson, D.C.7
  • 27
    • 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. 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 1998;72:873–875.
    • (1998) J Virol , vol.72 , pp. 873-875
    • Turner, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 28
    • 0014281593 scopus 로고
    • Electron microscopy of herpes simplex virus. I. Entry
    • Morgan C, Rose HM, Mednis B. Electron microscopy of herpes simplex virus. I. Entry. J Virol 1968;2:507–516.
    • (1968) J Virol , vol.2 , pp. 507-516
    • Morgan, C.1    Rose, H.M.2    Mednis, B.3
  • 29
    • 0016293618 scopus 로고
    • Herpes simplex virus and human cytomegalovirus replication in WI-38 cells. II. An ultrastructural study of viral penetration
    • Smith JD, de Harven E. Herpes simplex virus and human cytomegalovirus replication in WI-38 cells. II. An ultrastructural study of viral penetration. J Virol 1974;14:945–956.
    • (1974) J Virol , vol.14 , pp. 945-956
    • Smith, J.D.1    de Harven, E.2
  • 30
    • 0023388477 scopus 로고
    • Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface
    • Fuller AO, Spear PG. Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface. Proc Natl Acad Sci USA 1987;84:5454–5458.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5454-5458
    • Fuller, A.O.1    Spear, P.G.2
  • 31
    • 0023190313 scopus 로고
    • The mode of entry of herpes simplex virus type 1 into Vero cells
    • Koyama AH, Uchida T. The mode of entry of herpes simplex virus type 1 into Vero cells. Microbiol Immunol 1987;31:123–130.
    • (1987) Microbiol Immunol , vol.31 , pp. 123-130
    • Koyama, A.H.1    Uchida, T.2
  • 32
    • 0026100907 scopus 로고
    • Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway
    • Wittels M, Spear PG. Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway. Virus Res 1991;18:271–290.
    • (1991) Virus Res , vol.18 , pp. 271-290
    • Wittels, M.1    Spear, P.G.2
  • 33
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik B, Ebersold MW, Helenius A. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J Cell Biol 1997;136:1007–1021.
    • (1997) J Cell Biol , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 34
    • 0037404499 scopus 로고    scopus 로고
    • Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells
    • Nicola AV, McEvoy AM, Straus SE. Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J Virol 2003;77:5324–5332.
    • (2003) J Virol , vol.77 , pp. 5324-5332
    • Nicola, A.V.1    McEvoy, A.M.2    Straus, S.E.3
  • 35
    • 0023772685 scopus 로고
    • Herpes simplex virus infection of the human sensory neuron. An electron microscopy study
    • Lycke E, Hamark B, Johansson M, Krotochwil A, Lycke J, Svennerholm B. Herpes simplex virus infection of the human sensory neuron. An electron microscopy study. Arch Virol 1988;101:87–104.
    • (1988) Arch Virol , vol.101 , pp. 87-104
    • Lycke, E.1    Hamark, B.2    Johansson, M.3    Krotochwil, A.4    Lycke, J.5    Svennerholm, B.6
  • 36
    • 19944423114 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway
    • Nicola AV, Hou J, Major EO, Straus SE. Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway. J Virol 2005;79:7609–7616.
    • (2005) J Virol , vol.79 , pp. 7609-7616
    • Nicola, A.V.1    Hou, J.2    Major, E.O.3    Straus, S.E.4
  • 37
    • 48749114826 scopus 로고    scopus 로고
    • Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry
    • Maurer UE, Sodeik B, Grunewald K. Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry. Proc Natl Acad Sci USA 2008;105:10559–10564.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10559-10564
    • Maurer, U.E.1    Sodeik, B.2    Grunewald, K.3
  • 38
    • 80054000888 scopus 로고    scopus 로고
    • Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin- and cholesterol-dependent
    • Rahn E, Petermann P, Hsu MJ, Rixon FJ, Knebel-Morsdorf D. Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin- and cholesterol-dependent. PLoS One 2011;6:e25464.
