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Volumn 44, Issue 3, 2006, Pages 313-324

Expression of foreign protein epitopes at the surface of recombinant yellow fever 17D viruses based on three-dimensional modeling of its envelope protein

Author keywords

Attenuation; E protein structure; Foreign epitope expression; Yellow fever 17D virus

Indexed keywords

COMPLEMENTARY DNA; EPITOPE; GLYCOPROTEIN E, FLAVIVIRUS; LIVE VACCINE; VIRUS ENVELOPE PROTEIN; VIRUS RNA; YELLOW FEVER VACCINE;

EID: 33646893262     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:44:3:313     Document Type: Conference Paper
Times cited : (15)

References (56)
  • 1
    • 0021863828 scopus 로고
    • Nucleotide sequence of yellow fever virus: Implications for flavivirus gene expression and evolution
    • Rice, C. M., Lenches E. M., Eddy S. R., Shin S. J., Sheets R. L., and Strauss, J. H. (1985) Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution. Science 229, 726-733.
    • (1985) Science , vol.229 , pp. 726-733
    • Rice, C.M.1    Lenches, E.M.2    Eddy, S.R.3    Shin, S.J.4    Sheets, R.L.5    Strauss, J.H.6
  • 2
    • 0642379621 scopus 로고    scopus 로고
    • Pathogenesis and pathophysiology of yellow fever
    • Monath, T. P. and Barrett, A. D. (2003) Pathogenesis and pathophysiology of yellow fever. Adv. Virus Res. 60, 343-395.
    • (2003) Adv. Virus Res. , vol.60 , pp. 343-395
    • Monath, T.P.1    Barrett, A.D.2
  • 3
    • 0024892209 scopus 로고
    • Transcription of infectious yellow fever RNA from full-length cDNA templates produced by in vitro ligation
    • 2a. Rice, C.M., Grakoui, A., Galler, R., and Chambers, T. J., (1984) Transcription of infectious yellow fever RNA from full-length cDNA templates produced by in vitro ligation. New Biol. 1, 285-296.
    • (1984) New Biol. , vol.1 , pp. 285-296
    • Rice, C.M.1    Grakoui, A.2    Galler, R.3    Chambers, T.J.4
  • 4
    • 1442333330 scopus 로고    scopus 로고
    • Chimeric flaviviruses: Novel vaccines against dengue fever, tick-borne encephalitis, and Japanese encephalitis
    • Lai, C. J. and Monath, T. P. (2003) Chimeric flaviviruses: novel vaccines against dengue fever, tick-borne encephalitis, and Japanese encephalitis. Adv. Virus Res. 61, 469-509.
    • (2003) Adv. Virus Res. , vol.61 , pp. 469-509
    • Lai, C.J.1    Monath, T.P.2
  • 6
    • 0026041584 scopus 로고
    • Poliovirus antigen chimeras
    • Rose, C. S. and Evans, D. J. (1991) Poliovirus antigen chimeras. Trends Biotechnol. 9, 415-421.
    • (1991) Trends Biotechnol. , vol.9 , pp. 415-421
    • Rose, C.S.1    Evans, D.J.2
  • 7
    • 0039774784 scopus 로고
    • Poliovirus type 1/type 3 antigenic hybrid virus constructed in vitro elicits type 1 and type 3 neutralizing antibodies in rabbits and monkeys
    • Murray, M. G., Kuhn, R. J., Arita, M., Kawamura, N., Nomoto, A., and Wimmer, E. (1988) Poliovirus type 1/type 3 antigenic hybrid virus constructed in vitro elicits type 1 and type 3 neutralizing antibodies in rabbits and monkeys. Proc. Natl. Acad. Sci. USA 85, 3203-3207.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3203-3207
    • Murray, M.G.1    Kuhn, R.J.2    Arita, M.3    Kawamura, N.4    Nomoto, A.5    Wimmer, E.6
  • 8
    • 0026645490 scopus 로고
    • Immunogenicity and antigenicity of chimeric picornaviruses which express hepatitis A virus (HAV) peptide sequences: Evidence for a neutralization domain near the amino terminus of VP1 of HAV
    • Lemon, S. M., Barclay, W., Ferguson, M., et al. (1992) Immunogenicity and antigenicity of chimeric picornaviruses which express hepatitis A virus (HAV) peptide sequences: evidence for a neutralization domain near the amino terminus of VP1 of HAV. Virology 188, 285-295.
    • (1992) Virology , vol.188 , pp. 285-295
    • Lemon, S.M.1    Barclay, W.2    Ferguson, M.3
  • 10
    • 0029125373 scopus 로고
    • