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Volumn 114, Issue 1-2, 2005, Pages 54-62

The glycosylation pattern of baculovirus expressed envelope protein E2 affects its ability to prevent infection with bovine viral diarrhoea virus

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLYCOPROTEIN E2; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 27744474818     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2005.05.011     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 0034610244 scopus 로고    scopus 로고
    • Recombinant bovine adenovirus type 3 expressing bovine viral diarrhea virus glycoprotein E2 induces an immune response in cotton rats
    • M.K. Baxi, D. Deregt, J. Robertson, L.A. Babiuk, T. Schlapp, and S.K. Tikoo Recombinant bovine adenovirus type 3 expressing bovine viral diarrhea virus glycoprotein E2 induces an immune response in cotton rats Virology 278 2000 234 243
    • (2000) Virology , vol.278 , pp. 234-243
    • Baxi, M.K.1    Deregt, D.2    Robertson, J.3    Babiuk, L.A.4    Schlapp, T.5    Tikoo, S.K.6
  • 2
    • 0034231849 scopus 로고    scopus 로고
    • Folding of viral envelope glycoproteins in the endoplasmic reticulum
    • I. Braakman, and E. van Anken Folding of viral envelope glycoproteins in the endoplasmic reticulum Traffic 1 2000 533 539
    • (2000) Traffic , vol.1 , pp. 533-539
    • Braakman, I.1    Van Anken, E.2
  • 3
    • 0036056989 scopus 로고    scopus 로고
    • A single glycosylation site within the receptor-binding domain of the avian sarcoma/leukosis virus glycoprotein is critical for receptor binding
    • S.E. Delos, M.J. Burdick, and J.M. White A single glycosylation site within the receptor-binding domain of the avian sarcoma/leukosis virus glycoprotein is critical for receptor binding Virology 294 2002 354 363
    • (2002) Virology , vol.294 , pp. 354-363
    • Delos, S.E.1    Burdick, M.J.2    White, J.M.3
  • 4
    • 0021984076 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin. the low pH-induced conformational change
    • R.W. Doms, A. Helenius, and J. White Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change J. Biol. Chem. 260 1985 2973 2981
    • (1985) J. Biol. Chem. , vol.260 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 5
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • R.W. Doms, R.A. Lamb, J.K. Rose, and A. Helenius Folding and assembly of viral membrane proteins Virology 193 1993 545 562
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 6
    • 0023258708 scopus 로고
    • Differences in virus-induced polypeptides in cells infected by cytopathic and noncytopathic biotypes of bovine virus diarrhea-mucosal disease virus
    • R.O. Donis, and E.J. Dubovi Differences in virus-induced polypeptides in cells infected by cytopathic and noncytopathic biotypes of bovine virus diarrhea-mucosal disease virus Virology 158 1987 168 173
    • (1987) Virology , vol.158 , pp. 168-173
    • Donis, R.O.1    Dubovi, E.J.2
  • 7
    • 0023449319 scopus 로고
    • Molecular specificity of the antibody responses of cattle naturally and experimentally infected with cytopathic and noncytopathic bovine viral diarrhea virus biotypes
    • R.O. Donis, and E.J. Dubovi Molecular specificity of the antibody responses of cattle naturally and experimentally infected with cytopathic and noncytopathic bovine viral diarrhea virus biotypes Am. J. Vet. Res. 48 1987 1549 1554
    • (1987) Am. J. Vet. Res. , vol.48 , pp. 1549-1554
    • Donis, R.O.1    Dubovi, E.J.2
  • 8
    • 0032804299 scopus 로고    scopus 로고
