메뉴 건너뛰기




Volumn 89, Issue 9, 2008, Pages 2114-2121

Formation of bovine viral diarrhea virus E1-E2 heterodimers is essential for virus entry and depends on charged residues in the transmembrane domains

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GLYCOPROTEIN E1; GLYCOPROTEIN E2; HETERODIMER; LYSINE; AMINO ACID; GP53, BOVINE VIRAL DIARRHEA VIRUS; HYBRID PROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 52649124704     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.2008/001792-0     Document Type: Article
Times cited : (58)

References (28)
  • 1
    • 0037416146 scopus 로고    scopus 로고
    • Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes
    • Bartosch, B., Dubuisson, J. & Cosset, F. L. (2003). Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes. J Exp Med 197, 633-642.
    • (2003) J Exp Med , vol.197 , pp. 633-642
    • Bartosch, B.1    Dubuisson, J.2    Cosset, F.L.3
  • 2
    • 0023709836 scopus 로고
    • Monoclonal antibodies with neutralizing activity segregate isolates of bovine viral diarrhea virus into groups
    • Bolin, S., Moennig, V., Kelso Gourley, N. E. & Ridpath, J. (1988). Monoclonal antibodies with neutralizing activity segregate isolates of bovine viral diarrhea virus into groups. Arch Virol 99, 117-123.
    • (1988) Arch Virol , vol.99 , pp. 117-123
    • Bolin, S.1    Moennig, V.2    Kelso Gourley, N.E.3    Ridpath, J.4
  • 3
    • 0029589519 scopus 로고
    • Preferential initiation at the second AUG of the measles virus F mRNA: A role for the long untranslated region
    • Cathomen, T., Buchholz, C. J., Spielhofer, P. & Cattaneo, R. (1995). Preferential initiation at the second AUG of the measles virus F mRNA: a role for the long untranslated region. Virology 214, 628-632.
    • (1995) Virology , vol.214 , pp. 628-632
    • Cathomen, T.1    Buchholz, C.J.2    Spielhofer, P.3    Cattaneo, R.4
  • 4
    • 26244462660 scopus 로고    scopus 로고
    • Contribution of the charged residues of hepatitis C virus glycoprotein E2 transmembrane domain to the functions of the E1E2 heterodimer
    • Ciczora, Y., Callens, N., Montpellier, C., Bartosch, B., Cosset, F. L., Op, D. B. & Dubuisson, J. (2005). Contribution of the charged residues of hepatitis C virus glycoprotein E2 transmembrane domain to the functions of the E1E2 heterodimer. J Gen Virol 86, 2793-2798.
    • (2005) J Gen Virol , vol.86 , pp. 2793-2798
    • Ciczora, Y.1    Callens, N.2    Montpellier, C.3    Bartosch, B.4    Cosset, F.L.5    Op, D.B.6    Dubuisson, J.7
  • 5
    • 33847175190 scopus 로고    scopus 로고
    • The transmembrane domains of HCV envelope glycoproteins: Residues involved in E1E2 heterodimerization and involvement of these domains in virus entry
    • Ciczora, Y., Callens, N., Penin, F., Pecheur, E. I. & Dubuisson, J. (2006). The transmembrane domains of HCV envelope glycoproteins: residues involved in E1E2 heterodimerization and involvement of these domains in virus entry. J Virol 81, 2372-2381.
    • (2006) J Virol , vol.81 , pp. 2372-2381
    • Ciczora, Y.1    Callens, N.2    Penin, F.3    Pecheur, E.I.4    Dubuisson, J.5
  • 6
    • 0034031173 scopus 로고    scopus 로고
    • Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins
    • Cocquerel, L., Wychowski, C., Minner, F., Penin, F. & Dubuisson, J. (2000). Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins. J Virol 74, 3623-3633.
    • (2000) J Virol , vol.74 , pp. 3623-3633
    • Cocquerel, L.1    Wychowski, C.2    Minner, F.3    Penin, F.4    Dubuisson, J.5
  • 9
    • 0023238703 scopus 로고
    • Characterization of bovine viral diarrhoea-mucosal disease virus-specific proteins in bovine cells
    • Donis, R. O. & Dubovi, E. J. (1987). Characterization of bovine viral diarrhoea-mucosal disease virus-specific proteins in bovine cells. J Gen Virol 68, 1597-1605.
