메뉴 건너뛰기




Volumn 307, Issue 2, 2003, Pages 255-265

Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins

Author keywords

Glycoprotein structure; Hepatitis C virus envelope glycoproteins; Pestivirus; Proteomics; Viral fusion proteins; Virus evolution

Indexed keywords

HYBRID PROTEIN; MEMBRANE PROTEIN; PROTEIN PRECURSOR; PROTEIN PRM; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

EID: 0037444329     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0042-6822(02)00065-X     Document Type: Article
Times cited : (118)

References (38)
  • 1
    • 0032989258 scopus 로고    scopus 로고
    • Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E
    • Allison S.L., Stiasny K., Stadler K., Mandl C.W., Heinz F.X. Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E. J. Virol. 73:1999;5605-5612.
    • (1999) J. Virol. , vol.73 , pp. 5605-5612
    • Allison, S.L.1    Stiasny, K.2    Stadler, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 2
    • 0023718983 scopus 로고
    • Secondary structure prediction: Combination of three different methods
    • Biou V., Gibrat J.F., Levin J.M., Robson B., Garnier J. Secondary structure prediction combination of three different methods. Protein Eng. 2:1988;185-191.
    • (1988) Protein Eng. , vol.2 , pp. 185-191
    • Biou, V.1    Gibrat, J.F.2    Levin, J.M.3    Robson, B.4    Garnier, J.5
  • 3
    • 0036199093 scopus 로고    scopus 로고
    • Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions
    • Carneiro F.A., Bianconi M.L., Weissmuller G., Stauffer F., Da Poian A.T. Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions. J. Virol. 76:2002;3756-3764.
    • (2002) J. Virol. , vol.76 , pp. 3756-3764
    • Carneiro, F.A.1    Bianconi, M.L.2    Weissmuller, G.3    Stauffer, F.4    Da Poian, A.T.5
  • 4
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr C.M., Kim P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:1993;823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 5
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell. 89:1997;263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 6
    • 0036146271 scopus 로고    scopus 로고
    • Analysis of the C-terminal membrane anchor domains of hepatitis C virus glycoproteins E1 and E2: Toward a topological model
    • Charloteaux B., Lins L., Moereels H., Brasseur R. Analysis of the C-terminal membrane anchor domains of hepatitis C virus glycoproteins E1 and E2 toward a topological model. J. Virol. 76:2002;1944-1958.
    • (2002) J. Virol. , vol.76 , pp. 1944-1958
    • Charloteaux, B.1    Lins, L.2    Moereels, H.3    Brasseur, R.4
  • 7
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou P.Y., Fasman G.D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry. 13:1974;211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 8
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • Crill W.D., Roehrig J.T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75:2001;7769-7773.
    • (2001) J. Virol. , vol.75 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 10
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher W.R. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell. 50:1987;327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 11
    • 0001846607 scopus 로고    scopus 로고
    • Similar structural models of the transmembrane glycoproteins of Ebola and avian sarcoma viruses
    • Gallaher W.R. Similar structural models of the transmembrane glycoproteins of Ebola and avian sarcoma viruses. Cell. 85:1996;1-2.
    • (1996) Cell , vol.85 , pp. 1-2
    • Gallaher, W.R.1
  • 13
    • 3142545672 scopus 로고    scopus 로고
    • The viral transmembrane superfamily: Possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor
    • Gallaher W.R., DiSimone C., Buchmeier M.J. The viral transmembrane superfamily possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor. BMC Microbiol. 1:2001;1.
    • (2001) BMC Microbiol. , vol.1 , pp. 1
    • Gallaher, W.R.1    DiSimone, C.2    Buchmeier, M.J.3
  • 14
    • 0033819541 scopus 로고    scopus 로고
    • E2-p7 region of the bovine viral diarrhea virus polyprotein: Processing and functional studies
    • Harada T., Tautz N., Thiel H.J. E2-p7 region of the bovine viral diarrhea virus polyprotein processing and functional studies. J. Virol. 74:2000;9498-9506.
    • (2000) J. Virol. , vol.74 , pp. 9498-9506
    • Harada, T.1    Tautz, N.2    Thiel, H.J.3
  • 16
    • 0000207681 scopus 로고
    • TMbase - A database of membrane-spanning segments
    • Hofmann, K. Stoffel, 1993. TMbase - a database of membrane-spanning segments. Biol. Chem. Hoppe-Seyler 374, 166.
    • (1993) Biol. Chem. Hoppe-Seyler , pp. 374
    • Hofmann1    Stoffel, K.2
  • 17
    • 0030704752 scopus 로고    scopus 로고
    • Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors
    • Hulst M.M., Moormann R.J. Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus E(rns) and E2 interact with different receptors. J. Gen. Virol. 78:1997;2779-2787.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2779-2787
    • Hulst, M.M.1    Moormann, R.J.2
  • 20
    • 0037085304 scopus 로고    scopus 로고
    • Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop
