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Volumn 139, Issue 4, 2009, Pages 283-290

High-level expression of rabies virus glycoprotein with the RNA-based Semliki Forest Virus expression vector

Author keywords

Rabies virus; Rabies virus glycoprotein (RVGP); Semliki Forest Virus (SFV)

Indexed keywords

CELL LINES; EXPRESSION VECTORS; HIGH-LEVEL EXPRESSIONS; RABIES VIRUS; RABIES VIRUS GLYCOPROTEIN (RVGP); SEMLIKI FOREST VIRUS (SFV); VIRAL DISEASE;

EID: 60549087512     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2008.12.009     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 38849097721 scopus 로고    scopus 로고
    • Analytical approach for the extraction of recombinant membrane viral glycoprotein from stably transfected Drosophila melanogaster cells
    • Astray R.M., Augusto E., Yokomizo A.Y., and Pereira C.A. Analytical approach for the extraction of recombinant membrane viral glycoprotein from stably transfected Drosophila melanogaster cells. Biotechnol. J. 3 (2008) 98-103
    • (2008) Biotechnol. J. , vol.3 , pp. 98-103
    • Astray, R.M.1    Augusto, E.2    Yokomizo, A.Y.3    Pereira, C.A.4
  • 2
    • 14744292350 scopus 로고
    • Semliki Forest virus expression system: production of conditionally infectious recombinant particles
    • Berglund P., Sjöberg M., Garoff H., Atkins G.J., Sheahan B.J., and Liljeström P. Semliki Forest virus expression system: production of conditionally infectious recombinant particles. Biotechnology 11 (1993) 916-920
    • (1993) Biotechnology , vol.11 , pp. 916-920
    • Berglund, P.1    Sjöberg, M.2    Garoff, H.3    Atkins, G.J.4    Sheahan, B.J.5    Liljeström, P.6
  • 3
    • 0028075840 scopus 로고
    • The pathogenesis of rabies and other lyssaviral infections: recent studies
    • Charlton K.M. The pathogenesis of rabies and other lyssaviral infections: recent studies. Curr. Top. Microbiol. Immunol. 187 (1994) 95-119
    • (1994) Curr. Top. Microbiol. Immunol. , vol.187 , pp. 95-119
    • Charlton, K.M.1
  • 4
    • 0017683346 scopus 로고
    • Rabies virus glycoprotein. II. Biological and serological characterization
    • Cox J.H., Dietzschold B., and Schneider L.G. Rabies virus glycoprotein. II. Biological and serological characterization. Infect. Immun. 16 (1977) 754-759
    • (1977) Infect. Immun. , vol.16 , pp. 754-759
    • Cox, J.H.1    Dietzschold, B.2    Schneider, L.G.3
  • 5
    • 23844451664 scopus 로고    scopus 로고
    • Biochemical and immunogenic characterization of soluble human immunodeficiency virus type 1 envelope glycoprotein trimers expressed by Semliki Forest Virus
    • Forsell M.N., Li Y., Sundbäck M., Svehla K., Liljeström P., Mascola J.R., Wyatt R., and Karlsson Hedestam G.B. Biochemical and immunogenic characterization of soluble human immunodeficiency virus type 1 envelope glycoprotein trimers expressed by Semliki Forest Virus. J. Virol. 79 (2005) 10902-10914
    • (2005) J. Virol. , vol.79 , pp. 10902-10914
    • Forsell, M.N.1    Li, Y.2    Sundbäck, M.3    Svehla, K.4    Liljeström, P.5    Mascola, J.R.6    Wyatt, R.7    Karlsson Hedestam, G.B.8
  • 10
    • 0033492168 scopus 로고    scopus 로고
    • Transient gene expression in mammalian and mosquito cells using a recombinant Semliki Forest virus expressing T7 RNA polymerase
    • Kohl A., Billecocq A., Préhaud C., Yadani F.Z., and Bouloy M. Transient gene expression in mammalian and mosquito cells using a recombinant Semliki Forest virus expressing T7 RNA polymerase. Appl. Microbiol. Biotechnol. 53 (1999) 51-56
    • (1999) Appl. Microbiol. Biotechnol. , vol.53 , pp. 51-56
    • Kohl, A.1    Billecocq, A.2    Préhaud, C.3    Yadani, F.Z.4    Bouloy, M.5
  • 11
    • 0037020152 scopus 로고    scopus 로고
    • Rabies virus glycoprotein (RVG) is a trimeric ligand for the N-terminal cysteine-rich domain of the mammalian p75 neurotrophin receptor
    • Langevin C., Jaaro H., Bressanelli S., Fainzilber M., and Tuffereau C. Rabies virus glycoprotein (RVG) is a trimeric ligand for the N-terminal cysteine-rich domain of the mammalian p75 neurotrophin receptor. J. Biol. Chem. 277 (2002) 37655-37662
    • (2002) J. Biol. Chem. , vol.277 , pp. 37655-37662
