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Volumn 85, Issue 11, 2011, Pages 5644-5650

Activation of the alphavirus spike protein is suppressed by bound E3

Author keywords

[No Author keywords available]

Indexed keywords

FURIN; GLYCOPROTEIN E1; LIPOSOME; PROTEIN E3; PROTEIN P62; PROTEINASE K; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS SPIKE PROTEIN;

EID: 79956155459     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00130-11     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 0018126813 scopus 로고
    • Evidence for an autoprotease activity of Sindbis virus capsid protein
    • Aliperti, G., and M. J. Schlesinger. 1978. Evidence for an autoprotease activity of Sindbis virus capsid protein. Virology 90:366-369.
    • (1978) Virology , vol.90 , pp. 366-369
    • Aliperti, G.1    Schlesinger, M.J.2
  • 2
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • Allison, S. L., et al. 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
  • 3
    • 0035823046 scopus 로고    scopus 로고
    • Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin
    • Band, A. M., J. Maatta, L. Kaariainen, and E. Kuismanen. 2001. Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin. FEBS Lett. 505:118-124.
    • (2001) FEBS Lett , vol.505 , pp. 118-124
    • Band, A.M.1    Maatta, J.2    Kaariainen, L.3    Kuismanen, E.4
  • 4
    • 14744292350 scopus 로고
    • Semliki Forest virus expression system: production of conditionally infectious recombinant particles
    • Berglund, P., et al. 1993. Semliki Forest virus expression system: production of conditionally infectious recombinant particles. Biotechnology 11:916-920.
    • (1993) Biotechnology , vol.11 , pp. 916-920
    • Berglund, P.1
  • 5
    • 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., J. M. Wahlberg, H. Garoff, and J. Wilschut. 1993. Membrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein. EMBO J. 12:693-701.
    • (1993) EMBO J , vol.12 , pp. 693-701
    • Bron, R.1    Wahlberg, J.M.2    Garoff, H.3    Wilschut, J.4
  • 6
    • 0028919758 scopus 로고
    • Nucleocapsid and glycoprotein organization in an enveloped virus
    • Cheng, R. H., et al. 1995. Nucleocapsid and glycoprotein organization in an enveloped virus. Cell 80:621-630.
    • (1995) Cell , vol.80 , pp. 621-630
    • Cheng, R.H.1
  • 7
    • 0023775458 scopus 로고
    • Dissection of Semliki Forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells
    • de Curtis, I., and K. Simons. 1988. Dissection of Semliki Forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells. Proc. Natl. Acad. Sci. U. S. A. 85:8052-8056.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 8052-8056
    • de Curtis, I.1    Simons, K.2
  • 8
    • 0036462411 scopus 로고    scopus 로고
    • pH homeostasis of cellular organelles
    • Demaurex, N. 2002. pH homeostasis of cellular organelles. News Physiol. Sci. 17:1-5.
    • (2002) News Physiol. Sci. , vol.17 , pp. 1-5
    • Demaurex, N.1
  • 9
    • 0031941594 scopus 로고    scopus 로고
    • Mechanism of acidification of the trans-Golgi network (TGN) In situ measurements of pH using retrieval of TGN38 and furin from the cell surface
    • Demaurex, N., W. Furuya, S. D'Souza, J. S. Bonifacino, and S. Grinstein. 1998. Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface. J. Biol. Chem. 273:2044-2051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2044-2051
    • Demaurex, N.1    Furuya, W.2    D'Souza, S.3    Bonifacino, J.S.4    Grinstein, S.5
  • 11
    • 0033836520 scopus 로고    scopus 로고
    • The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
    • Gagescu, R., et al. 2000. The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Mol. Biol. Cell 11:2775-2791.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2775-2791
    • Gagescu, R.1
  • 12
    • 0019300295 scopus 로고
    • Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins
    • Garoff, H., A. M. Frischauf, K. Simons, H. Lehrach, and H. Delius. 1980. Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins. Nature 288:236-241.
    • (1980) Nature , vol.288 , pp. 236-241
    • Garoff, H.1    Frischauf, A.M.2    Simons, K.3    Lehrach, H.4    Delius, H.5
  • 13
    • 0025144560 scopus 로고
    • The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
    • Garoff, H., D. Huylebroeck, A. Robinson, U. Tillman, and P. Liljestrom. 1990. The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation. J. Cell Biol. 111:867-876.
    • (1990) J. Cell Biol. , vol.111 , pp. 867-876
    • Garoff, H.1    Huylebroeck, D.2    Robinson, A.3    Tillman, U.4    Liljestrom, P.5
  • 14
    • 0018177156 scopus 로고
    • Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro
    • Garoff, H., K. Simons, and B. Dobberstein. 1978. Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro. J. Mol. Biol. 124:587-600.
    • (1978) J. Mol. Biol. , vol.124 , pp. 587-600
    • Garoff, H.1    Simons, K.2    Dobberstein, B.3
  • 15
    • 0016285594 scopus 로고
    • Isolation and characterization of the membrane proteins of Semliki Forest virus
    • Garoff, H., K. Simons, and O. Renkonen. 1974. Isolation and characterization of the membrane proteins of Semliki Forest virus. Virology 61:493-504.
    • (1974) Virology , vol.61 , pp. 493-504
    • Garoff, H.1    Simons, K.2    Renkonen, O.3
  • 16
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons, D. L., et al. 2004. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427:320-325.
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1
  • 17
    • 0028152964 scopus 로고
    • Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein
    • Klimjack, M. R., S. Jeffrey, and M. Kielian. 1994. Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein. J. Virol. 68:6940-6946.
    • (1994) J. Virol. , vol.68 , pp. 6940-6946
    • Klimjack, M.R.1    Jeffrey, S.2    Kielian, M.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 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., 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
  • 20
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • Li, L., J. Jose, Y. Xiang, R. J. Kuhn, and M. G. Rossmann. 2010. Structural changes of envelope proteins during alphavirus fusion. Nature 468:705-708.
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 21
    • 0025012156 scopus 로고
    • Spike protein oligomerization control of Semliki Forest virus fusion
    • Lobigs, M., J. M. Wahlberg, and H. Garoff. 1990. Spike protein oligomerization control of Semliki Forest virus fusion. J. Virol. 64:5214-5218.
    • (1990) J. Virol. , vol.64 , pp. 5214-5218
    • Lobigs, M.1    Wahlberg, J.M.2    Garoff, H.3
  • 22
    • 0025003156 scopus 로고
    • Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1
    • Lobigs, M., H. X. Zhao, and H. Garoff. 1990. Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1. J. Virol. 64:4346-4355.
    • (1990) J. Virol. , vol.64 , pp. 4346-4355
    • Lobigs, M.1    Zhao, H.X.2    Garoff, H.3
  • 23
    • 0020724144 scopus 로고
    • Penetration of Semliki Forest virus from acidic prelysosomal vacuoles
    • Marsh, M., E. Bolzau, and A. Helenius. 1983. Penetration of Semliki Forest virus from acidic prelysosomal vacuoles. Cell 32:931-940.
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 24
    • 0023275581 scopus 로고
    • Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease
    • Melancon, P., and H. Garoff. 1987. Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease. J. Virol. 61:1301-1309.
    • (1987) J. Virol. , vol.61 , pp. 1301-1309
    • Melancon, P.1    Garoff, H.2
  • 25
    • 0029953199 scopus 로고    scopus 로고
    • Assembly of the Sindbis virus spike protein complex
    • Mulvey, M., and D. T. Brown. 1996. Assembly of the Sindbis virus spike protein complex. Virology 219:125-132.