    • Langeduk J.P. Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop. J. Biol. Chem. 277:2002;5308-5314.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5308-5314
    • Langeduk, J.P.1
  • 21
    • 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 M.W., Navaza J., Fuller S.D., Wengler G., Rey F.A. The fusion glycoprotein shell of Semliki Forest virus an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell. 105:2001;137-148.
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6    Rey, F.A.7
  • 23
    • 0033818910 scopus 로고    scopus 로고
    • Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site
    • Mandl C.W., Allison S.L., Holzmann H., Meixner T., Heinz F.X. Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site. J. Virol. 74:2000;9601-9609.
    • (2000) J. Virol. , vol.74 , pp. 9601-9609
    • Mandl, C.W.1    Allison, S.L.2    Holzmann, H.3    Meixner, T.4    Heinz, F.X.5
  • 24
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W.R., Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 25
    • 0025323617 scopus 로고
    • Characterization of a putative cellular receptor for HIV-1 transmembrane glycoprotein using synthetic peptides
    • Qureshi N., Coy D., Garry R., Henderson L.A. Characterization of a putative cellular receptor for HIV-1 transmembrane glycoprotein using synthetic peptides. AIDS. 4:1990;553-558.
    • (1990) AIDS , vol.4 , pp. 553-558
    • Qureshi, N.1    Coy, D.2    Garry, R.3    Henderson, L.A.4
  • 26
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey F.A., Heinz F.X., Mandl C., Kunz C., Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature. 375:1995;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
    • 0036309399 scopus 로고    scopus 로고
    • Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers
    • Roche S., Gaudin Y. Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers. Virology. 297:2002;128-135.
    • (2002) Virology , vol.297 , pp. 128-135
    • Roche, S.1    Gaudin, Y.2
  • 28
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith T.F., Waterman M.S. Identification of common molecular subsequences. J. Mol. Biol. 147:1981;195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 29
    • 0030764780 scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler K., Allison S.L., Schalich J., Heinz F.X. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 71:1981;8475-8481.
    • (1981) J. Virol. , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 30
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • Suarez T., Gallaher W.R., Agirre A., Goni F.M., Nieva J.L. Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein putative role during viral fusion. J. Virol. 74:2000;8038-8047.
    • (2000) J. Virol. , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 31
    • 0026025737 scopus 로고
    • Variable and hypervariable domains are found in the regions of HCV corresponding to the flavivirus envelope and NS1 proteins and the pestivirus envelope glycoproteins
    • Weiner A.J., Brauer M.J., Rosenblatt J., Richman K.H., Tung J., Crawford K., Bonino F., Saracco G., Choo Q.L., Houghton M., Han J.H. Variable and hypervariable domains are found in the regions of HCV corresponding to the flavivirus envelope and NS1 proteins and the pestivirus envelope glycoproteins. Virology. 180:1991;842-848.
    • (1991) Virology , vol.180 , pp. 842-848
    • Weiner, A.J.1    Brauer, M.J.2    Rosenblatt, J.3    Richman, K.H.4    Tung, J.5    Crawford, K.6    Bonino, F.7    Saracco, G.8    Choo, Q.L.9    Houghton, M.10    Han, J.H.11
  • 32
    • 0032214714 scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn W., Carfi A., Lee K.H., Skehel J.J., Wiley D.C. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell. 2:1985;605-616.
    • (1985) Mol. Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 33
    • 0029878665 scopus 로고    scopus 로고
    • The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide
    • Weissenhorn W., Wharton S.A., Calder L.J., Earl P.L., Moss B., Aliprandis E., Skehel J.J., Wiley D.C. The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO J. 15:1996;1507-1514.
    • (1996) EMBO J. , vol.15 , pp. 1507-1514
    • Weissenhorn, W.1    Wharton, S.A.2    Calder, L.J.3    Earl, P.L.4    Moss, B.5    Aliprandis, E.6    Skehel, J.J.7    Wiley, D.C.8
  • 34
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild C., Greenwell T., Matthews T. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res. Hum. Retro. 9:1993;1051-1053.
    • (1993) AIDS Res. Hum. Retro. , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 35
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild C.T., Shugars D.C., Greenwell T.K., McDanal C.B., Matthews T.J. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA. 91:1994;9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 36
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson I.A., Skehel J.J., Wiley D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature. 289:1981;366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 37
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:1996;842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.