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Volumn 88, Issue 5, 2014, Pages 2677-2689

Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein b

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GLYCOPROTEIN B; LIPID; LIPOSOME; MONOCLONAL ANTIBODY; PEPTIDE ANTIBODY; POLYCLONAL ANTIBODY;

EID: 84896724942     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03200-13     Document Type: Article
Times cited : (47)

References (61)
  • 2
    • 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. http://dx.doi.org/10.1128 /JVI.01700-10.
    • (2010) J. Virol. , vol.84 , pp. 12292-12299
    • Atanasiu, D.1    Saw, W.T.2    Cohen, G.H.3    Eisenberg, R.J.4
  • 3
    • 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
    • Atanasiu D, Cairns TM, Whitbeck JC, Saw WT, Rao S, Eisenberg RJ, Cohen GH. 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):e00046 -13. http://dx.doi.org/10.1128/mBio.00046-13.
    • (2013) mBio , vol.4 , Issue.2
    • Atanasiu, D.1    Cairns, T.M.2    Whitbeck, J.C.3    Saw, W.T.4    Rao, S.5    Eisenberg, R.J.6    Cohen, G.H.7
  • 5
    • 1842850945 scopus 로고    scopus 로고
    • Herpes simplex virus: receptors and ligands for cell entry
    • Spear PG. 2004. Herpes simplex virus: receptors and ligands for cell entry. Cell. Microbiol. 6:401-410. http://dx.doi.org/10.1111/j.1462-5822.2004 .00389.x.
    • (2004) Cell. Microbiol. , vol.6 , pp. 401-410
    • Spear, P.G.1
  • 6
    • 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. 2010. Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1. J. Virol. 84:12924-12933. http://dx.doi.org/10.1128/JVI.01750-10.
    • (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
  • 7
    • 62449188223 scopus 로고    scopus 로고
    • Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B
    • Backovic M, Longnecker R, Jardetzky TS. 2009. Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B. Proc. Natl. Acad. Sci. U. S. A. 106:2880-2885. http://dx.doi.org/10.1073/pnas.0810530106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2880-2885
    • Backovic, M.1    Longnecker, R.2    Jardetzky, T.S.3
  • 8
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche S, Bressanelli S, Rey FA, Gaudin Y. 2006. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 313:187-191. http://dx.doi.org/10.1126/science.1127683.
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 9
    • 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. http://dx.doi.org /10.1038/nsmb.1484.
    • (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
  • 10
    • 84877706768 scopus 로고    scopus 로고
    • Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form
    • Vitu E, Sharma S, Stampfer SD, Heldwein EE. 2013. Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form. J. Mol. Biol. 425:2056-2071. http://dx.doi.org/10.1016/j.jmb .2013.03.001.
    • (2013) J. Mol. Biol. , vol.425 , pp. 2056-2071
    • Vitu, E.1    Sharma, S.2    Stampfer, S.D.3    Heldwein, E.E.4
  • 11
    • 84871704386 scopus 로고    scopus 로고
    • HCMV gB shares structural and functional properties with gB proteins from other herpesviruses
    • Sharma S, Wisner TW, Johnson DC, Heldwein EE. 2013. HCMV gB shares structural and functional properties with gB proteins from other herpesviruses. Virology 435:239-249. http://dx.doi.org/10.1016/j.virol .2012.09.024.
    • (2013) Virology , vol.435 , pp. 239-249
    • Sharma, S.1    Wisner, T.W.2    Johnson, D.C.3    Heldwein, E.E.4
  • 12
    • 35348938515 scopus 로고    scopus 로고
    • Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins
    • Backovic M, Leser GP, Lamb RA, Longnecker R, Jardetzky TS. 2007. Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins. Virology 368:102-113. http://dx.doi.org/10.1016/j .virol.2007.06.031.
    • (2007) Virology , vol.368 , pp. 102-113
    • Backovic, M.1    Leser, G.P.2    Lamb, R.A.3    Longnecker, R.4    Jardetzky, T.S.5
  • 15
    • 34247570805 scopus 로고    scopus 로고
    • Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B
    • Hannah BP, Heldwein EE, Bender FC, Cohen GH, Eisenberg RJ. 2007. Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B. J. Virol. 81:4858-4865. http://dx.doi.org/10.1128/JVI.02755 -06.
    • (2007) J. Virol. , vol.81 , pp. 4858-4865
    • Hannah, B.P.1    Heldwein, E.E.2    Bender, F.C.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 16
    • 67449093075 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops
    • Hannah BP, Cairns TM, Bender FC, Whitbeck JC, Lou H, Eisenberg RJ, Cohen GH. 2009. Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops. J. Virol. 83:6825-6836. http://dx .doi.org/10.1128/JVI.00301-09.
    • (2009) J. Virol. , vol.83 , pp. 6825-6836
    • Hannah, B.P.1    Cairns, T.M.2    Bender, F.C.3    Whitbeck, J.C.4    Lou, H.5    Eisenberg, R.J.6    Cohen, G.H.7
  • 17
    • 84886891960 scopus 로고    scopus 로고
    • Dual split protein-based fusion assay reveals that mutations to herpes simplex virus (HSV) glycoprotein gB alter the kinetics of cell-cell fusion induced by HSV entry glycoproteins
    • Atanasiu D, Saw WT, Gallagher JR, Hannah BP, Matsuda Z, Whitbeck JC, Cohen GH, Eisenberg RJ. 2013. Dual split protein-based fusion assay reveals that mutations to herpes simplex virus (HSV) glycoprotein gB alter the kinetics of cell-cell fusion induced by HSV entry glycoproteins. J. Virol. 87:11332-11345. http://dx.doi.org/10.1128/JVI.01700-13.
    • (2013) J. Virol. , vol.87 , pp. 11332-11345
    • Atanasiu, D.1    Saw, W.T.2    Gallagher, J.R.3    Hannah, B.P.4    Matsuda, Z.5    Whitbeck, J.C.6    Cohen, G.H.7    Eisenberg, R.J.8
  • 18
    • 70350322295 scopus 로고    scopus 로고
    • Fusion between perinuclear virions and the outer nuclear membrane requires the fusogenic activity of herpes simplex virus gB
    • Wright CC, Wisner TW, Hannah BP, Eisenberg RJ, Cohen GH, Johnson DC. 2009. Fusion between perinuclear virions and the outer nuclear membrane requires the fusogenic activity of herpes simplex virus gB. J. Virol. 83:11847-11856. http://dx.doi.org/10.1128/JVI.01397-09.
    • (2009) J. Virol. , vol.83 , pp. 11847-11856
    • Wright, C.C.1    Wisner, T.W.2    Hannah, B.P.3    Eisenberg, R.J.4    Cohen, G.H.5    Johnson, D.C.6
  • 19
    • 24644432375 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry
    • Bender FC, Whitbeck JC, Lou H, Cohen GH, Eisenberg RJ. 2005. Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry. J. Virol. 79:11588-11597. http: //dx.doi.org/10.1128/JVI.79.18.11588-11597.2005.
    • (2005) J. Virol. , vol.79 , pp. 11588-11597
    • Bender, F.C.1    Whitbeck, J.C.2    Lou, H.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 20
    • 77950513683 scopus 로고    scopus 로고
    • Bimolecular complementation defines functional regions of herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion
    • Atanasiu D, Whitbeck JC, de Leon MP, Lou H, Hannah BP, Cohen GH, Eisenberg RJ. 2010. Bimolecular complementation defines functional regions of herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion. J. Virol. 84:3825-3834. http://dx.doi.org /10.1128/JVI.02687-09.
    • (2010) J. Virol. , vol.84 , pp. 3825-3834
    • Atanasiu, D.1    Whitbeck, J.C.2    de Leon, M.P.3    Lou, H.4    Hannah, B.P.5    Cohen, G.H.6    Eisenberg, R.J.7
  • 21
    • 36749035394 scopus 로고    scopus 로고
    • Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion
    • Atanasiu D, Whitbeck JC, Cairns TM, Reilly B, Cohen GH, Eisenberg RJ. 2007. Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion. Proc. Natl. Acad. Sci. U. S. A. 104:18718-18723. http://dx.doi.org/10.1073 /pnas.0707452104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18718-18723
    • Atanasiu, D.1    Whitbeck, J.C.2    Cairns, T.M.3    Reilly, B.4    Cohen, G.H.5    Eisenberg, R.J.6
  • 22
    • 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. 1989. Domain structure of herpes simplex virus 1 glycoprotein B: neutralizing epitopes map in regions of continuous and discontinuous residues. Virology 172:11-24. http://dx.doi.org/10.1016/0042-6822(89)90102-5.