    • (2011) PLoS One , vol.6
    • Rahn, E.1    Petermann, P.2    Hsu, M.J.3    Rixon, F.J.4    Knebel-Morsdorf, D.5
  • 39
    • 0038082194 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) infection of human fibroblast cells occurs through endocytosis
    • Akula SM, Naranatt PP, Walia NS, Wang FZ, Fegley B, Chandran B. Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) infection of human fibroblast cells occurs through endocytosis. J Virol 2003;77:7978–7990.
    • (2003) J Virol , vol.77 , pp. 7978-7990
    • Akula, S.M.1    Naranatt, P.P.2    Walia, N.S.3    Wang, F.Z.4    Fegley, B.5    Chandran, B.6
  • 40
    • 30344435010 scopus 로고    scopus 로고
    • Human cytomegalovirus entry into epithelial and endothelial cells depends on genes UL128 to UL150 and occurs by endocytosis and low-pH fusion
    • Ryckman BJ, Jarvis MA, Drummond DD, Nelson JA, Johnson DC. Human cytomegalovirus entry into epithelial and endothelial cells depends on genes UL128 to UL150 and occurs by endocytosis and low-pH fusion. J Virol 2006;80:710–722.
    • (2006) J Virol , vol.80 , pp. 710-722
    • Ryckman, B.J.1    Jarvis, M.A.2    Drummond, D.D.3    Nelson, J.A.4    Johnson, D.C.5
  • 41
    • 33750298267 scopus 로고    scopus 로고
    • Postentry events are responsible for restriction of productive varicella-zoster virus infection in Chinese hamster ovary cells
    • Finnen RL, Mizokami KR, Banfield BW, Cai GY, Simpson SA, Pizer LI, Levin MJ. Postentry events are responsible for restriction of productive varicella-zoster virus infection in Chinese hamster ovary cells. J Virol 2006;80:10325–10334.
    • (2006) J Virol , vol.80 , pp. 10325-10334
    • Finnen, R.L.1    Mizokami, K.R.2    Banfield, B.W.3    Cai, G.Y.4    Simpson, S.A.5    Pizer, L.I.6    Levin, M.J.7
  • 42
    • 35148822681 scopus 로고    scopus 로고
    • Equine herpesvirus 1 enters cells by two different pathways, and infection requires the activation of the cellular kinase ROCK1
    • Frampton AR Jr, Stolz DB, Uchida H, Goins WF, Cohen JB, Glorioso JC. Equine herpesvirus 1 enters cells by two different pathways, and infection requires the activation of the cellular kinase ROCK1. J Virol 2007;81:10879–10889.
    • (2007) J Virol , vol.81 , pp. 10879-10889
    • Frampton, A.R.1    Stolz, D.B.2    Uchida, H.3    Goins, W.F.4    Cohen, J.B.5    Glorioso, J.C.6
  • 43
    • 7644240967 scopus 로고    scopus 로고
    • Entry of herpes simplex virus mediated by chimeric forms of nectin1 retargeted to endosomes or to lipid rafts occurs through acidic endosomes
    • Gianni T, Campadelli-Fiume G, Menotti L. Entry of herpes simplex virus mediated by chimeric forms of nectin1 retargeted to endosomes or to lipid rafts occurs through acidic endosomes. J Virol 2004;78:12268–12276.
    • (2004) J Virol , vol.78 , pp. 12268-12276
    • Gianni, T.1    Campadelli-Fiume, G.2    Menotti, L.3
  • 45
    • 33846520001 scopus 로고    scopus 로고
    • Nectin-2-mediated entry of a syncytial strain of herpes simplex virus via pH-independent fusion with the plasma membrane of Chinese hamster ovary cells
    • Delboy MG, Patterson JL, Hollander AM, Nicola AV. Nectin-2-mediated entry of a syncytial strain of herpes simplex virus via pH-independent fusion with the plasma membrane of Chinese hamster ovary cells. Virol J 2006;3:105.
    • (2006) Virol J , vol.3 , pp. 105
    • Delboy, M.G.1    Patterson, J.L.2    Hollander, A.M.3    Nicola, A.V.4
  • 46
    • 53849128530 scopus 로고    scopus 로고
    • Role for nectin-1 in herpes simplex virus 1 entry and spread in human retinal pigment epithelial cells
    • Tiwari V, Oh MJ, Kovacs M, Shukla SY, Valyi-Nagy T, Shukla D. Role for nectin-1 in herpes simplex virus 1 entry and spread in human retinal pigment epithelial cells. FEBS J 2008;275:5272–5285.