    • (1996) Virology , vol.219 , pp. 125-132
    • Mulvey, M.1    Brown, D.T.2
  • 26
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 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
  • 27
    • 0026567676 scopus 로고
    • Membrane fusion process of Semliki Forest virus II. Cleavage-dependent reorganization of the spike protein complex controls virus entry
    • Salminen, A., J. M. Wahlberg, M. Lobigs, P. Liljestrom, and H. Garoff. 1992. Membrane fusion process of Semliki Forest virus. II. Cleavage-dependent reorganization of the spike protein complex controls virus entry. J. Cell Biol. 116:349-357.
    • (1992) J. Cell Biol. , vol.116 , pp. 349-357
    • Salminen, A.1    Wahlberg, J.M.2    Lobigs, M.3    Liljestrom, P.4    Garoff, H.5
  • 28
    • 0029011658 scopus 로고
    • Communication of post-Golgi elements with early endocytic pathway: regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor
    • Sariola, M., J. Saraste, and E. Kuismanen. 1995. Communication of post-Golgi elements with early endocytic pathway: regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor. J. Cell Sci. 108:2465-2475.
    • (1995) J. Cell Sci. , vol.108 , pp. 2465-2475
    • Sariola, M.1    Saraste, J.2    Kuismanen, E.3
  • 29
    • 0037334555 scopus 로고    scopus 로고
    • Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion
    • Sjöberg, M., and H. Garoff. 2003. Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion. J. Virol. 77:3441-3450.
    • (2003) J. Virol. , vol.77 , pp. 3441-3450
    • Sjöberg, M.1    Garoff, H.2
  • 30
    • 84884843054 scopus 로고    scopus 로고
    • Growth of Semliki Forest virus
    • J. E. Celis (ed.), 3rd ed. Academic Press, New York NY
    • Sjöberg, E. M., and H. Garoff. 2006. Growth of Semliki Forest virus, p. 419-423. In J. E. Celis (ed.), Cell biology: a laboratory handbook, 3rd ed., vol. 1. Academic Press, New York, NY.
    • (2006) Cell biology: a laboratory handbook , vol.1 , pp. 419-423
    • Sjöberg, E.M.1    Garoff, H.2
  • 31
    • 0017366499 scopus 로고
    • Envelopments of Sindbis virus: synthesis and organization of proteins in cells infected with wild type and maturationdefective mutants
    • Smith, J. F., and D. T. Brown. 1977. Envelopments of Sindbis virus: synthesis and organization of proteins in cells infected with wild type and maturationdefective mutants. J. Virol. 22:662-678.
    • (1977) J. Virol. , vol.22 , pp. 662-678
    • Smith, J.F.1    Brown, D.T.2
  • 32
    • 0028088152 scopus 로고
    • The alphaviruses: gene expression, replication, and evolution
    • Strauss, J. H., and E. G. Strauss. 1994. The alphaviruses: gene expression, replication, and evolution. Microbiol. Rev. 58:491-562.
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 33
    • 0024455501 scopus 로고
    • The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation
    • Wahlberg, J. M., W. A. Boere, and H. Garoff. 1989. The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation. J. Virol. 63:4991-4997.
    • (1989) J. Virol. , vol.63 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.2    Garoff, H.3
  • 34
    • 0026495818 scopus 로고
    • Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein
    • Wahlberg, J. M., R. Bron, J. Wilschut, and H. Garoff. 1992. Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein. J. Virol. 66:7309-7318.
    • (1992) J. Virol. , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3    Garoff, H.4
  • 35
    • 0026584727 scopus 로고
    • Membrane fusion process of Semliki Forest virus I. Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells
    • Wahlberg, J. M., and H. Garoff. 1992. Membrane fusion process of Semliki Forest virus. I. Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells. J. Cell Biol. 116:339-348.
    • (1992) J. Cell Biol. , vol.116 , pp. 339-348