    • (1989) Virology , vol.172 , pp. 11-24
    • Pereira, L.1    Ali, M.2    Kousoulas, K.3    Huo, B.4    Banks, T.5
  • 23
    • 0026543842 scopus 로고
    • Domains of herpes simplex virus I glycoprotein B that function in virus penetration, cell-to-cell spread, and cell fusion
    • Navarro D, Paz P, Pereira L. 1992. Domains of herpes simplex virus I glycoprotein B that function in virus penetration, cell-to-cell spread, and cell fusion. Virology 186:99-112. http://dx.doi.org/10.1016/0042-6822 (92)90064-V.
    • (1992) Virology , vol.186 , pp. 99-112
    • Navarro, D.1    Paz, P.2    Pereira, L.3
  • 24
    • 0022515749 scopus 로고
    • Antigenic variation (mar mutations) in herpes simplex virus glycoprotein B can induce temperature-dependent alterations in gB processing and virus production
    • Marlin SD, Highlander SL, Holland TC, Levine M, Glorioso JC. 1986. Antigenic variation (mar mutations) in herpes simplex virus glycoprotein B can induce temperature-dependent alterations in gB processing and virus production. J. Virol. 59:142-153.
    • (1986) J. Virol. , vol.59 , pp. 142-153
    • Marlin, S.D.1    Highlander, S.L.2    Holland, T.C.3    Levine, M.4    Glorioso, J.C.5
  • 25
    • 0024504465 scopus 로고
    • Identification of mar mutations in herpes simplex virus type 1 glycoprotein B which alter antigenic structure and function in virus penetration
    • Highlander SL, Dorney DJ, Gage PJ, Holland TC, Cai W, Person S, Levine M, Glorioso JC. 1989. Identification of mar mutations in herpes simplex virus type 1 glycoprotein B which alter antigenic structure and function in virus penetration. J. Virol. 63:730-738.
    • (1989) J. Virol. , vol.63 , pp. 730-738
    • Highlander, S.L.1    Dorney, D.J.2    Gage, P.J.3    Holland, T.C.4    Cai, W.5    Person, S.6    Levine, M.7    Glorioso, J.C.8
  • 26
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
    • White JM, Delos SE, Brecher M, Schornberg K. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219. http://dx.doi.org/10.1080/10409230802058320.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 27
    • 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. 2012. The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes. mBio 3(6):e00429 -12. http://dx.doi.org /10.1128/mBio.00429-12.
    • (2012) mBio , vol.3 , Issue.6
    • 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
  • 28
    • 0042890360 scopus 로고    scopus 로고
    • Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry
    • Bender FC, Whitbeck JC, Ponce de Leon M, Lou H, Eisenberg RJ, Cohen GH. 2003. Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry. J. Virol. 77:9542-9552. http://dx.doi.org/10.1128/JVI.77.17.9542-9552.2003.
    • (2003) J. Virol. , vol.77 , pp. 9542-9552
    • Bender, F.C.1    Whitbeck, J.C.2    Ponce de Leon, M.3    Lou, H.4    Eisenberg, R.J.5    Cohen, G.H.6
  • 29
    • 80052075784 scopus 로고    scopus 로고
    • Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment
    • Cairns TM, Whitbeck JC, Lou H, Heldwein EE, Chowdary TK, Eisenberg RJ, Cohen GH. 2011. Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment. J. Virol. 85:6175-6184. http://dx.doi.org/10.1128/JVI.00119-11.
    • (2011) J. Virol. , vol.85 , pp. 6175-6184
    • Cairns, T.M.1    Whitbeck, J.C.2    Lou, H.3    Heldwein, E.E.4    Chowdary, T.K.5    Eisenberg, R.J.6    Cohen, G.H.7
  • 30
    • 84864390291 scopus 로고    scopus 로고
    • Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation
    • Silverman JL, Greene NG, King DS, Heldwein EE. 2012. Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation. J. Virol. 86:8171-8184. http://dx.doi.org/10.1128/JVI.00932-12.