    • (2008) FEBS J , vol.275 , pp. 5272-5285
    • Tiwari, V.1    Oh, M.J.2    Kovacs, M.3    Shukla, S.Y.4    Valyi-Nagy, T.5    Shukla, D.6
  • 47
    • 78650773037 scopus 로고    scopus 로고
    • HSV-1 infection of human corneal epithelial cells: receptor-mediated entry and trends of re-infection
    • Shah A, Farooq AV, Tiwari V, Kim MJ, Shukla D. HSV-1 infection of human corneal epithelial cells: receptor-mediated entry and trends of re-infection. Mol Vis 2010;16:2476–2486.
    • (2010) Mol Vis , vol.16 , pp. 2476-2486
    • Shah, A.1    Farooq, A.V.2    Tiwari, V.3    Kim, M.J.4    Shukla, D.5
  • 49
    • 56349157011 scopus 로고    scopus 로고
    • Structure-function analysis of herpes simplex virus glycoprotein B with fusion-from-without activity
    • Roller DG, Dollery SJ, Doyle JL, Nicola AV. Structure-function analysis of herpes simplex virus glycoprotein B with fusion-from-without activity. Virology 2008;382:207–216.
    • (2008) Virology , vol.382 , pp. 207-216
    • Roller, D.G.1    Dollery, S.J.2    Doyle, J.L.3    Nicola, A.V.4
  • 50
    • 78650663541 scopus 로고    scopus 로고
    • {alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2
    • Gianni T, Gatta V, Campadelli-Fiume G. {alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2. Proc Natl Acad Sci USA 2010;107:22260–22265.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 22260-22265
    • Gianni, T.1    Gatta, V.2    Campadelli-Fiume, G.3
  • 51
    • 70349795535 scopus 로고    scopus 로고
    • Infectious entry of equine herpesvirus-1 into host cells through different endocytic pathways
    • Hasebe R, Sasaki M, Sawa H, Wada R, Umemura T, Kimura T. Infectious entry of equine herpesvirus-1 into host cells through different endocytic pathways. Virology 2009;393:198–209.
    • (2009) Virology , vol.393 , pp. 198-209
    • Hasebe, R.1    Sasaki, M.2    Sawa, H.3    Wada, R.4    Umemura, T.5    Kimura, T.6
  • 52
    • 38049107480 scopus 로고    scopus 로고
    • Human cytomegalovirus uses two distinct pathways to enter retinal pigmented epithelial cells
    • Wang D, Yu QC, Schroer J, Murphy E, Shenk T. Human cytomegalovirus uses two distinct pathways to enter retinal pigmented epithelial cells. Proc Natl Acad Sci USA 2007;104:20037–20042.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20037-20042
    • Wang, D.1    Yu, Q.C.2    Schroer, J.3    Murphy, E.4    Shenk, T.5
  • 54
    • 0038758763 scopus 로고    scopus 로고
    • Characterization of entry mechanisms of human herpesvirus 8 by using an Rta-dependent reporter cell line
    • Inoue N, Winter J, Lal RB, Offermann MK, Koyano S. Characterization of entry mechanisms of human herpesvirus 8 by using an Rta-dependent reporter cell line. J Virol 2003;77:8147–8152.
    • (2003) J Virol , vol.77 , pp. 8147-8152
    • Inoue, N.1    Winter, J.2    Lal, R.B.3    Offermann, M.K.4    Koyano, S.5
  • 55
    • 65349165676 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells
    • Raghu H, Sharma-Walia N, Veettil MV, Sadagopan S, Chandran B. Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells. J Virol 2009;83:4895–4911.
    • (2009) J Virol , vol.83 , pp. 4895-4911
    • Raghu, H.1    Sharma-Walia, N.2    Veettil, M.V.3    Sadagopan, S.4    Chandran, B.5
  • 56
    • 70049116403 scopus 로고    scopus 로고
    • Actin dynamics regulate multiple endosomal steps during Kaposi's sarcoma-associated herpesvirus entry and trafficking in endothelial cells
    • Greene W, Gao SJ. Actin dynamics regulate multiple endosomal steps during Kaposi's sarcoma-associated herpesvirus entry and trafficking in endothelial cells. PLoS Pathog 2009;5:e1000512.
