메뉴 건너뛰기




Volumn 277, Issue , 2006, Pages 57-65

Entry functions and antigenic structure of flavivirus envelope proteins

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 33947493080     PISSN: 15282511     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (4)

References (35)
  • 1
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • Allison SL, Schalich J, Stiasny K, Mandl CW, Kunz C, Heinz FX 1995 Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J Virol 69:695-700
    • (1995) J Virol , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 2
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • Allison SL, Schalich J, Stiasny K, Mandl CW, Heinz FX 2001 Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J Virol 75:4268-4275
    • (2001) J Virol , vol.75 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 4
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • Bressanelli S, Stiasny K, Allison SL et al 2004 Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J 23:728-738
    • (2004) EMBO J , vol.23 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3
  • 5
    • 0024557418 scopus 로고
    • Antigenic relationships between flaviviruses as determined by cross-neutralization tests with polyclonal antisera
    • Calisher CH, Karabatsos N, Dalrymple JM et al 1989 Antigenic relationships between flaviviruses as determined by cross-neutralization tests with polyclonal antisera. J Gen Virol 70:37-43
    • (1989) J Gen Virol , vol.70 , pp. 37-43
    • Calisher, C.H.1    Karabatsos, N.2    Dalrymple, J.M.3
  • 6
    • 0034732136 scopus 로고    scopus 로고
    • Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system
    • Corver J, Ortiz A, Allison SL, Schalich J, Heinz FX, Wilschut J 2000 Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system. Virology 269:37-46
    • (2000) Virology , vol.269 , pp. 37-46
    • Corver, J.1    Ortiz, A.2    Allison, S.L.3    Schalich, J.4    Heinz, F.X.5    Wilschut, J.6
  • 9
    • 0035265843 scopus 로고    scopus 로고
    • Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus
    • Ferlenghi I, Clarke M, Ruttan T et al 2001 Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus. Mol Cell 7:593-602
    • (2001) Mol Cell , vol.7 , pp. 593-602
    • Ferlenghi, I.1    Clarke, M.2    Ruttan, T.3
  • 10
    • 0035900003 scopus 로고    scopus 로고
    • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process
    • Gallo SA, Puri A, Blumenthal R 2001 HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process. Biochemistry 40:12231-12236
    • (2001) Biochemistry , vol.40 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 11
    • 56249107362 scopus 로고    scopus 로고
    • Heinz FX, Collet MS, Purcell RH et al 2003 Family Flaviviridae. In: Van Regenmortel MH, Fauquet CM, Bishop DHL et al (eds) Virus taxonomy. Seventh report of the international committee on taxonomy of viruses. Academic Press, San Diego p 859-878
    • Heinz FX, Collet MS, Purcell RH et al 2003 Family Flaviviridae. In: Van Regenmortel MH, Fauquet CM, Bishop DHL et al (eds) Virus taxonomy. Seventh report of the international committee on taxonomy of viruses. Academic Press, San Diego p 859-878
  • 13
    • 0033649526 scopus 로고    scopus 로고
    • Specific roles for lipids in virus fusion and exit. Examples from the alphaviruses
    • Kielian M, Chatterjee PK, Gibbons DL, Lu YE 2000 Specific roles for lipids in virus fusion and exit. Examples from the alphaviruses. Subcell Biochem 34:409-455
    • (2000) Subcell Biochem , vol.34 , pp. 409-455
    • Kielian, M.1    Chatterjee, P.K.2    Gibbons, D.L.3    Lu, Y.E.4
  • 14
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • Kuhn RJ, Zhang W, Rossmann MG et al 2002 Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108:717-725
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3
  • 15
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of Semliki Forest virus. An icosahedral assembly primed for fusogenic activation at endosomal pH
    • Lescar J, Roussel A, Wien MW et al 2001 The fusion glycoprotein shell of Semliki Forest virus. An icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 105:137-148
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3
  • 16
    • 1542676405 scopus 로고    scopus 로고
    • Molecular biology of flaviviruses
    • Lindenbach BD, Rice CM 2003 Molecular biology of flaviviruses. Adv Virus Res 59:23-61
    • (2003) Adv Virus Res , vol.59 , pp. 23-61
    • Lindenbach, B.D.1    Rice, C.M.2
  • 18
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan GB, Markosyan RM, Hemmati H, Delmedico MK, Lambert DM, Cohen FS 2000 Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J Cell Biol 151:413-423
    • (2000) J Cell Biol , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 19
  • 20
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y, Ogata S, Clements D, Harrison SC 2004 Structure of the dengue virus envelope protein after membrane fusion. Nature 427:313-319