    • (1987) J Gen Virol , vol.68 , pp. 1597-1605
    • Donis, R.O.1    Dubovi, E.J.2
  • 10
    • 0033992596 scopus 로고    scopus 로고
    • Folding, assembly and subcellular localization of hepatitis C virus glycoproteins
    • Dubuisson, J. (2000). Folding, assembly and subcellular localization of hepatitis C virus glycoproteins. Curr Top Microbiol Immunol 242, 135-148.
    • (2000) Curr Top Microbiol Immunol , vol.242 , pp. 135-148
    • Dubuisson, J.1
  • 11
    • 24644472832 scopus 로고    scopus 로고
    • rns represents an unusual type of membrane anchor
    • rns represents an unusual type of membrane anchor. J Virol 79, 11901-11913.
    • (2005) J Virol , vol.79 , pp. 11901-11913
    • Fetzer, C.1    Tews, B.A.2    Meyers, G.3
  • 12
    • 0025847832 scopus 로고
    • Immunofluorescence studies of biotype-specific expression of bovine viral diarrhoea virus epitopes in infected cells
    • Greiser-Wilke, I., Dittmar, K. E., Liess, B. & Moennig, V. (1991). Immunofluorescence studies of biotype-specific expression of bovine viral diarrhoea virus epitopes in infected cells. J Gen Virol 72, 2015-2019.
    • (1991) J Gen Virol , vol.72 , pp. 2015-2019
    • Greiser-Wilke, I.1    Dittmar, K.E.2    Liess, B.3    Moennig, V.4
  • 13
    • 0034777114 scopus 로고    scopus 로고
    • Localization of viral proteins in cells infected with bovine viral diarrhoea virus
    • Grummer, B., Beer, M., Liebler-Tenorio, E. & Greiser-Wilke, I. (2001). Localization of viral proteins in cells infected with bovine viral diarrhoea virus. J Gen Virol 82, 2597-2605.
    • (2001) J Gen Virol , vol.82 , pp. 2597-2605
    • Grummer, B.1    Beer, M.2    Liebler-Tenorio, E.3    Greiser-Wilke, I.4
  • 14
    • 18144407947 scopus 로고    scopus 로고
    • Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes
    • Hanika, A., Larisch, B., Steinmann, E., Schwegmann-Weßels, C., Herrler, G. & Zimmer, G. (2005). Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes. J Gen Virol 86, 1455-1465.
    • (2005) J Gen Virol , vol.86 , pp. 1455-1465
    • Hanika, A.1    Larisch, B.2    Steinmann, E.3    Schwegmann-Weßels, C.4    Herrler, G.5    Zimmer, G.6
  • 16
    • 0030704752 scopus 로고    scopus 로고
    • rns and E2 interact with different receptors
    • rns and E2 interact with different receptors. J Gen Virol 78, 2779-2787.
    • (1997) J Gen Virol , vol.78 , pp. 2779-2787
    • Hulst, M.M.1    Moormann, R.J.2
  • 17
    • 0034807137 scopus 로고    scopus 로고
    • Interaction of classical swine fever virus with membrane-associated heparan sulfate: Role for virus replication in vivo and virulence
    • Hulst, M. M., Van Gennip, H. G., Vlot, A. C., Schooten, E., De Smit, A. J. & Moormann, R. J. (2001). Interaction of classical swine fever virus with membrane-associated heparan sulfate: role for virus replication in vivo and virulence. J Virol 75, 9585-9595.
    • (2001) J Virol , vol.75 , pp. 9585-9595
    • Hulst, M.M.1    Van Gennip, H.G.2    Vlot, A.C.3    Schooten, E.4    De Smit, A.J.5    Moormann, R.J.6
  • 19
    • 2442667610 scopus 로고    scopus 로고
    • The surface glycoprotein E2 of bovine viral diarrhoea virus contains an intracellular localization signal
    • Köhl, W., Zimmer, G., Greiser-Wilke, I., Haas, L., Moennig, V. & Herrler, G. (2004). The surface glycoprotein E2 of bovine viral diarrhoea virus contains an intracellular localization signal. J Gen Virol 85, 1101-1111.
    • (2004) J Gen Virol , vol.85 , pp. 1101-1111
    • Köhl, W.1    Zimmer, G.2    Greiser-Wilke, I.3    Haas, L.4    Moennig, V.5    Herrler, G.6
  • 20
    • 0031968815 scopus 로고    scopus 로고
    • Functional role of hepatitis C virus chimeric glycoproteins in the infectivity of pseudotyped virus
    • Lagging, L. M., Meyer, K., Owens, R. J. & Ray, R. (1998). Functional role of hepatitis C virus chimeric glycoproteins in the infectivity of pseudotyped virus. J Virol 72, 3539-3546.