    • (2009) PLoS Pathog , vol.5
    • Greene, W.1    Gao, S.J.2
  • 57
    • 77956181131 scopus 로고    scopus 로고
    • Characterization of entry and infection of monocytic THP-1 cells by Kaposi's sarcoma associated herpesvirus (KSHV): role of heparan sulfate, DC-SIGN, integrins and signaling
    • Kerur N, Veettil MV, Sharma-Walia N, Sadagopan S, Bottero V, Paul AG, Chandran B. Characterization of entry and infection of monocytic THP-1 cells by Kaposi's sarcoma associated herpesvirus (KSHV): role of heparan sulfate, DC-SIGN, integrins and signaling. Virology 2010;406:103–116.
    • (2010) Virology , vol.406 , pp. 103-116
    • Kerur, N.1    Veettil, M.V.2    Sharma-Walia, N.3    Sadagopan, S.4    Bottero, V.5    Paul, A.G.6    Chandran, B.7
  • 58
    • 78049495027 scopus 로고    scopus 로고
    • Rhesus rhadinovirus infection of rhesus fibroblasts occurs through clathrin-mediated endocytosis
    • Zhang W, Zhou F, Greene W, Gao SJ. Rhesus rhadinovirus infection of rhesus fibroblasts occurs through clathrin-mediated endocytosis. J Virol 2010;84:11709–11717.
    • (2010) J Virol , vol.84 , pp. 11709-11717
    • Zhang, W.1    Zhou, F.2    Greene, W.3    Gao, S.J.4
  • 59
    • 45949085102 scopus 로고    scopus 로고
    • Glycoprotein B switches conformation during murid herpesvirus 4 entry
    • Gillet L, Colaco S, Stevenson PG. Glycoprotein B switches conformation during murid herpesvirus 4 entry. J Gen Virol 2008;89:1352–1363.
    • (2008) J Gen Virol , vol.89 , pp. 1352-1363
    • Gillet, L.1    Colaco, S.2    Stevenson, P.G.3
  • 60
    • 77549086793 scopus 로고    scopus 로고
    • Low pH-induced conformational change in herpes simplex virus glycoprotein B
    • Dollery SJ, Delboy MG, Nicola AV. Low pH-induced conformational change in herpes simplex virus glycoprotein B. J Virol 2010;84:3759–3766.
    • (2010) J Virol , vol.84 , pp. 3759-3766
    • Dollery, S.J.1    Delboy, M.G.2    Nicola, A.V.3
  • 61
    • 84960493876 scopus 로고    scopus 로고
    • Polyethylene glycol-mediated fusion of herpes simplex type 1 virions with the plasma membrane of cells that support endocytic entry
    • Walker EB, Pritchard SM, Cunha CW, Aguilar HC, Nicola AV. Polyethylene glycol-mediated fusion of herpes simplex type 1 virions with the plasma membrane of cells that support endocytic entry. Virol J 2015;12:190.
    • (2015) Virol J , vol.12 , pp. 190
    • Walker, E.B.1    Pritchard, S.M.2    Cunha, C.W.3    Aguilar, H.C.4    Nicola, A.V.5
  • 62
    • 0020042010 scopus 로고
    • Inhibition of Semliki forest virus penetration by lysosomotropic weak bases
    • Helenius A, Marsh M, White J. Inhibition of Semliki forest virus penetration by lysosomotropic weak bases. J Gen Virol 1982;5847–61.
    • (1982) J Gen Virol , vol.58 , pp. 47-61
    • Helenius, A.1    Marsh, M.2    White, J.3
  • 64
    • 0031026138 scopus 로고    scopus 로고
    • SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface
    • Marsh M, Bron R. SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface. J Cell Sci 1997;110:95–103.