    • Recombinant adenoviruses expressing the E2 protein of bovine viral diarrhea virus induce humoral and cellular immune responses
    • S.M. Elahi, S.H. Shen, B.G. Talbot, B. Massie, S. Harpin, and Y. Elazhary Recombinant adenoviruses expressing the E2 protein of bovine viral diarrhea virus induce humoral and cellular immune responses FEMS Microbiol. Lett. 177 1999 159 166
    • (1999) FEMS Microbiol. Lett. , vol.177 , pp. 159-166
    • Elahi, S.M.1    Shen, S.H.2    Talbot, B.G.3    Massie, B.4    Harpin, S.5    Elazhary, Y.6
  • 9
    • 0033946411 scopus 로고    scopus 로고
    • Germinal centre localization of bovine viral diarrhoea virus in persistently infected animals
    • M.D. Fray, E.A. Supple, W.I. Morrison, and B. Charleston Germinal centre localization of bovine viral diarrhoea virus in persistently infected animals J. Gen. Virol. 81 2000 1669 1673
    • (2000) J. Gen. Virol. , vol.81 , pp. 1669-1673
    • Fray, M.D.1    Supple, E.A.2    Morrison, W.I.3    Charleston, B.4
  • 10
    • 0026489261 scopus 로고
    • Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus
    • P.J. Gallagher, J.M. Henneberry, J.F. Sambrook, and M.J. Gething Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus J. Virol. 66 1992 7136 7145
    • (1992) J. Virol. , vol.66 , pp. 7136-7145
    • Gallagher, P.J.1    Henneberry, J.M.2    Sambrook, J.F.3    Gething, M.J.4
  • 11
    • 0018786653 scopus 로고
    • The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature-sensitive and undergoes intracellular aggregation at elevated temperatures
    • R. Gibson, S. Schlesinger, and S. Kornfeld The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature-sensitive and undergoes intracellular aggregation at elevated temperatures J. Biol. Chem. 254 1979 3600 3607
    • (1979) J. Biol. Chem. , vol.254 , pp. 3600-3607
    • Gibson, R.1    Schlesinger, S.2    Kornfeld, S.3
  • 12
    • 0034632629 scopus 로고    scopus 로고
    • Presence of bovine viral diarrhea virus (BVDV) E2 glycoprotein in VSV recombinant particles and induction of neutralizing BVDV antibodies in mice
    • P.R. Grigera, M.P. Marzocca, A.V. Capozzo, L. Buonocore, R.O. Donis, and J.K. Rose Presence of bovine viral diarrhea virus (BVDV) E2 glycoprotein in VSV recombinant particles and induction of neutralizing BVDV antibodies in mice Virus Res. 69 2000 3 15
    • (2000) Virus Res. , vol.69 , pp. 3-15
    • Grigera, P.R.1    Marzocca, M.P.2    Capozzo, A.V.3    Buonocore, L.4    Donis, R.O.5    Rose, J.K.6
  • 13
    • 0030667061 scopus 로고    scopus 로고
    • The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
    • D.N. Hebert, J.X. Zhang, W. Chen, B. Foellmer, and A. Helenius The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin J. Cell Biol. 139 1997 613 623
    • (1997) J. Cell Biol. , vol.139 , pp. 613-623
    • Hebert, D.N.1    Zhang, J.X.2    Chen, W.3    Foellmer, B.4    Helenius, A.5
  • 14
    • 0002343237 scopus 로고    scopus 로고
    • Family Flaviviridae
    • van Regnmortel, M.H.V., Fanquet, C.M., Bishop, D.H.L., Carstens, E.V., Estes, M.K., Lemon, S.M., Manilott, J., Mayo, M.A., McGeoch, D.J., Pringle, C.R., Wickner, R.B. (Eds.), Virus Taxonomy, Academic Press
    • Heinz, F., Collet, M., Purrchell, R., Gould, E., Howard, C., Hougton, M., Moorman, R., Rice, C., Theil, H.-J., 2000. Family Flaviviridae. In: van Regnmortel, M.H.V., Fanquet, C.M., Bishop, D.H.L., Carstens, E.V., Estes, M.K., Lemon, S.M., Manilott, J., Mayo, M.A., McGeoch, D.J., Pringle, C.R., Wickner, R.B. (Eds.), Virus Taxonomy, Proceedings of the seventh Report of International Committee on Taxonomy of Viruses. Academic Press, pp. 859-878.
