메뉴 건너뛰기




Volumn 9, Issue 12, 2013, Pages 1-14

αvβ6- and αvβ8-Integrins Serve As Interchangeable Receptors for HSV gH/gL to Promote Endocytosis and Activation of Membrane Fusion

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAVBETA6 INTEGRIN; ALPHAVBETA8 INTEGRIN; MEMBRANE FUSION PROTEIN; UNCLASSIFIED DRUG; GLYCOPROTEIN H, HERPES SIMPLEX VIRUS TYPE 1; GLYCOPROTEIN L, HUMAN HERPESVIRUS 1; INTEGRIN; INTEGRIN ALPHAVBETA8; TUMOR ANTIGEN; VIRUS ENVELOPE PROTEIN; VIRUS RECEPTOR;

EID: 84892870179     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003806     Document Type: Article
Times cited : (81)

References (69)
  • 1
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison SC, (2008) Viral membrane fusion. Nat Struct Mol Biol 15: 690-698.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 690-698
    • Harrison, S.C.1
  • 3
    • 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, (2011) Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol 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
  • 4
    • 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
  • 5
    • 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, (1998) 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 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
  • 6
    • 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, (1996) Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 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
  • 7
    • 16544365188 scopus 로고    scopus 로고
    • The herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2
    • Cocchi F, Menotti L, Di Ninni V, Lopez M, Campadelli-Fiume G, (2004) The herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2. J Virol 78: 4720-4729.
    • (2004) J Virol , vol.78 , pp. 4720-4729
    • Cocchi, F.1    Menotti, L.2    Di Ninni, V.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 8
    • 21544456647 scopus 로고    scopus 로고
    • The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors
    • Fusco D, Forghieri C, Campadelli-Fiume G, (2005) The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors. Proc Natl Acad Sci U S A 102: 9323-9328.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9323-9328
    • Fusco, D.1    Forghieri, C.2    Campadelli-Fiume, G.3
  • 9
    • 70349750234 scopus 로고    scopus 로고
    • Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD
    • Avitabile E, Forghieri C, Campadelli-Fiume G, (2009) Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD. J Virol 83: 10752-10760.
    • (2009) J Virol , vol.83 , pp. 10752-10760
    • Avitabile, E.1    Forghieri, C.2    Campadelli-Fiume, G.3
  • 10
    • 78049513712 scopus 로고    scopus 로고
    • Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB
    • Atanasiu D, Saw WT, 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.1    Saw, W.T.2    Cohen, G.H.3    Eisenberg, R.J.4
  • 12
    • 28644433999 scopus 로고    scopus 로고
    • Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry
    • Krummenacher C, Supekar VM, Whitbeck JC, Lazear E, Connolly SA, et al. (2005) Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry. Embo J 24: 4144-4153.
    • (2005) Embo J , vol.24 , pp. 4144-4153
    • Krummenacher, C.1    Supekar, V.M.2    Whitbeck, J.C.3    Lazear, E.4    Connolly, S.A.5
  • 13
    • 80053449684 scopus 로고    scopus 로고
    • Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1
    • Di Giovine P, Settembre EC, Bhargava AK, Luftig MA, Lou H, et al. (2011) Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1. PLoS Pathog 7: e1002277.
    • (2011) PLoS Pathog , vol.7
    • Di Giovine, P.1    Settembre, E.C.2    Bhargava, A.K.3    Luftig, M.A.4    Lou, H.5
  • 14
    • 67650566358 scopus 로고    scopus 로고
    • Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL through the C-terminal profusion
    • Gianni T, Amasio M, Campadelli-Fiume G, (2009) Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL through the C-terminal profusion. 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
  • 15
    • 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, (2012) Viral and cellular contributions to herpes simplex virus entry into the cell. Curr Opin Virol 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
  • 16
    • 0031801093 scopus 로고    scopus 로고
    • Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells
    • Wang X, Kenyon WJ, Li Q, Mullberg J, Hutt-Fletcher LM, (1998) Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells. J Virol 72: 5552-5558.