    • (1997) J Cell Sci , vol.110 , pp. 95-103
    • Marsh, M.1    Bron, R.2
  • 65
    • 77549083960 scopus 로고    scopus 로고
    • Role of the UL45 protein in herpes simplex virus entry via low pH-dependent endocytosis and its relationship to the conformation and function of glycoprotein B
    • Dollery SJ, Lane KD, Delboy MG, Roller DG, Nicola AV. Role of the UL45 protein in herpes simplex virus entry via low pH-dependent endocytosis and its relationship to the conformation and function of glycoprotein B. Virus Res 2010;149:115–118.
    • (2010) Virus Res , vol.149 , pp. 115-118
    • Dollery, S.J.1    Lane, K.D.2    Delboy, M.G.3    Roller, D.G.4    Nicola, A.V.5
  • 67
    • 84874704500 scopus 로고    scopus 로고
    • The amino terminus of herpes simplex virus 1 glycoprotein K is required for virion entry via the paired immunoglobulin-like type-2 receptor alpha
    • Chowdhury S, Chouljenko VN, Naderi M, Kousoulas KG. The amino terminus of herpes simplex virus 1 glycoprotein K is required for virion entry via the paired immunoglobulin-like type-2 receptor alpha. J Virol 2013;87:3305–3313.
    • (2013) J Virol , vol.87 , pp. 3305-3313
    • Chowdhury, S.1    Chouljenko, V.N.2    Naderi, M.3    Kousoulas, K.G.4
  • 68
    • 84908378560 scopus 로고    scopus 로고
    • Herpes simplex virus internalization into epithelial cells requires Na+/H+ exchangers and p21-activated kinases but neither clathrin- nor caveolin-mediated endocytosis
    • Devadas D, Koithan T, Diestel R, Prank U, Sodeik B, Dohner K. Herpes simplex virus internalization into epithelial cells requires Na+/H+ exchangers and p21-activated kinases but neither clathrin- nor caveolin-mediated endocytosis. J Virol 2014;88:13378–13395.
    • (2014) J Virol , vol.88 , pp. 13378-13395
    • Devadas, D.1    Koithan, T.2    Diestel, R.3    Prank, U.4    Sodeik, B.5    Dohner, K.6
  • 69
    • 0021325510 scopus 로고
    • Early events in the infection of human B lymphocytes by Epstein-Barr virus: the internalization process
    • Nemerow GR, Cooper NR. Early events in the infection of human B lymphocytes by Epstein-Barr virus: the internalization process. Virology 1984;132:186–198.
    • (1984) Virology , vol.132 , pp. 186-198
    • Nemerow, G.R.1    Cooper, N.R.2
  • 70
    • 0026696312 scopus 로고
    • Epstein-Barr virus enters B cells and epithelial cells by different routes
    • Miller N, Hutt-Fletcher LM. Epstein-Barr virus enters B cells and epithelial cells by different routes. J Virol 1992;66:3409–3414.
    • (1992) J Virol , vol.66 , pp. 3409-3414
    • Miller, N.1    Hutt-Fletcher, L.M.2
  • 71
    • 0026787140 scopus 로고
    • Human cytomegalovirus penetrates host cells by pH-independent fusion at the cell surface
    • Compton T, Nepomuceno RR, Nowlin DM. Human cytomegalovirus penetrates host cells by pH-independent fusion at the cell surface. Virology 1992;191:387–395.
    • (1992) Virology , vol.191 , pp. 387-395
    • Compton, T.1    Nepomuceno, R.R.2    Nowlin, D.M.3
  • 72
    • 84866893032 scopus 로고    scopus 로고
    • PDGF receptor-alpha does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway
    • Vanarsdall AL, Wisner TW, Lei H, Kazlauskas A, Johnson DC. PDGF receptor-alpha does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway. PLoS Pathog 2012;8:e1002905.
    • (2012) PLoS Pathog , vol.8
    • Vanarsdall, A.L.1    Wisner, T.W.2    Lei, H.3    Kazlauskas, A.4    Johnson, D.C.5
  • 73
    • 84859527579 scopus 로고    scopus 로고
    • Human cytomegalovirus entry into dendritic cells occurs via a macropinocytosis-like pathway in a pH-independent and cholesterol-dependent manner
    • Haspot F, Lavault A, Sinzger C, Laib Sampaio K, Stierhof YD, Pilet P, Bressolette-Bodin C, Halary F. Human cytomegalovirus entry into dendritic cells occurs via a macropinocytosis-like pathway in a pH-independent and cholesterol-dependent manner. PLoS One 2012;7:e34795.