    • (2000) Proceedings of the Seventh Report of International Committee on Taxonomy of Viruses , pp. 859-878
    • Heinz, F.1    Collet, M.2    Purrchell, R.3    Gould, E.4    Howard, C.5    Hougton, M.6    Moorman, R.7    Rice, C.8    Theil, H.-J.9
  • 15
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • A. Helenius, and M. Aebi Intracellular functions of N-linked glycans Science 291 2001 2364 2369
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 16
    • 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
    • M.M. Hulst, and R.J. Moormann 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
  • 17
    • 0036714407 scopus 로고    scopus 로고
    • Identification of the glycosaminoglycan-binding site on the glycoprotein E(rns) of bovine viral diarrhoea virus by site-directed mutagenesis
    • M. Iqbal, and J.W. McCauley Identification of the glycosaminoglycan- binding site on the glycoprotein E(rns) of bovine viral diarrhoea virus by site-directed mutagenesis J. Gen. Virol. 83 2002 2153 2159
    • (2002) J. Gen. Virol. , vol.83 , pp. 2153-2159
    • Iqbal, M.1    McCauley, J.W.2
  • 18
    • 0017356042 scopus 로고
    • Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis viruses
    • R. Leavitt, S. Schlesinger, and S. Kornfeld Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis viruses J. Virol. 21 1977 375 385
    • (1977) J. Virol. , vol.21 , pp. 375-385
    • Leavitt, R.1    Schlesinger, S.2    Kornfeld, S.3
  • 19
    • 0842304523 scopus 로고    scopus 로고
    • CD46 is a cellular receptor for bovine viral diarrhea virus
    • K. Maurer, T. Krey, V. Moennig, H.J. Thiel, and T. Rumenapf CD46 is a cellular receptor for bovine viral diarrhea virus J. Virol. 78 2004 1792 1799
    • (2004) J. Virol. , vol.78 , pp. 1792-1799
    • Maurer, K.1    Krey, T.2    Moennig, V.3    Thiel, H.J.4    Rumenapf, T.5
  • 20
    • 2942647917 scopus 로고    scopus 로고
    • Influence of N-glycans on processing and biological activity of the nipah virus fusion protein
    • M. Moll, A. Kaufmann, and A. Maisner Influence of N-glycans on processing and biological activity of the nipah virus fusion protein J. Virol. 78 2004 7274 7278
    • (2004) J. Virol. , vol.78 , pp. 7274-7278
    • Moll, M.1    Kaufmann, A.2    Maisner, A.3
  • 21
    • 0031713177 scopus 로고    scopus 로고
    • Location-specific, unequal contribution of the N-glycans in simian immunodeficiency virus gp120 to viral infectivity and removal of multiple glycans without disturbing infectivity
    • S. Ohgimoto, T. Shioda, K. Mori, E.E. Nakayama, H. Hu, and Y. Nagai Location-specific, unequal contribution of the N-glycans in simian immunodeficiency virus gp120 to viral infectivity and removal of multiple glycans without disturbing infectivity J. Virol. 72 1998 8365 8370
    • (1998) J. Virol. , vol.72 , pp. 8365-8370
    • Ohgimoto, S.1    Shioda, T.2    Mori, K.3    Nakayama, E.E.4    Hu, H.5    Nagai, Y.6
  • 22
    • 2342544913 scopus 로고    scopus 로고
    • Loss of N-linked glycosylation from the hemagglutinin-neuraminidase protein alters virulence of Newcastle disease virus
    • A. Panda, S. Elankumaran, S. Krishnamurthy, Z. Huang, and S.K. Samal Loss of N-linked glycosylation from the hemagglutinin-neuraminidase protein alters virulence of Newcastle disease virus J. Virol. 78 2004 4965 4975
    • (2004) J. Virol. , vol.78 , pp. 4965-4975
    • Panda, A.1    Elankumaran, S.2    Krishnamurthy, S.3    Huang, Z.4    Samal, S.K.5
  • 23
    • 0021911623 scopus 로고
    • Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs
    • J.S. Robertson, C.W. Naeve, R.G. Webster, J.S. Bootman, R. Newman, and G.C. Schild Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs Virology 143 1985 166 174