    • (1998) J Virol , vol.72 , pp. 5552-5558
    • Wang, X.1    Kenyon, W.J.2    Li, Q.3    Mullberg, J.4    Hutt-Fletcher, L.M.5
  • 17
    • 0036183981 scopus 로고    scopus 로고
    • Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1
    • Mullen MM, Haan KM, Longnecker R, Jardetzky TS, (2002) Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1. Mol Cell 9: 375-385.
    • (2002) Mol Cell , vol.9 , pp. 375-385
    • Mullen, M.M.1    Haan, K.M.2    Longnecker, R.3    Jardetzky, T.S.4
  • 18
    • 4444348501 scopus 로고    scopus 로고
    • Human cytomegalovirus UL131-128 genes are indispensable for virus growth in endothelial cells and virus transfer to leukocytes
    • Hahn G, Revello MG, Patrone M, Percivalle E, Campanini G, et al. (2004) Human cytomegalovirus UL131-128 genes are indispensable for virus growth in endothelial cells and virus transfer to leukocytes. J Virol 78: 10023-10033.
    • (2004) J Virol , vol.78 , pp. 10023-10033
    • Hahn, G.1    Revello, M.G.2    Patrone, M.3    Percivalle, E.4    Campanini, G.5
  • 19
    • 84878442997 scopus 로고    scopus 로고
    • CD134 is a cellular receptor specific for human herpesvirus-6B entry
    • Tang H, Serada S, Kawabata A, Ota M, Hayashi E, et al. (2013) CD134 is a cellular receptor specific for human herpesvirus-6B entry. Proc Natl Acad Sci U S A 110: 9096-9099.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9096-9099
    • Tang, H.1    Serada, S.2    Kawabata, A.3    Ota, M.4    Hayashi, E.5
  • 20
    • 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 USA 106: 20464-20469.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20464-20469
    • Chesnokova, L.S.1    Nishimura, S.L.2    Hutt-Fletcher, L.M.3
  • 21
    • 7444256550 scopus 로고    scopus 로고
    • Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain
    • Feire AL, Koss H, Compton T, (2004) Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain. Proc Natl Acad Sci U S A 101: 15470-15475.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15470-15475
    • Feire, A.L.1    Koss, H.2    Compton, T.3
  • 22
    • 33750827767 scopus 로고    scopus 로고
    • Human cytomegalovirus envelope glycoproteins B and H are necessary for TLR2 activation in permissive cells
    • Boehme KW, Guerrero M, Compton T, (2006) Human cytomegalovirus envelope glycoproteins B and H are necessary for TLR2 activation in permissive cells. J Immunol 177: 7094-7102.
    • (2006) J Immunol , vol.177 , pp. 7094-7102
    • Boehme, K.W.1    Guerrero, M.2    Compton, T.3
  • 23
    • 77649197259 scopus 로고    scopus 로고
    • Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells
    • Chandran B, (2010) Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells. J Virol 84: 2188-2199.
    • (2010) J Virol , vol.84 , pp. 2188-2199
    • Chandran, B.1
  • 24
    • 84860832684 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus interacts with EphrinA2 receptor to amplify signaling essential for productive infection
    • Chakraborty S, Veettil MV, Bottero V, Chandran B, (2012) Kaposi's sarcoma-associated herpesvirus interacts with EphrinA2 receptor to amplify signaling essential for productive infection. Proc Natl Acad Sci U S A 109: E1163-1172.
    • (2012) Proc Natl Acad Sci U S A , vol.109
    • Chakraborty, S.1    Veettil, M.V.2    Bottero, V.3    Chandran, B.4
  • 25
    • 84862016090 scopus 로고    scopus 로고
    • The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi's sarcoma-associated herpesvirus
    • Hahn AS, Kaufmann JK, Wies E, Naschberger E, Panteleev-Ivlev J, et al. (2012) The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi's sarcoma-associated herpesvirus. Nat Med 18: 961-966.