    • Langevin, C.1    Jaaro, H.2    Bressanelli, S.3    Fainzilber, M.4    Tuffereau, C.5
  • 12
    • 14744304517 scopus 로고
    • A new generation of animal cell expression vectors based on the Semliki Forest virus replicon
    • Liljeström P., and Garoff H. A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Biotechnology 9 (1991) 1356-1361
    • (1991) Biotechnology , vol.9 , pp. 1356-1361
    • Liljeström, P.1    Garoff, H.2
  • 13
    • 0027966894 scopus 로고
    • High-level expression of the human neurokinin-1 receptor in mammalian cell lines using the Semliki Forest virus expression system
    • Lundström K., Mills A., Buell G., Allet E., Adami N., and Liljeström P. High-level expression of the human neurokinin-1 receptor in mammalian cell lines using the Semliki Forest virus expression system. Eur. J. Biochem. 224 (1994) 917-921
    • (1994) Eur. J. Biochem. , vol.224 , pp. 917-921
    • Lundström, K.1    Mills, A.2    Buell, G.3    Allet, E.4    Adami, N.5    Liljeström, P.6
  • 14
    • 0036972976 scopus 로고    scopus 로고
    • Semliki forest virus-based expression for versatile use in receptor research
    • Lundström K. Semliki forest virus-based expression for versatile use in receptor research. J. Recept. Signal. Transduct. Res. 22 (2002) 229-240
    • (2002) J. Recept. Signal. Transduct. Res. , vol.22 , pp. 229-240
    • Lundström, K.1
  • 15
    • 0037450521 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins
    • Lundström K. Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins. Biochim. Biophys. Acta 1610 (2003) 90-96
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 90-96
    • Lundström, K.1
  • 16
    • 0036271962 scopus 로고    scopus 로고
    • Rabies virus glycoprotein can fold in two alternative, antigenically distinct conformations depending on membrane-anchor type
    • Maillard A.P., and Gaudin Y. Rabies virus glycoprotein can fold in two alternative, antigenically distinct conformations depending on membrane-anchor type. J. Gen. Virol. 83 (2002) 1465-1476
    • (2002) J. Gen. Virol. , vol.83 , pp. 1465-1476
    • Maillard, A.P.1    Gaudin, Y.2
  • 17
    • 60549096000 scopus 로고    scopus 로고
    • National Association of State Public Health Veterinarians, Inc. (NASPHV); Centers for Disease Control and Prevention (CDC); Council of State and Territorial Epidemiologists; American Veterinary Medical Association, 2007. Compendium of measures to prevent disease associated with animals in public settings: National Association of State Public Health Veterinarians, Inc. (NASPHV), 56, pp. 1-14.
    • National Association of State Public Health Veterinarians, Inc. (NASPHV); Centers for Disease Control and Prevention (CDC); Council of State and Territorial Epidemiologists; American Veterinary Medical Association, 2007. Compendium of measures to prevent disease associated with animals in public settings: National Association of State Public Health Veterinarians, Inc. (NASPHV), vol. 56, pp. 1-14.
  • 18
    • 0023750140 scopus 로고
    • Interleukin-2 production in vitro: a new approach to the study of rabies vaccine immunogenicity as appraised by testing different glycoprotein presentations
    • Perrin P., Joffret M.L., Oth D., Leclerc C., Sureau P., and Thibodeau L. Interleukin-2 production in vitro: a new approach to the study of rabies vaccine immunogenicity as appraised by testing different glycoprotein presentations. Vaccine 6 (1988) 331-338
    • (1988) Vaccine , vol.6 , pp. 331-338
    • Perrin, P.1    Joffret, M.L.2    Oth, D.3    Leclerc, C.4    Sureau, P.5    Thibodeau, L.6
  • 19
    • 0002849040 scopus 로고    scopus 로고
    • Enzyme linked immunosorbent assay (ELISA) for the determination of glycoprotein content of rabies vaccines
    • Meslin F.X., Kaplan M.M., and Koprowski H. (Eds), WHO, Geneva
    • Perrin P., Lafon M., and Sureau P. Enzyme linked immunosorbent assay (ELISA) for the determination of glycoprotein content of rabies vaccines. In: Meslin F.X., Kaplan M.M., and Koprowski H. (Eds). Laboratory Techniques in Rabies. 4th ed. (1996), WHO, Geneva 383-388
    • (1996) Laboratory Techniques in Rabies. 4th ed. , pp. 383-388
    • Perrin, P.1    Lafon, M.2    Sureau, P.3
  • 20