    • (1985) Virology , vol.143 , pp. 166-174
    • Robertson, J.S.1    Naeve, C.W.2    Webster, R.G.3    Bootman, J.S.4    Newman, R.5    Schild, G.C.6
  • 24
    • 2342629333 scopus 로고    scopus 로고
    • Analysis of N-linked glycosylation of hantaan virus glycoproteins and the role of oligosaccharide side chains in protein folding and intracellular trafficking
    • X. Shi, and R.M. Elliott Analysis of N-linked glycosylation of hantaan virus glycoproteins and the role of oligosaccharide side chains in protein folding and intracellular trafficking J. Virol. 78 2004 5414 5422
    • (2004) J. Virol. , vol.78 , pp. 5414-5422
    • Shi, X.1    Elliott, R.M.2
  • 25
    • 1242293619 scopus 로고    scopus 로고
    • HCV E2 glycoprotein: Mutagenesis of N-linked glycosylation sites and its effects on E2 expression and processing
    • T. Slater-Handshy, D.A. Droll, X. Fan, A.M. Di Bisceglie, and T.J. Chambers HCV E2 glycoprotein: mutagenesis of N-linked glycosylation sites and its effects on E2 expression and processing Virology 319 2004 36 48
    • (2004) Virology , vol.319 , pp. 36-48
    • Slater-Handshy, T.1    Droll, D.A.2    Fan, X.3    Di Bisceglie, A.M.4    Chambers, T.J.5
  • 26
    • 0023723072 scopus 로고
    • Selective removal of alpha heavy-chain glycosylation sites causes immunoglobulin a degradation and reduced secretion
    • A.K. Taylor, and R. Wall Selective removal of alpha heavy-chain glycosylation sites causes immunoglobulin A degradation and reduced secretion Mol. Cell. Biol. 8 1988 4197 4203
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4197-4203
    • Taylor, A.K.1    Wall, R.2
  • 27
    • 0025955758 scopus 로고
    • Hog cholera virus: Molecular composition of virions from a pestivirus
    • H.J. Thiel, R. Stark, E. Weiland, T. Rumenapf, and G. Meyers Hog cholera virus: molecular composition of virions from a pestivirus J. Virol. 65 1991 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
  • 28
    • 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
    • Z. Wang, Y. Nie, P. Wang, M. Ding, and H. Deng Characterization of classical swine fever virus entry by using pseudotyped viruses: E1 and E2 are sufficient to mediate viral entry Virology 330 2004 332 341
    • (2004) Virology , vol.330 , pp. 332-341
    • Wang, Z.1    Nie, Y.2    Wang, P.3    Ding, M.4    Deng, H.5
  • 29
    • 0032904783 scopus 로고    scopus 로고
    • Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles
    • F. Weiland, E. Weiland, G. Unger, A. Saalmuller, and H.J. Thiel Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles J. Gen. Virol. 80 1999 1157 1165
    • (1999) J. Gen. Virol. , vol.80 , pp. 1157-1165
    • Weiland, F.1    Weiland, E.2    Unger, G.3    Saalmuller, A.4    Thiel, H.J.5
  • 30
    • 0024757663 scopus 로고
    • Antigenic differentiation of pestivirus strains with monoclonal antibodies against hog cholera virus
    • G. Wensvoort, C. Terpstra, E.P. de Kluijver, C. Kragten, and J.C. Warnaar Antigenic differentiation of pestivirus strains with monoclonal antibodies against hog cholera virus Vet. Microbiol. 21 1989 9 20
    • (1989) Vet. Microbiol. , vol.21 , pp. 9-20
    • Wensvoort, G.1    Terpstra, C.2    De Kluijver, E.P.3    Kragten, C.4    Warnaar, J.C.5
  • 32
    • 0035037076 scopus 로고    scopus 로고
    • N-glycans of F protein differentially affect fusion activity of human respiratory syncytial virus
    • G. Zimmer, I. Trotz, and G. Herrler N-glycans of F protein differentially affect fusion activity of human respiratory syncytial virus J. Virol. 75 2001 4744 4751
    • (2001) J. Virol. , vol.75 , pp. 4744-4751
    • Zimmer, G.1    Trotz, I.2    Herrler, G.3


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