    • (2012) Nat Med , vol.18 , pp. 961-966
    • Hahn, A.S.1    Kaufmann, J.K.2    Wies, E.3    Naschberger, E.4    Panteleev-Ivlev, J.5
  • 26
    • 66149115121 scopus 로고    scopus 로고
    • Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor alpha
    • Arii J, Uema M, Morimoto T, Sagara H, Akashi H, et al. (2009) Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor alpha. J Virol 83: 4520-4527.
    • (2009) J Virol , vol.83 , pp. 4520-4527
    • Arii, J.1    Uema, M.2    Morimoto, T.3    Sagara, H.4    Akashi, H.5
  • 27
    • 77957960097 scopus 로고    scopus 로고
    • Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1
    • Arii J, Goto H, Suenaga T, Oyama M, Kozuka-Hata H, et al. (2010) Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1. Nature 467: 859-862.
    • (2010) Nature , vol.467 , pp. 859-862
    • Arii, J.1    Goto, H.2    Suenaga, T.3    Oyama, M.4    Kozuka-Hata, H.5
  • 28
    • 76249083424 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein mediates membrane fusion and entry of neurotropic herpesviruses
    • Suenaga T, Satoh T, Somboonthum P, Kawaguchi Y, Mori Y, et al. (2010) Myelin-associated glycoprotein mediates membrane fusion and entry of neurotropic herpesviruses. Proc Natl Acad Sci USA 107: 866-871.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 866-871
    • Suenaga, T.1    Satoh, T.2    Somboonthum, P.3    Kawaguchi, Y.4    Mori, Y.5
  • 29
    • 84857871177 scopus 로고    scopus 로고
    • alphaVbeta3-integrin relocalizes nectin1 and routes herpes simplex virus to lipid rafts
    • Gianni T, Campadelli-Fiume G, (2012) alphaVbeta3-integrin relocalizes nectin1 and routes herpes simplex virus to lipid rafts. J Virol 86: 2850-2855.
    • (2012) J Virol , vol.86 , pp. 2850-2855
    • Gianni, T.1    Campadelli-Fiume, G.2
  • 30
    • 78650663541 scopus 로고    scopus 로고
    • alphavbeta3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2
    • Gianni T, Gatta V, Campadelli-Fiume G, (2010) alphavbeta3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2. Proc Natl Acad Sci U S A 107: 22260-22265.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22260-22265
    • Gianni, T.1    Gatta, V.2    Campadelli-Fiume, G.3
  • 32
    • 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
  • 33
    • 84864010826 scopus 로고    scopus 로고
    • Herpes Simplex Virus Glycoproteins gH/gL and gB Bind Toll-Like Receptor 2, and Soluble gH/gL Is Sufficient To Activate NF-kappaB
    • Leoni V, Gianni T, Salvioli S, Campadelli-Fiume G, (2012) Herpes Simplex Virus Glycoproteins gH/gL and gB Bind Toll-Like Receptor 2, and Soluble gH/gL Is Sufficient To Activate NF-kappaB. J Virol 86: 6555-6562.
    • (2012) J Virol , vol.86 , pp. 6555-6562
    • Leoni, V.1    Gianni, T.2    Salvioli, S.3    Campadelli-Fiume, G.4
  • 34
    • 0026042996 scopus 로고
    • Cloning and expression of a divergent integrin subunit beta 8
    • Moyle M, Napier MA, McLean JW, (1991) Cloning and expression of a divergent integrin subunit beta 8. J Biol Chem 266: 19650-19658.