    • Wahlberg, J.M.1    Garoff, H.2
  • 36
    • 0018395285 scopus 로고
    • Two small virus-specific polypeptides are produced during infection with Sindbis virus
    • Welch, W. J., and B. M. Sefton. 1979. Two small virus-specific polypeptides are produced during infection with Sindbis virus. J. Virol. 29:1186-1195.
    • (1979) J. Virol. , vol.29 , pp. 1186-1195
    • Welch, W.J.1    Sefton, B.M.2
  • 37
    • 0024327726 scopus 로고
    • Cell-associated West Nile flavivirus is covered with E+ pre-M protein heterodimers which are destroyed and reorganized by proteolytic cleavage during virus release
    • Wengler, G., and G. Wengler. 1989. Cell-associated West Nile flavivirus is covered with E+ pre-M protein heterodimers which are destroyed and reorganized by proteolytic cleavage during virus release. J. Virol. 63:2521-2526.
    • (1989) J. Virol. , vol.63 , pp. 2521-2526
    • Wengler, G.1    Wengler, G.2
  • 38
    • 0001696895 scopus 로고
    • pH-dependent fusion between the Semliki Forest virus membrane and liposomes
    • White, J., and A. Helenius. 1980. pH-dependent fusion between the Semliki Forest virus membrane and liposomes. Proc. Natl. Acad. Sci. U. S. A. 77:3273-3277.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 3273-3277
    • White, J.1    Helenius, A.2
  • 39
    • 78649817910 scopus 로고    scopus 로고
    • Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
    • Voss, J. E., et al. 2010. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature 468:709-712.
    • (2010) Nature , vol.468 , pp. 709-712
    • Voss, J.E.1
  • 40
    • 70450208515 scopus 로고    scopus 로고
    • Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion
    • Yu, I. M., et al. 2009. Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J. Virol. 83:12101-12107.
    • (2009) J. Virol. , vol.83 , pp. 12101-12107
    • Yu, I.M.1
  • 41
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu, I. M., et al. 2008. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319:1834-1837.
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.M.1
  • 42
    • 0036827856 scopus 로고    scopus 로고
    • Placement of the structural proteins in Sindbis virus
    • Zhang, W., et al. 2002. Placement of the structural proteins in Sindbis virus. J. Virol. 76:11645-11658.
    • (2002) J. Virol. , vol.76 , pp. 11645-11658
    • Zhang, W.1
  • 43
    • 0038201461 scopus 로고    scopus 로고
    • Structures of immature flavivirus particles
    • Zhang, Y., et al. 2003. Structures of immature flavivirus particles. EMBO J. 22:2604-2613.
    • (2003) EMBO J , vol.22 , pp. 2604-2613
    • Zhang, Y.1
  • 44
    • 78449249672 scopus 로고    scopus 로고
    • In vitro and in vivo studies identify important features of dengue virus pr-E protein interactions
    • Zheng, A., M. Umashankar, and M. Kielian. 2010. In vitro and in vivo studies identify important features of dengue virus pr-E protein interactions. PLoS Pathog. 6:e1001157.
    • (2010) PLoS Pathog , vol.6
    • Zheng, A.1    Umashankar, M.2    Kielian, M.3
  • 45
    • 0019216782 scopus 로고
    • Formation of the Semliki Forest virus membrane glycoprotein complexes in the infected cell
    • Ziemiecki, A., H. Garoff, and K. Simons. 1980. Formation of the Semliki Forest virus membrane glycoprotein complexes in the infected cell. J. Gen. Virol. 50:111-123.
    • (1980) J. Gen. Virol. , vol.50 , pp. 111-123
    • Ziemiecki, A.1    Garoff, H.2    Simons, K.3
  • 46
    • 0017803335 scopus 로고
    • Subunit composition of the membrane glycoprotein complex of Semliki Forest virus
    • Ziemiecki, A., and H. Garofff. 1978. Subunit composition of the membrane glycoprotein complex of Semliki Forest virus. J. Mol. Biol. 122:259-269.
    • (1978) J. Mol. Biol. , vol.122 , pp. 259-269
    • Ziemiecki, A.1    Garofff, H.2


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