    • (1998) J Virol , vol.72 , pp. 3539-3546
    • Lagging, L.M.1    Meyer, K.2    Owens, R.J.3    Ray, R.4
  • 21
    • 0019959320 scopus 로고
    • The interaction of antibody with the major surface glycoprotein of vesicular stomatitis virus. II. Monoclonal antibodies of nonneutralizing and cross-reactive epitopes of Indiana and New Jersey serotypes
    • Lefrancois, L. & Lyles, D. S. (1982). The interaction of antibody with the major surface glycoprotein of vesicular stomatitis virus. II. Monoclonal antibodies of nonneutralizing and cross-reactive epitopes of Indiana and New Jersey serotypes. Virology 121, 168-174.
    • (1982) Virology , vol.121 , pp. 168-174
    • Lefrancois, L.1    Lyles, D.S.2
  • 22
    • 0031925350 scopus 로고    scopus 로고
    • Infectious bovine viral diarrhea virus (strain NADL) RNA from stable cDNA clones: A cellular insertion determines NS3 production and viral cytopathogenicity
    • Mendez, E., Ruggli, N., Collett, M. S. & Rice, C. M. (1998). Infectious bovine viral diarrhea virus (strain NADL) RNA from stable cDNA clones: a cellular insertion determines NS3 production and viral cytopathogenicity. J Virol 72, 4737-4745.
    • (1998) J Virol , vol.72 , pp. 4737-4745
    • Mendez, E.1    Ruggli, N.2    Collett, M.S.3    Rice, C.M.4
  • 23
    • 33744782279 scopus 로고    scopus 로고
    • Analysis of ACE2 in polarized epithelial cells: Surface expression and function as receptor for severe acute respiratory syndrome-associated coronavirus
    • Ren, X., Glende, J., Al Falah, M., Schwegmann-Wessels, C., Qu, X., Tan, L., Tschernig, T., Deng, H., Naim, H. Y. & Herrler, G. (2006). Analysis of ACE2 in polarized epithelial cells: surface expression and function as receptor for severe acute respiratory syndrome-associated coronavirus. J Gen Virol 87, 1691-1695.
    • (2006) J Gen Virol , vol.87 , pp. 1691-1695
    • Ren, X.1    Glende, J.2    Al Falah, M.3    Schwegmann-Wessels, C.4    Qu, X.5    Tan, L.6    Tschernig, T.7    Deng, H.8    Naim, H.Y.9    Herrler, G.10
  • 24
    • 0027238125 scopus 로고
    • Processing of the envelope glycoproteins of pestiviruses
    • Rümenapf, T., Unger, G., Strauss, J. H. & Thiel, H. J. (1993). Processing of the envelope glycoproteins of pestiviruses. J Virol 67, 3288-3294.
    • (1993) J Virol , vol.67 , pp. 3288-3294
    • Rümenapf, T.1    Unger, G.2    Strauss, J.H.3    Thiel, H.J.4
  • 25
    • 0025955758 scopus 로고
    • Hog cholera virus: Molecular composition of virions from a pestivirus
    • Thiel, H. J., Stark, R., Weiland, E., Rumenapf, T. & Meyers, G. (1991). Hog cholera virus: molecular composition of virions from a pestivirus. J Virol 65, 4705-4712.
    • (1991) J Virol , vol.65 , pp. 4705-4712
    • Thiel, H.J.1    Stark, R.2    Weiland, E.3    Rumenapf, T.4    Meyers, G.5
  • 27
    • 7444268500 scopus 로고    scopus 로고
    • Characterization of classical swine fever virus entry by using pseudotyped viruses: E1 and E2 are sufficient to mediate viral entry
    • Wang, Z., Nie, Y., Wang, P., Ding, M. & Deng, H. (2004). Characterization of classical swine fever virus entry by using pseudotyped viruses: E1 and E2 are sufficient to mediate viral entry. Virology 330, 332-341.
    • (2004) Virology , vol.330 , pp. 332-341
    • Wang, Z.1    Nie, Y.2    Wang, P.3    Ding, M.4    Deng, H.5
  • 28
    • 0025307406 scopus 로고
    • Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer
    • Weiland, E., Stark, R., Haas, B., Rumenapf, T., Meyers, G. & Thiel, H. J. (1990). Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer. J Virol 64, 3563-3569.
    • (1990) J Virol , vol.64 , pp. 3563-3569
    • Weiland, E.1    Stark, R.2    Haas, B.3    Rumenapf, T.4    Meyers, G.5    Thiel, H.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.