    • (1991) J Biol Chem , vol.266 , pp. 19650-19658
    • Moyle, M.1    Napier, M.A.2    McLean, J.W.3
  • 35
    • 0032571765 scopus 로고    scopus 로고
    • Synaptic and glial localization of the integrin alphavbeta8 in mouse and rat brain
    • Nishimura SL, Boylen KP, Einheber S, Milner TA, Ramos DM, et al. (1998) Synaptic and glial localization of the integrin alphavbeta8 in mouse and rat brain. Brain Res 791: 271-282.
    • (1998) Brain Res , vol.791 , pp. 271-282
    • Nishimura, S.L.1    Boylen, K.P.2    Einheber, S.3    Milner, T.A.4    Ramos, D.M.5
  • 36
    • 0028171951 scopus 로고
    • Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1
    • Blystone SD, Graham IL, Lindberg FP, Brown EJ, (1994) Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1. J Cell Biol 127: 1129-1137.
    • (1994) J Cell Biol , vol.127 , pp. 1129-1137
    • Blystone, S.D.1    Graham, I.L.2    Lindberg, F.P.3    Brown, E.J.4
  • 38
    • 0002109061 scopus 로고
    • Membrane fusion induced by herpes simplex virus
    • In: Bentz J, editor, Boca Raton: CRC Press
    • Spear PG (1992) Membrane fusion induced by herpes simplex virus. In: Bentz J, editor. Viral Fusion Mechanism. Boca Raton: CRC Press. pp. 201-232.
    • (1992) Viral Fusion Mechanism , pp. 201-232
    • Spear, P.G.1
  • 39
    • 0027473606 scopus 로고
    • Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans
    • Gruenheid S, Gatzke L, Meadows H, Tufaro F, (1993) Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans. J Virol 67: 93-100.
    • (1993) J Virol , vol.67 , pp. 93-100
    • Gruenheid, S.1    Gatzke, L.2    Meadows, H.3    Tufaro, F.4
  • 40
    • 40749106962 scopus 로고    scopus 로고
    • PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B
    • Satoh T, Arii J, Suenaga T, Wang J, Kogure A, et al. (2008) PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B. Cell 132: 935-944.
    • (2008) Cell , vol.132 , pp. 935-944
    • Satoh, T.1    Arii, J.2    Suenaga, T.3    Wang, J.4    Kogure, A.5
  • 41
    • 77950489408 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins H/L bind to cells independently of alphavbeta3 integrin and inhibit virus entry, and their constitutive expression restricts infection
    • Gianni T, Cerretani A, Dubois R, Salvioli S, Blystone SS, et al. (2010) Herpes simplex virus glycoproteins H/L bind to cells independently of alphavbeta3 integrin and inhibit virus entry, and their constitutive expression restricts infection. J Virol 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
  • 42
    • 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, et al. (1992) Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted. J Virol 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
  • 43
    • 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
  • 44
    • 0035915995 scopus 로고    scopus 로고
    • Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate
    • Pertel PE, Fridberg A, Parish ML, Spear PG, (2001) Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate. Virology 279: 313-324.
    • (2001) Virology , vol.279 , pp. 313-324
    • Pertel, P.E.1    Fridberg, A.2    Parish, M.L.3    Spear, P.G.4
  • 45
    • 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, (2004) Entry of Herpes Simplex Virus Mediated by Chimeric Forms of Nectin1 Retargeted to Endosomes or to Lipid Rafts Occurs through Acidic Endosomes. J Virol 78: 12268-12276.
    • (2004) J Virol , vol.78 , pp. 12268-12276
    • Gianni, T.1    Campadelli-Fiume, G.2    Menotti, L.3
  • 46
    • 33645299331 scopus 로고    scopus 로고
    • Alphavbeta6 integrin in wound healing and cancer of the oral cavity
    • Thomas GJ, Nystrom ML, Marshall JF, (2006) Alphavbeta6 integrin in wound healing and cancer of the oral cavity. J Oral Pathol Med 35: 1-10.