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29 (2001) e45
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 22
    • 23844476258 scopus 로고    scopus 로고
    • Stable trimerization of recombinant rabies virus glycoprotein ectodomain is required for interaction with the p75NTR receptor
    • Sissoëff L., Mousli M., England P., and Tuffereau C. Stable trimerization of recombinant rabies virus glycoprotein ectodomain is required for interaction with the p75NTR receptor. J. Gen. Virol. 86 (2005) 2543-2552
    • (2005) J. Gen. Virol. , vol.86 , pp. 2543-2552
    • Sissoëff, L.1    Mousli, M.2    England, P.3    Tuffereau, C.4
  • 23
    • 0032906979 scopus 로고    scopus 로고
    • Two-helper RNA system for production of recombinant Semliki forest virus particles
    • Smerdou C., and Liljeström P. Two-helper RNA system for production of recombinant Semliki forest virus particles. J. Virol. 73 (1999) 1092-1098
    • (1999) J. Virol. , vol.73 , pp. 1092-1098
    • Smerdou, C.1    Liljeström, P.2
  • 24
    • 0020410707 scopus 로고
    • Rabies virus pathogenicity and challenge. Influence of the method of preparation, the route of inoculation, and the species. Comparison of the characteristics of the modified, fixed and wild strains
    • Soulebot J.P., Brun A., Chappuis G., Guillemin F., and Tixier G. Rabies virus pathogenicity and challenge. Influence of the method of preparation, the route of inoculation, and the species. Comparison of the characteristics of the modified, fixed and wild strains. Comp. Immunol. Microbiol. Infect. Dis. 5 (1982) 71-78
    • (1982) Comp. Immunol. Microbiol. Infect. Dis. , vol.5 , pp. 71-78
    • Soulebot, J.P.1    Brun, A.2    Chappuis, G.3    Guillemin, F.4    Tixier, G.5
  • 27
    • 0026739991 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Biotechnology 24 (1992) 145-149
    • (1992) Biotechnology , vol.24 , pp. 145-149
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 33846539190 scopus 로고    scopus 로고
    • Public health awareness of emerging zoonotic viruses of bats: a European perspective
    • Van der Poel W.H., Lina P.H., and Kramps J.A. Public health awareness of emerging zoonotic viruses of bats: a European perspective. Vector Borne Zoonotic Dis. 6 (2006) 315-324
    • (2006) Vector Borne Zoonotic Dis. , vol.6 , pp. 315-324
    • Van der Poel, W.H.1    Lina, P.H.2    Kramps, J.A.3
  • 29
    • 1642355140 scopus 로고    scopus 로고
    • Rabies and other lyssavirus diseases
    • Warrell M.J., and Warrell D.A. Rabies and other lyssavirus diseases. Lancet 363 9413 (2004) 959-969
    • (2004) Lancet , vol.363 , Issue.9413 , pp. 959-969
    • Warrell, M.J.1    Warrell, D.A.2
  • 30
    • 17844396916 scopus 로고    scopus 로고
    • Australian bat lyssavirus: a recently discovered new rhabdovirus
    • Warrilow D. Australian bat lyssavirus: a recently discovered new rhabdovirus. Curr. Top. Microbiol. Immunol. 292 (2005) 25-44
    • (2005) Curr. Top. Microbiol. Immunol. , vol.292 , pp. 25-44
    • Warrilow, D.1
  • 31
    • 0026339191 scopus 로고
    • Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
    • Whitt M.A., Buonocore L., Prehaud C., and Rose J.K. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 185 (1991) 681-688
    • (1991) Virology , vol.185 , pp. 681-688
    • Whitt, M.A.1    Buonocore, L.2    Prehaud, C.3    Rose, J.K.4
  • 32
    • 0037023805 scopus 로고    scopus 로고
    • WHO position paper. Rabies vaccines, 2002. Wkly. Epidemiol. Rec.77, 109-119.
    • WHO position paper. Rabies vaccines, 2002. Wkly. Epidemiol. Rec.77, 109-119.
  • 34
    • 33750492961 scopus 로고    scopus 로고
    • Dot-blot immunodetection as a versatile and high-throughput assay to evaluate recombinant GPCRs produced in the yeast Pichia pastoris
    • Zeder-Lutz G., Cherouati N., Reinhart C., Pattus F., and Wagner R. Dot-blot immunodetection as a versatile and high-throughput assay to evaluate recombinant GPCRs produced in the yeast Pichia pastoris. Protein Expr. Purif. 50 (2006) 118-127
    • (2006) Protein Expr. Purif. , vol.50 , pp. 118-127
    • Zeder-Lutz, G.1    Cherouati, N.2    Reinhart, C.3    Pattus, F.4    Wagner, R.5


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