    • (2012) J. Virol. , vol.86 , pp. 8171-8184
    • Silverman, J.L.1    Greene, N.G.2    King, D.S.3    Heldwein, E.E.4
  • 31
    • 18144403497 scopus 로고    scopus 로고
    • Epitope-mapping studies define two major neutralization sites on the vaccinia virus extracellular enveloped virus glycoprotein B5R
    • Aldaz-Carroll L, Whitbeck JC, Ponce de Leon M, Lou H, Hirao L, Isaacs SN, Moss B, Eisenberg RJ, Cohen GH. 2005. Epitope-mapping studies define two major neutralization sites on the vaccinia virus extracellular enveloped virus glycoprotein B5R. J. Virol. 79:6260-6271. http://dx.doi.org/10.1128/JVI.79.10.6260-6271.2005.
    • (2005) J. Virol. , vol.79 , pp. 6260-6271
    • Aldaz-Carroll, L.1    Whitbeck, J.C.2    Ponce de Leon, M.3    Lou, H.4    Hirao, L.5    Isaacs, S.N.6    Moss, B.7    Eisenberg, R.J.8    Cohen, G.H.9
  • 33
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • Heymann JB, Belnap DM. 2007. Bsoft: image processing and molecular modeling for electron microscopy. J. Struct. Biol. 157:3-18. http://dx.doi.org/10.1016/j.jsb.2006.06.006.
    • (2007) J. Struct. Biol. , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 34
    • 33644762976 scopus 로고    scopus 로고
    • Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function
    • Cairns TM, Shaner MS, Zuo Y, Ponce-de-Leon M, Baribaud I, Eisenberg RJ, Cohen GH, Whitbeck JC. 2006. Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function. J. Virol. 80:2596-2608. http://dx.doi.org/10.1128/JVI.80.6.2596-2608.2006.
    • (2006) J. Virol. , vol.80 , pp. 2596-2608
    • Cairns, T.M.1    Shaner, M.S.2    Zuo, Y.3    Ponce-de-Leon, M.4    Baribaud, I.5    Eisenberg, R.J.6    Cohen, G.H.7    Whitbeck, J.C.8
  • 35
    • 0033557076 scopus 로고    scopus 로고
    • Host range of human T-cell leukemia virus type I analyzed by a cell fusiondependent 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 fusiondependent reporter gene activation assay. Virology 254:235-244. http://dx.doi.org/10.1006/viro.1998.9530.
    • (1999) Virology , vol.254 , pp. 235-244
    • Okuma, K.1    Nakamura, M.2    Nakano, S.3    Niho, Y.4    Matsuura, Y.5
  • 36
    • 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. http: //dx.doi.org/10.1006/viro.2000.0713.
    • (2001) Virology , vol.279 , pp. 313-324
    • Pertel, P.E.1    Fridberg, A.2    Parish, M.L.3    Spear, P.G.4
  • 37
    • 0036839118 scopus 로고    scopus 로고
    • Structure-based analysis of the herpes simplex virus glycoproteinDbinding site present on herpesvirus entry mediator HveA (HVEM)
    • Connolly SA, Landsburg DJ, Carfi A, Wiley DC, Eisenberg RJ, Cohen GH. 2002. Structure-based analysis of the herpes simplex virus glycoproteinDbinding site present on herpesvirus entry mediator HveA (HVEM). J. Virol. 76:10894-10904. http://dx.doi.org/10.1128/JVI.76.21.10894-10904.2002.
    • (2002) J. Virol. , vol.76 , pp. 10894-10904
    • Connolly, S.A.1    Landsburg, D.J.2    Carfi, A.3    Wiley, D.C.4    Eisenberg, R.J.5    Cohen, G.H.6
  • 39
    • 0038758772 scopus 로고    scopus 로고
    • Structure-based mutagenesis of herpes simplex virus glycoproteinDdefines three critical regions at the gD-HveA/HVEM binding interface
    • Connolly SA, Landsburg DJ, Carfi A, Wiley DC, Cohen GH, Eisenberg RJ. 2003. Structure-based mutagenesis of herpes simplex virus glycoproteinDdefines three critical regions at the gD-HveA/HVEM binding interface. J. Virol. 77:8127-8140. http://dx.doi.org/10.1128/JVI.77.14.8127 -8140.2003.
    • (2003) J. Virol. , vol.77 , pp. 8127-8140
    • Connolly, S.A.1    Landsburg, D.J.2    Carfi, A.3    Wiley, D.C.4    Cohen, G.H.5    Eisenberg, R.J.6
  • 40
    • 0021206408 scopus 로고
    • Mutations affecting conformation or sequence of neutralizing epitopes identified by reactivity of viable plaques segregate from syn and ts domains of HSV-1(F) gB gene
    • Kousoulas KG, Pellett PE, Pereira L, Roizman B. 1984. Mutations affecting conformation or sequence of neutralizing epitopes identified by reactivity of viable plaques segregate from syn and ts domains of HSV-1(F) gB gene. Virology 135:379-394. http://dx.doi.org/10.1016/0042-6822 (84)90194-6.