    • (2006) J Oral Pathol Med , vol.35 , pp. 1-10
    • Thomas, G.J.1    Nystrom, M.L.2    Marshall, J.F.3
  • 47
    • 70349275248 scopus 로고    scopus 로고
    • Impact of Rac1 and Cdc42 signaling during early herpes simplex virus type 1 infection of keratinocytes
    • Petermann P, Haase I, Knebel-Morsdorf D, (2009) Impact of Rac1 and Cdc42 signaling during early herpes simplex virus type 1 infection of keratinocytes. J Virol 83: 9759-9772.
    • (2009) J Virol , vol.83 , pp. 9759-9772
    • Petermann, P.1    Haase, I.2    Knebel-Morsdorf, D.3
  • 48
    • 84855849822 scopus 로고    scopus 로고
    • Fusion of Epstein-Barr virus with epithelial cells can be triggered by alphavbeta5 in addition to alphavbeta6 and alphavbeta8, and integrin binding triggers a conformational change in glycoproteins gHgL
    • Chesnokova LS, Hutt-Fletcher LM, (2011) Fusion of Epstein-Barr virus with epithelial cells can be triggered by alphavbeta5 in addition to alphavbeta6 and alphavbeta8, and integrin binding triggers a conformational change in glycoproteins gHgL. J Virol 85: 13214-13223.
    • (2011) J Virol , vol.85 , pp. 13214-13223
    • Chesnokova, L.S.1    Hutt-Fletcher, L.M.2
  • 50
    • 36049006185 scopus 로고    scopus 로고
    • Cell integrins: commonly used receptors for diverse viral pathogens
    • Stewart PL, Nemerow GR, (2007) Cell integrins: commonly used receptors for diverse viral pathogens. Trends Microbiol 15: 500-507.
    • (2007) Trends Microbiol , vol.15 , pp. 500-507
    • Stewart, P.L.1    Nemerow, G.R.2
  • 52
    • 11144227268 scopus 로고    scopus 로고
    • Interaction of West Nile virus with alpha v beta 3 integrin mediates virus entry into cells
    • Chu JJ, Ng ML, (2004) Interaction of West Nile virus with alpha v beta 3 integrin mediates virus entry into cells. J Biol Chem 279: 54533-54541.
    • (2004) J Biol Chem , vol.279 , pp. 54533-54541
    • Chu, J.J.1    Ng, M.L.2
  • 53
    • 81255208061 scopus 로고    scopus 로고
    • The many roles of the highly interactive HSV protein ICP27, a key regulator of infection
    • Sandri-Goldin RM, (2011) The many roles of the highly interactive HSV protein ICP27, a key regulator of infection. Future Microbiol 6: 1261-1277.
    • (2011) Future Microbiol , vol.6 , pp. 1261-1277
    • Sandri-Goldin, R.M.1
  • 54
    • 84874035038 scopus 로고    scopus 로고
    • Regulation of alphaherpesvirus infections by the ICP0 family of proteins
    • Boutell C, Everett RD, (2013) Regulation of alphaherpesvirus infections by the ICP0 family of proteins. J Gen Virol 94: 465-481.
    • (2013) J Gen Virol , vol.94 , pp. 465-481
    • Boutell, C.1    Everett, R.D.2
  • 55
    • 77950838827 scopus 로고    scopus 로고
    • Role of herpes simplex virus ICP0 in the transactivation of genes introduced by infection or transfection: a reappraisal
    • Kalamvoki M, Roizman B, (2010) Role of herpes simplex virus ICP0 in the transactivation of genes introduced by infection or transfection: a reappraisal. J Virol 84: 4222-4228.
    • (2010) J Virol , vol.84 , pp. 4222-4228
    • Kalamvoki, M.1    Roizman, B.2
  • 56
    • 58149399387 scopus 로고    scopus 로고
    • The two functions of herpes simplex virus 1 ICP0, inhibition of silencing by the CoREST/REST/HDAC complex and degradation of PML, are executed in tandem
    • Gu H, Roizman B, (2009) The two functions of herpes simplex virus 1 ICP0, inhibition of silencing by the CoREST/REST/HDAC complex and degradation of PML, are executed in tandem. J Virol 83: 181-187.