    • (2012) PLoS One , vol.7
    • Haspot, F.1    Lavault, A.2    Sinzger, C.3    Laib Sampaio, K.4    Stierhof, Y.D.5    Pilet, P.6    Bressolette-Bodin, C.7    Halary, F.8
  • 74
    • 84958999568 scopus 로고    scopus 로고
    • HCMV induces macropinocytosis for host cell entry in fibroblasts
    • Hetzenecker S, Helenius A, Krzyzaniak MA. HCMV induces macropinocytosis for host cell entry in fibroblasts. Traffic 2016;17:351–368.
    • (2016) Traffic , vol.17 , pp. 351-368
    • Hetzenecker, S.1    Helenius, A.2    Krzyzaniak, M.A.3
  • 75
    • 18744382150 scopus 로고    scopus 로고
    • Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1
    • Milne RS, Nicola AV, Whitbeck JC, Eisenberg RJ, Cohen GH. Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1. J Virol 2005;79:6655–6663.
    • (2005) J Virol , vol.79 , pp. 6655-6663
    • Milne, R.S.1    Nicola, A.V.2    Whitbeck, J.C.3    Eisenberg, R.J.4    Cohen, G.H.5
  • 76
    • 77950489408 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infection
    • Gianni T, Cerretani A, Dubois R, Salvioli S, Blystone SS, Rey F, Campadelli-Fiume G. Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infection. J Virol 2010;84:4013–4025.
    • (2010) J Virol , vol.84 , pp. 4013-4025
    • Gianni, T.1    Cerretani, A.2    Dubois, R.3    Salvioli, S.4    Blystone, S.S.5    Rey, F.6    Campadelli-Fiume, G.7
  • 77
    • 78649512396 scopus 로고    scopus 로고
    • Reversible conformational change in herpes simplex virus glycoprotein B with fusion-from-without activity is triggered by mildly acidic pH
    • Siekavizza-Robles CR, Dollery SJ, Nicola AV. Reversible conformational change in herpes simplex virus glycoprotein B with fusion-from-without activity is triggered by mildly acidic pH. Virol J 2010;7:352.
    • (2010) Virol J , vol.7 , pp. 352
    • Siekavizza-Robles, C.R.1    Dollery, S.J.2    Nicola, A.V.3
  • 79
    • 80053964873 scopus 로고    scopus 로고
    • Low-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity
    • Dollery SJ, Wright CC, Johnson DC, Nicola AV. Low-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity. J Virol 2011;85:9964–9973.
    • (2011) J Virol , vol.85 , pp. 9964-9973
    • Dollery, S.J.1    Wright, C.C.2    Johnson, D.C.3    Nicola, A.V.4
  • 80
    • 0023718635 scopus 로고
    • Antibody-resistant mutations in cross-reactive and type-specific epitopes of herpes simplex virus 1 glycoprotein B map in separate domains
    • Kousoulas KG, Huo B, Pereira L. Antibody-resistant mutations in cross-reactive and type-specific epitopes of herpes simplex virus 1 glycoprotein B map in separate domains. Virology 1988;166:423–431.
    • (1988) Virology , vol.166 , pp. 423-431
    • Kousoulas, K.G.1    Huo, B.2    Pereira, L.3
  • 82
    • 0024458284 scopus 로고
    • Domain structure of herpes simplex virus 1 glycoprotein B: neutralizing epitopes map in regions of continuous and discontinuous residues
    • Pereira L, Ali M, Kousoulas K, Huo B, Banks T. Domain structure of herpes simplex virus 1 glycoprotein B: neutralizing epitopes map in regions of continuous and discontinuous residues. Virology 1989;172:11–24.