    • (1984) Virology , vol.135 , pp. 379-394
    • Kousoulas, K.G.1    Pellett, P.E.2    Pereira, L.3    Roizman, B.4
  • 41
    • 0021930782 scopus 로고
    • Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: primary sequence and predicted protein structure of the wild type and of monoclonal antibodyresistant mutants
    • Pellett PE, Kousoulas KG, Pereira L, Roizman B. 1985. Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: primary sequence and predicted protein structure of the wild type and of monoclonal antibodyresistant mutants. J. Virol. 53:243-253.
    • (1985) J. Virol. , vol.53 , pp. 243-253
    • Pellett, P.E.1    Kousoulas, K.G.2    Pereira, L.3    Roizman, B.4
  • 42
    • 0019813298 scopus 로고
    • Differential immunologic reactivity and processing of glycoproteins gA and gB of herpes simplex virus types 1 and 2 made in Vero and HEp-2 cells
    • Pereira L, Dondero D, Norrild B, Roizman B. 1981. Differential immunologic reactivity and processing of glycoproteins gA and gB of herpes simplex virus types 1 and 2 made in Vero and HEp-2 cells. Proc. Natl. Acad. Sci. U. S. A. 78:5202-5206. http://dx.doi.org/10.1073/pnas.78.8.5202.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 5202-5206
    • Pereira, L.1    Dondero, D.2    Norrild, B.3    Roizman, B.4
  • 44
    • 0034904724 scopus 로고    scopus 로고
    • Multimeric humanized varicella-zoster virus antibody fragments to gH neutralize virus while monomeric fragments do not
    • Drew PD, Moss MT, Pasieka TJ, Grose C, Harris WJ, Porter AJ. 2001. Multimeric humanized varicella-zoster virus antibody fragments to gH neutralize virus while monomeric fragments do not. J. Gen. Virol. 82: 1959-1963. http://vir.sgmjournals.org/content/82/8/1959.long.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1959-1963
    • Drew, P.D.1    Moss, M.T.2    Pasieka, T.J.3    Grose, C.4    Harris, W.J.5    Porter, A.J.6
  • 46
    • 0028957940 scopus 로고
    • Protection from lethal coronavirus infection by immunoglobulin fragments
    • Lamarre A, Talbot PJ. 1995. Protection from lethal coronavirus infection by immunoglobulin fragments. J. Immunol. 154:3975-3984.
    • (1995) J. Immunol. , vol.154 , pp. 3975-3984
    • Lamarre, A.1    Talbot, P.J.2
  • 47
    • 80053964873 scopus 로고    scopus 로고
    • Low-pHdependent 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. 2011. Low-pHdependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity. J. Virol. 85:9964-9973. http://dx.doi.org/10.1128/JVI.05291-11.
    • (2011) J. Virol. , vol.85 , pp. 9964-9973
    • Dollery, S.J.1    Wright, C.C.2    Johnson, D.C.3    Nicola, A.V.4
  • 48
    • 77549086793 scopus 로고    scopus 로고
    • Low pH-induced conformational change in herpes simplex virus glycoprotein B
    • Dollery SJ, Delboy MG, Nicola AV. 2010. Low pH-induced conformational change in herpes simplex virus glycoprotein B. J. Virol. 84:3759- 3766. http://dx.doi.org/10.1128/JVI.02573-09.
    • (2010) J. Virol. , vol.84 , pp. 3759-3766
    • Dollery, S.J.1    Delboy, M.G.2    Nicola, A.V.3
  • 49
    • 78649512396 scopus 로고    scopus 로고
    • Reversible conformational change in herpes simplex virus glycoprotein B with fusion-fromwithout activity is triggered by mildly acidic pH
    • Siekavizza-Robles CR, Dollery SJ, Nicola AV. 2010. Reversible conformational change in herpes simplex virus glycoprotein B with fusion-fromwithout activity is triggered by mildly acidic pH. Virol. J. 7:352. http://dx.doi.org/10.1186/1743-422X-7-352.