    • (2009) J Virol , vol.83 , pp. 181-187
    • Gu, H.1    Roizman, B.2
  • 57
    • 53749099520 scopus 로고    scopus 로고
    • Construction of a fully retargeted herpes simplex virus 1 recombinant capable of entering cells solely via human epidermal growth factor receptor 2
    • Menotti L, Cerretani A, Hengel H, Campadelli-Fiume G, (2008) Construction of a fully retargeted herpes simplex virus 1 recombinant capable of entering cells solely via human epidermal growth factor receptor 2. J Virol 20: 10153-10161.
    • (2008) J Virol , vol.20 , pp. 10153-10161
    • Menotti, L.1    Cerretani, A.2    Hengel, H.3    Campadelli-Fiume, G.4
  • 58
    • 11144225840 scopus 로고    scopus 로고
    • A 50-A separation of the integrin alpha v beta 3 extracellular domain C termini reveals an intermediate activation state
    • Gline SE, Cambier S, Govaerts C, Nishimura SL, (2004) A 50-A separation of the integrin alpha v beta 3 extracellular domain C termini reveals an intermediate activation state. J Biol Chem 279: 54567-54572.
    • (2004) J Biol Chem , vol.279 , pp. 54567-54572
    • Gline, S.E.1    Cambier, S.2    Govaerts, C.3    Nishimura, S.L.4
  • 59
    • 0037192933 scopus 로고    scopus 로고
    • The integrin alpha(v)beta8 mediates epithelial homeostasis through MT1-MMP-dependent activation of TGF-beta1
    • Mu D, Cambier S, Fjellbirkeland L, Baron JL, Munger JS, et al. (2002) The integrin alpha(v)beta8 mediates epithelial homeostasis through MT1-MMP-dependent activation of TGF-beta1. J Cell Biol 157: 493-507.
    • (2002) J Cell Biol , vol.157 , pp. 493-507
    • Mu, D.1    Cambier, S.2    Fjellbirkeland, L.3    Baron, J.L.4    Munger, J.S.5
  • 60
    • 0031691062 scopus 로고    scopus 로고
    • Interactions of soluble recombinant integrin alphav beta5 with human adenoviruses
    • Mathias P, Galleno M, Nemerow GR, (1998) Interactions of soluble recombinant integrin alphav beta5 with human adenoviruses. J Virol 72: 8669-8675.
    • (1998) J Virol , vol.72 , pp. 8669-8675
    • Mathias, P.1    Galleno, M.2    Nemerow, G.R.3
  • 61
    • 0038279935 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH and gL
    • Avitabile E, Lombardi G, Campadelli-Fiume G, (2003) Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH and gL. Journal of Virology 77: 6836-6844.
    • (2003) Journal of Virology , vol.77 , pp. 6836-6844
    • Avitabile, E.1    Lombardi, G.2    Campadelli-Fiume, G.3
  • 62
    • 0033557076 scopus 로고    scopus 로고
    • Host range of human T-cell leukemia virus type I analyzed by a cell fusion-dependent reporter gene activation assay
    • Okuma K, Nakamura M, Nakano S, Niho Y, Matsuura Y, (1999) Host range of human T-cell leukemia virus type I analyzed by a cell fusion-dependent reporter gene activation assay. Virology 254: 235-244.