    • (1989) Virology , vol.172 , pp. 11-24
    • Pereira, L.1    Ali, M.2    Kousoulas, K.3    Huo, B.4    Banks, T.5
  • 85
    • 78649413011 scopus 로고    scopus 로고
    • Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1
    • Stampfer SD, Lou H, Cohen GH, Eisenberg RJ, Heldwein EE. Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1. J Virol 2010;84:12924–12933.
    • (2010) J Virol , vol.84 , pp. 12924-12933
    • Stampfer, S.D.1    Lou, H.2    Cohen, G.H.3    Eisenberg, R.J.4    Heldwein, E.E.5
  • 86
    • 0022348304 scopus 로고
    • Fusion from without induced by herpes simplex virus type 1
    • Falke D, Knoblich A, Muller S. Fusion from without induced by herpes simplex virus type 1. Intervirology 1985;24:211–219.
    • (1985) Intervirology , vol.24 , pp. 211-219
    • Falke, D.1    Knoblich, A.2    Muller, S.3
  • 87
    • 0031555641 scopus 로고    scopus 로고
    • Identification of the fusion-from-without determinants of herpes simplex virus type 1 glycoprotein B
    • Saharkhiz-Langroodi A, Holland TC. Identification of the fusion-from-without determinants of herpes simplex virus type 1 glycoprotein B. Virology 1997;227:153–159.
    • (1997) Virology , vol.227 , pp. 153-159
    • Saharkhiz-Langroodi, A.1    Holland, T.C.2
  • 88
    • 0033895221 scopus 로고    scopus 로고
    • Characterization of cell-cell fusion mediated by herpes simplex virus 2 glycoproteins gB, gD, gH and gL in transfected cells
    • Muggeridge MI. Characterization of cell-cell fusion mediated by herpes simplex virus 2 glycoproteins gB, gD, gH and gL in transfected cells. J Gen Virol 2000;81(Pt 8):2017–2027.
    • (2000) J Gen Virol , vol.81 , pp. 2017-2027
    • Muggeridge, M.I.1
  • 89
    • 84864015840 scopus 로고    scopus 로고
    • Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH
    • Muggeridge MI. Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH. J Virol 2012;86:6444–6456.
    • (2012) J Virol , vol.86 , pp. 6444-6456
    • Muggeridge, M.I.1
  • 91
    • 84872166777 scopus 로고    scopus 로고
    • The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes
    • Shelly SS, Cairns TM, Whitbeck JC, Lou H, Krummenacher C, Cohen GH, Eisenberg RJ. The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes. MBio 2012;3:1–11.
    • (2012) MBio , vol.3 , pp. 1-11
    • Shelly, S.S.1    Cairns, T.M.2    Whitbeck, J.C.3    Lou, H.4    Krummenacher, C.5    Cohen, G.H.6    Eisenberg, R.J.7
  • 93
    • 33645791673 scopus 로고    scopus 로고
    • Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEM
    • Whitbeck JC, Zuo Y, Milne RS, Cohen GH, Eisenberg RJ. Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEM. J Virol 2006;80:3773–3780.
    • (2006) J Virol , vol.80 , pp. 3773-3780
    • Whitbeck, J.C.1    Zuo, Y.2    Milne, R.S.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 94
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein g
    • Roche S, Rey FA, Gaudin Y, Bressanelli S. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein g. Science 2007;315:843–848.
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 98
  • 99
    • 0023550869 scopus 로고
    • Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers
    • Doms RW, Keller DS, Helenius A, Balch WE. Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J Cell Biol 1987;105:1957–1969.
    • (1987) J Cell Biol , vol.105 , pp. 1957-1969
    • Doms, R.W.1    Keller, D.S.2    Helenius, A.3    Balch, W.E.4
  • 100
    • 33747065188 scopus 로고    scopus 로고
    • Mapping the conformational epitope of a neutralizing antibody (AcV1) directed against the AcMNPV GP64 protein
    • Zhou J, Blissard GW. Mapping the conformational epitope of a neutralizing antibody (AcV1) directed against the AcMNPV GP64 protein. Virology 2006;352:427–437.
    • (2006) Virology , vol.352 , pp. 427-437
    • Zhou, J.1    Blissard, G.W.2
  • 101
    • 0026018237 scopus 로고
    • Reversible conformational changes and fusion activity of rabies virus glycoprotein
    • Gaudin Y, Tuffereau C, Segretain D, Knossow M, Flamand A. Reversible conformational changes and fusion activity of rabies virus glycoprotein. J Virol 1991;65:4853–4859.
