메뉴 건너뛰기




Volumn 41, Issue 5, 2011, Pages 1159-1163

Molecular mechanisms of flavivirus membrane fusion

Author keywords

Flavivirus; Fusion trigger; Histidine; Membrane fusion; Viral fusion protein

Indexed keywords

E PROTEIN; HISTIDINE; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN; VIRUS PROTEIN;

EID: 84855225539     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-009-0370-4     Document Type: Review
Times cited : (93)

References (39)
  • 1
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • DOI 10.1128/JVI.75.9.4268-4275.2001
    • 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 (Pubitemid 32410139)
    • (2001) Journal of Virology , vol.75 , Issue.9 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 3
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • DOI 10.1038/sj.emboj.7600064
    • Bressanelli S, Stiasny K, Allison SL, Stura EA, Duquerroy S, Lescar J, Heinz FX, Rey FA (2004) Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J 23:728-738 (Pubitemid 38425440)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3    Stura, E.A.4    Duquerroy, S.5    Lescar, J.6    Heinz, F.X.7    Rey, F.A.8
  • 6
    • 0034732136 scopus 로고    scopus 로고
    • Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system
    • DOI 10.1006/viro.1999.0172
    • 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 (Pubitemid 30183167)
    • (2000) Virology , vol.269 , Issue.1 , pp. 37-46
    • Corver, J.1    Ortiz, A.2    Allison, S.L.3    Schalich, J.4    Heinz, F.X.5    Wilschut, J.6
  • 9
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz R, Stiasny K, Heinz FX (2008) Identification of specific histidines as pH sensors in flavivirus membrane fusion. J Cell Biol 183:353-361
    • (2008) J Cell Biol , vol.183 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 10
    • 35348925573 scopus 로고    scopus 로고
    • Flaviviruses
    • Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (eds), 5th edn. Lippincott, Philadelphia
    • Gubler D, Kuno G, Markhoff L (2006) Flaviviruses. In: Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (eds) Fields virology, 5th edn. Lippincott, Philadelphia, pp 1153-1252
    • (2006) Fields Virology , pp. 1153-1252
    • Gubler, D.1    Kuno, G.2    Markhoff, L.3
  • 11
    • 55949125587 scopus 로고    scopus 로고
    • The pH sensor for flavivirus membrane fusion
    • Harrison SC (2008a) The pH sensor for flavivirus membrane fusion. J Cell Biol 183:177-179
    • (2008) J Cell Biol , vol.183 , pp. 177-179
    • Harrison, S.C.1
  • 13
    • 33749266195 scopus 로고    scopus 로고
    • The role of histidine residues in low-pH-mediated viral membrane fusion
    • DOI 10.1016/j.str.2006.07.011, PII S096921260600356X
    • Kampmann T, Mueller DS, Mark AE, Young PR, Kobe B (2006) The role of histidine residues in low-pH-mediated viral membrane fusion. Structure 14:1481-1487 (Pubitemid 44486813)
    • (2006) Structure , vol.14 , Issue.10 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5
  • 15
    • 29144497159 scopus 로고    scopus 로고
    • Class II virus membrane fusion proteins
    • DOI 10.1016/j.virol.2005.09.036, PII S0042682205006008
    • Kielian M (2006) Class II virus membrane fusion proteins. Virology 344:38-47 (Pubitemid 41814448)
    • (2006) Virology , vol.344 , Issue.1 , pp. 38-47
    • Kielian, M.1
  • 16
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • DOI 10.1038/nrmicro1326, PII N1326
    • Kielian M, Rey FA (2006) Virus membrane-fusion proteins: more than one way to make a hairpin. Nat Rev Microbiol 4:67-76 (Pubitemid 43135288)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.1 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 18
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • DOI 10.1038/nrm2417, PII NRM2417
    • Martens S, McMahon HT (2008) Mechanisms of membrane fusion: disparate players and common principles. Nat Rev Mol Cell Biol 9:543-556 (Pubitemid 351881838)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.7 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 20
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • DOI 10.1038/nature02165
    • Modis Y, Ogata S, Clements D, Harrison SC (2004) Structure of the dengue virus envelope protein after membrane fusion. Nature 427:313-319 (Pubitemid 38133652)
    • (2004) Nature , vol.427 , Issue.6972 , 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
    • DOI 10.1128/JVI.79.2.1223-1231.2005
    • 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 (Pubitemid 40053904)
    • (2005) Journal of Virology , vol.79 , Issue.2 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 22
    • 29144519316 scopus 로고    scopus 로고
    • Poxvirus entry and membrane fusion