    • (1999) Virology , vol.254 , pp. 235-244
    • Okuma, K.1    Nakamura, M.2    Nakano, S.3    Niho, Y.4    Matsuura, Y.5
  • 63
    • 0034326620 scopus 로고    scopus 로고
    • DNA vaccination against rat her-2/Neu p185 more effectively inhibits carcinogenesis than transplantable carcinomas in transgenic BALB/c mice
    • Rovero S, Amici A, Carlo ED, Bei R, Nanni P, et al. (2000) DNA vaccination against rat her-2/Neu p185 more effectively inhibits carcinogenesis than transplantable carcinomas in transgenic BALB/c mice. J Immunol 165: 5133-5142.
    • (2000) J Immunol , vol.165 , pp. 5133-5142
    • Rovero, S.1    Amici, A.2    Carlo, E.D.3    Bei, R.4    Nanni, P.5
  • 64
    • 0028172192 scopus 로고
    • Integrin alpha v beta 8. Interaction with vitronectin and functional divergence of the beta 8 cytoplasmic domain
    • Nishimura SL, Sheppard D, Pytela R, (1994) Integrin alpha v beta 8. Interaction with vitronectin and functional divergence of the beta 8 cytoplasmic domain. J Biol Chem 269: 28708-28715.
    • (1994) J Biol Chem , vol.269 , pp. 28708-28715
    • Nishimura, S.L.1    Sheppard, D.2    Pytela, R.3
  • 65
    • 2442671781 scopus 로고    scopus 로고
    • Integrin alphavbeta8 functions as a receptor for foot-and-mouth disease virus: role of the beta-chain cytodomain in integrin-mediated infection
    • Jackson T, Clark S, Berryman S, Burman A, Cambier S, et al. (2004) Integrin alphavbeta8 functions as a receptor for foot-and-mouth disease virus: role of the beta-chain cytodomain in integrin-mediated infection. J Virol 78: 4533-4540.
    • (2004) J Virol , vol.78 , pp. 4533-4540
    • Jackson, T.1    Clark, S.2    Berryman, S.3    Burman, A.4    Cambier, S.5
  • 66
    • 0036173066 scopus 로고    scopus 로고
    • Effects of herpes simplex virus on structure and function of nectin-1/HveC
    • Krummenacher C, Baribaud I, Sanzo JF, Cohen GH, Eisenberg RJ, (2002) Effects of herpes simplex virus on structure and function of nectin-1/HveC. J Virol 76: 2424-2433.
    • (2002) J Virol , vol.76 , pp. 2424-2433
    • Krummenacher, C.1    Baribaud, I.2    Sanzo, J.F.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 67
    • 0028858576 scopus 로고
    • Monoclonal antibody 9EG7 defines a novel beta 1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni G, Shih DT, Buck CA, Hemler ME, (1995) Monoclonal antibody 9EG7 defines a novel beta 1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J Biol Chem 270: 25570-25577.
    • (1995) J Biol Chem , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 68
    • 34247115646 scopus 로고    scopus 로고
    • Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions
    • Bender FC, Samanta M, Heldwein EE, de Leon MP, Bilman E, et al. (2007) Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions. J Virol 81: 3827-3841.
    • (2007) J Virol , vol.81 , pp. 3827-3841
    • Bender, F.C.1    Samanta, M.2    Heldwein, E.E.3    de Leon, M.P.4    Bilman, E.5
  • 69
    • 84880072554 scopus 로고    scopus 로고
    • Regulation of herpes simplex virus gB-induced cell-cell fusion by mutant forms of gH/gL in the absence of gD and cellular receptors
    • doi:10.1128/mBio.00046-13
    • Atanasiu D, Cairns TM, Whitbeck JC, Saw WT, Rao S, et al. (2013) Regulation of herpes simplex virus gB-induced cell-cell fusion by mutant forms of gH/gL in the absence of gD and cellular receptors. MBio 4 (2):: pii: e00046-13 doi:10.1128/mBio.00046-13.
    • (2013) MBio , vol.4 , Issue.2 , pp. 13
    • Atanasiu, D.1    Cairns, T.M.2    Whitbeck, J.C.3    Saw, W.T.4    Rao, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.