    • (2010) Virol. J. , vol.7 , pp. 352
    • Siekavizza-Robles, C.R.1    Dollery, S.J.2    Nicola, A.V.3
  • 50
    • 0023195273 scopus 로고
    • Predicted structure of tail-fiber proteins of T-even type phages
    • Riede I, Schwarz H, Jahnig F. 1987. Predicted structure of tail-fiber proteins of T-even type phages. FEBS Lett. 215:145-150. http://dx.doi.org /10.1016/0014-5793(87)80130-8.
    • (1987) FEBS Lett. , vol.215 , pp. 145-150
    • Riede, I.1    Schwarz, H.2    Jahnig, F.3
  • 51
    • 0030564888 scopus 로고    scopus 로고
    • Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: a hinged viral adhesin
    • Cerritelli ME, Wall JS, Simon MN, Conway JF, Steven AC. 1996. Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: a hinged viral adhesin. J. Mol. Biol. 260:767-780. http://dx.doi.org/10.1006/jmbi.1996.0436.
    • (1996) J. Mol. Biol. , vol.260 , pp. 767-780
    • Cerritelli, M.E.1    Wall, J.S.2    Simon, M.N.3    Conway, J.F.4    Steven, A.C.5
  • 54
    • 62749124125 scopus 로고    scopus 로고
    • Monoclonal antibodies against the fusion peptide of hemagglutinin protect mice from lethal influenza A virus H5N1 infection
    • Prabhu N, Prabakaran M, Ho HT, Velumani S, Qiang J, Goutama M, Kwang J. 2009. Monoclonal antibodies against the fusion peptide of hemagglutinin protect mice from lethal influenza A virus H5N1 infection. J. Virol. 83:2553-2562. http://dx.doi.org/10.1128/JVI.02165-08.
    • (2009) J. Virol. , vol.83 , pp. 2553-2562
    • Prabhu, N.1    Prabakaran, M.2    Ho, H.T.3    Velumani, S.4    Qiang, J.5    Goutama, M.6    Kwang, J.7
  • 55
    • 0026055421 scopus 로고
    • Epitope mapping of two immunodominant domains of gp41, the transmembrane protein of human immunodeficiency virus type 1, using ten human monoclonal antibodies
    • Xu JY, Gorny MK, Palker T, Karwowska S, Zolla-Pazner S. 1991. Epitope mapping of two immunodominant domains of gp41, the transmembrane protein of human immunodeficiency virus type 1, using ten human monoclonal antibodies. J. Virol. 65:4832-4838.
    • (1991) J. Virol. , vol.65 , pp. 4832-4838
    • Xu, J.Y.1    Gorny, M.K.2    Palker, T.3    Karwowska, S.4    Zolla-Pazner, S.5
  • 56
    • 0025861673 scopus 로고
    • Two immunodominant domains of gp41 bind antibodies which enhance human immunodeficiency virus type 1 infection in vitro
    • Robinson WE, Jr, Gorny MK, Xu JY, Mitchell WM, Zolla-Pazner S. 1991. Two immunodominant domains of gp41 bind antibodies which enhance human immunodeficiency virus type 1 infection in vitro. J. Virol. 65:4169-4176.
    • (1991) J. Virol. , vol.65 , pp. 4169-4176
    • Robinson, W.E.1    Gorny, M.K.2    Xu, J.Y.3    Mitchell, W.M.4    Zolla-Pazner, S.5
  • 57
    • 0030997127 scopus 로고    scopus 로고
    • Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein
    • Earl PL, Broder CC, Doms RW, Moss B. 1997. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol. 71:2674-2684.
    • (1997) J. Virol. , vol.71 , pp. 2674-2684
    • Earl, P.L.1    Broder, C.C.2    Doms, R.W.3    Moss, B.4
  • 58
    • 1542615646 scopus 로고    scopus 로고
    • Identifying epitopes of HIV-1 that induce protective antibodies
    • Zolla-Pazner S. 2004. Identifying epitopes of HIV-1 that induce protective antibodies. Nat. Rev. Immunol. 4:199-210. http://dx.doi.org/10.1038 /nri1307.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 199-210
    • Zolla-Pazner, S.1
  • 60
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS. 2006. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439:38-44. http://dx.doi.org/10.1038/nature04322.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 61
    • 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. 2007. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 315: 843-848. http://dx.doi.org/10.1126/science.1135710.
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4


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