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 21
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • Modis Y, Ogata S, Clements D, Harrison SC 2005 Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J Virol 79:1223-1231
    • (2005) J Virol , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 23
    • 21044448356 scopus 로고    scopus 로고
    • Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus
    • Oliphant T, Engle M, Nybakken GE et al 2005 Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus. Nat Med 11:522-530
    • (2005) Nat Med , vol.11 , pp. 522-530
    • Oliphant, T.1    Engle, M.2    Nybakken, G.E.3
  • 24
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC 1995 The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375:291-298
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 25
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler K, Allison SL, Schalich J, Heinz FX 1997 Proteolytic activation of tick-borne encephalitis virus by furin. J Virol 71:8475-8481
    • (1997) J Virol , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 26
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • Stiasny K, Allison SL, Marchler-Bauer A, Kunz C, Heinz FX 1996 Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J Virol 70:8142-8147
    • (1996) J Virol , vol.70 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 27
    • 0034903691 scopus 로고    scopus 로고
    • Role of metastability and acidic pH in membrane fusion by tick-borne encephalitis virus
    • Stiasny K, Allison SL, Mandl CW, Heinz FX 2001 Role of metastability and acidic pH in membrane fusion by tick-borne encephalitis virus. J Virol 75:7392-7398
    • (2001) J Virol , vol.75 , pp. 7392-7398
    • Stiasny, K.1    Allison, S.L.2    Mandl, C.W.3    Heinz, F.X.4
  • 28
    • 0036198006 scopus 로고    scopus 로고
    • Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH
    • Stiasny K, Allison SL, Schalich J, Heinz FX 2002 Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH. J Virol 76:3784-3790
    • (2002) J Virol , vol.76 , pp. 3784-3790
    • Stiasny, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 29
    • 0038759003 scopus 로고    scopus 로고
    • Involvement of lipids in different steps of the flavivirus fusion mechanism
    • Stiasny K, Koessl C, Heinz FX 2003 Involvement of lipids in different steps of the flavivirus fusion mechanism. J Virol 77:7856-7862
    • (2003) J Virol , vol.77 , pp. 7856-7862
    • Stiasny, K.1    Koessl, C.2    Heinz, F.X.3
  • 30
    • 1542347705 scopus 로고    scopus 로고
    • Characterization of a membraneassociated trimeric low-pH-induced form of the class II viral fusion protein E from tickborne encephalitis virus and its crystallization
    • Stiasny K, Bressanelli S, Lepault J, Rey FA, Heinz FX 2004 Characterization of a membraneassociated trimeric low-pH-induced form of the class II viral fusion protein E from tickborne encephalitis virus and its crystallization. J Virol 78:3178-3183
    • (2004) J Virol , vol.78 , pp. 3178-3183
    • Stiasny, K.1    Bressanelli, S.2    Lepault, J.3    Rey, F.A.4    Heinz, F.X.5
  • 31
    • 56249103262 scopus 로고    scopus 로고
    • Structural and functional dissection of the flavivirus membrane fusion pathway
    • Submitted
    • Stiasny K, Koessl C, Lepault J, Rey FA, Heinz FX 2006a Structural and functional dissection of the flavivirus membrane fusion pathway. Submitted
    • (2006)
    • Stiasny, K.1    Koessl, C.2    Lepault, J.3    Rey, F.A.4    Heinz, F.X.5
  • 32
    • 84959110586 scopus 로고    scopus 로고
    • Cryptic nature of the dominant flavivirus cross-reactive antigenic site
    • Submitted
    • Stiasny K, Kiermayr S, Holzmann H, Heinz FX 2006b Cryptic nature of the dominant flavivirus cross-reactive antigenic site. Submitted
    • (2006)
    • Stiasny, K.1    Kiermayr, S.2    Holzmann, H.3    Heinz, F.X.4
  • 33
    • 0242574743 scopus 로고    scopus 로고
    • Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
    • Zhang W, Chipman PR, Corver J et al 2003a Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat Struct Biol 10:907-912
    • (2003) Nat Struct Biol , vol.10 , pp. 907-912
    • Zhang, W.1    Chipman, P.R.2    Corver, J.3
  • 34
    • 0038201461 scopus 로고    scopus 로고
    • Structures of immature flavivirus particles
    • Zhang Y, Corver J, Chipman PR et al 2003b Structures of immature flavivirus particles. EMBO J 22:2604-2613
    • (2003) EMBO J , vol.22 , pp. 2604-2613
    • Zhang, Y.1    Corver, J.2    Chipman, P.R.3
  • 35
    • 4444338894 scopus 로고    scopus 로고
    • Conformational changes of the flavivirus E glycoprotein
    • Zhang Y, Zhang W, Ogata S et al 2004 Conformational changes of the flavivirus E glycoprotein. Structure (Camb) 12:1607-1618
    • (2004) Structure (Camb) , vol.12 , pp. 1607-1618
    • Zhang, Y.1    Zhang, W.2    Ogata, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.