    • (1991) J Virol , vol.65 , pp. 4853-4859
    • Gaudin, Y.1    Tuffereau, C.2    Segretain, D.3    Knossow, M.4    Flamand, A.5
  • 102
    • 44749085794 scopus 로고    scopus 로고
    • Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited
    • Roche S, Albertini AA, Lepault J, Bressanelli S, Gaudin Y. Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited. Cell Mol Life Sci 2008;65:1716–1728.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1716-1728
    • Roche, S.1    Albertini, A.A.2    Lepault, J.3    Bressanelli, S.4    Gaudin, Y.5
  • 103
    • 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
  • 104
    • 84919629153 scopus 로고    scopus 로고
    • Cellular mechanisms of alpha herpesvirus egress: live cell fluorescence microscopy of pseudorabies virus exocytosis
    • Hogue IB, Bosse JB, Hu JR, Thiberge SY, Enquist LW. Cellular mechanisms of alpha herpesvirus egress: live cell fluorescence microscopy of pseudorabies virus exocytosis. PLoS Pathog 2014;10:e1004535.
    • (2014) PLoS Pathog , vol.10
    • Hogue, I.B.1    Bosse, J.B.2    Hu, J.R.3    Thiberge, S.Y.4    Enquist, L.W.5
  • 105
    • 0036309399 scopus 로고    scopus 로고
    • Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers
    • Roche S, Gaudin Y. Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers. Virology 2002;297:128–135.
    • (2002) Virology , vol.297 , pp. 128-135
    • Roche, S.1    Gaudin, Y.2
  • 106
    • 0020684366 scopus 로고
    • Conformational changes in Sindbis virus envelope proteins accompanying exposure to low pH
    • Edwards J, Mann E, Brown DT. Conformational changes in Sindbis virus envelope proteins accompanying exposure to low pH. J Virol 1983;45:1090–1097.
    • (1983) J Virol , vol.45 , pp. 1090-1097
    • Edwards, J.1    Mann, E.2    Brown, D.T.3
  • 107
    • 0027509351 scopus 로고
    • Membrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein
    • Bron R, Wahlberg JM, Garoff H, Wilschut J. Membrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein. EMBO J 1993;12:693–701.
    • (1993) EMBO J , vol.12 , pp. 693-701
    • Bron, R.1    Wahlberg, J.M.2    Garoff, H.3    Wilschut, J.4
  • 108
    • 0022539658 scopus 로고
    • Fusion of fluorescently labeled Sendai virus envelopes with living cultured cells as monitored by fluorescence dequenching
    • Chejanovsky N, Henis YI, Loyter A. Fusion of fluorescently labeled Sendai virus envelopes with living cultured cells as monitored by fluorescence dequenching. Exp Cell Res 1986;164:353–365.
    • (1986) Exp Cell Res , vol.164 , pp. 353-365
    • Chejanovsky, N.1    Henis, Y.I.2    Loyter, A.3
  • 109
    • 0023954154 scopus 로고
    • Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism
    • McClure MO, Marsh M, Weiss RA. Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism. EMBO J 1988;7:513–518.
    • (1988) EMBO J , vol.7 , pp. 513-518
    • McClure, M.O.1    Marsh, M.2    Weiss, R.A.3
  • 110
    • 0000460134 scopus 로고
    • Penetration of herpes simplex virus into human epidermoid cells
    • Huang AS, Wagner RR. Penetration of herpes simplex virus into human epidermoid cells. Proc Soc Exp Biol Med 1964;116:863–869.
    • (1964) Proc Soc Exp Biol Med , vol.116 , pp. 863-869
    • Huang, A.S.1    Wagner, R.R.2
  • 111
    • 0019918329 scopus 로고
    • Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells
    • Johnson DC, Spear PG. Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells. J Virol 1982;43:1102–1112.
    • (1982) J Virol , vol.43 , pp. 1102-1112
    • Johnson, D.C.1    Spear, P.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.