    • DOI 10.1016/j.virol.2005.09.037, PII S004268220500601X
    • Moss B (2006) Poxvirus entry and membrane fusion. Virology 344:48-54 (Pubitemid 41814449)
    • (2006) Virology , vol.344 , Issue.1 , pp. 48-54
    • Moss, B.1
  • 25
    • 66149103151 scopus 로고    scopus 로고
    • Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion
    • Nayak V, Dessau M, Kucera K, Anthony K, Ledizet M, Modis Y (2009) Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion. J Virol 83:4338-4344
    • (2009) J Virol , vol.83 , pp. 4338-4344
    • Nayak, V.1    Dessau, M.2    Kucera, K.3    Anthony, K.4    Ledizet, M.5    Modis, Y.6
  • 26
    • 70450162409 scopus 로고    scopus 로고
    • Protonation of individual histidine residues is not required for the pH-dependent entry of West Nile virus: Evaluation of the "histidine- switch" hypothesis
    • doi:10.1128/JVI.01072-09
    • Nelson S, Poddar S, Lin TY, Pierson TC (2009) Protonation of individual histidine residues is not required for the pH-dependent entry of West Nile virus: evaluation of the "histidine-switch" hypothesis. J Virol. doi:10.1128/JVI.01072-09
    • (2009) J Virol.
    • Nelson, S.1    Poddar, S.2    Lin, T.Y.3    Pierson, T.C.4
  • 28
    • 66149140928 scopus 로고    scopus 로고
    • Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein
    • Qin ZL, Zheng Y, Kielian M (2009) Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein. J Virol 83:4670-4677
    • (2009) J Virol , vol.83 , pp. 4670-4677
    • Qin, Z.L.1    Zheng, Y.2    Kielian, M.3
  • 29
    • 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
  • 30
  • 31
    • 33644799064 scopus 로고    scopus 로고
    • Structure and interactions at the viral surface of the envelope protein E1 of semliki forest virus
    • DOI 10.1016/j.str.2005.09.014, PII S0969212605003941
    • Roussel A, Lescar J, Vaney MC, Wengler G, Wengler G, Rey FA (2006) Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus. Structure 14:75-86 (Pubitemid 43350075)
    • (2006) Structure , vol.14 , Issue.1 , pp. 75-86
    • Roussel, A.1    Lescar, J.2    Vaney, M.-C.3    Wengler, G.4    Wengler, G.5    Rey, F.A.6
  • 32
    • 0029888374 scopus 로고    scopus 로고
    • Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
    • Schalich J, Allison SL, Stiasny K, Mandl CW, Kunz C, Heinz FX (1996) Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J Virol 70:4549-4557 (Pubitemid 26187453)
    • (1996) Journal of Virology , vol.70 , Issue.7 , pp. 4549-4557
    • Schalich, J.1    Allison, S.L.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 33
    • 3142510881 scopus 로고    scopus 로고
    • Intracellular and viral membrane fusion: A uniting mechanism
    • DOI 10.1016/j.ceb.2004.06.015, PII S0955067404000845
    • Sollner TH (2004) Intracellular and viral membrane fusion: a uniting mechanism. Curr Opin Cell Biol 16:429-435 (Pubitemid 38903150)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 429-435
    • Sollner, T.H.1
  • 34
    • 33847240145 scopus 로고    scopus 로고
    • Intracellular pH sensors: Design principles and functional significance
    • Srivastava J, Barber DL, Jacobson MP (2007) Intracellular pH sensors: design principles and functional significance. Physiology 22:30-39
    • (2007) Physiology , vol.22 , pp. 30-39
    • Srivastava, J.1    Barber, D.L.2    Jacobson, M.P.3
  • 35
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • DOI 10.1126/science.1093373
    • Stevens J, Corper AL, Basler CF, Taubenberger JK, Palese P, Wilson IA (2004) Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 303:1866-1870 (Pubitemid 38374878)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1866-1870
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5    Wilson, I.A.6
  • 36
    • 33749042583 scopus 로고    scopus 로고
    • Flavivirus membrane fusion
    • DOI 10.1099/vir.0.82210-0
    • Stiasny K, Heinz FX (2006) Flavivirus membrane fusion. J Gen Virol 87:2755-2766 (Pubitemid 44463884)
    • (2006) Journal of General Virology , vol.87 , Issue.10 , pp. 2755-2766
    • Stiasny, K.1    Heinz, F.X.2
  • 37
    • 34248149810 scopus 로고    scopus 로고
    • Virus membrane fusion
    • DOI 10.1016/j.febslet.2007.01.093, PII S0014579307001664, Membrane Trafficking
    • Weissenhorn W, Hinz A, Gaudin Y (2007) Virus membrane fusion. FEBS Lett 581:2150-2155 (Pubitemid 46722604)
    • (2007) FEBS Letters , vol.581 , Issue.11 , pp. 2150-2155
    • Weissenhorn, W.1    Hinz, A.2    Gaudin, Y.3
  • 38
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • DOI 10.1080/10409230802058320, PII 794225034
    • 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 (Pubitemid 351883153)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.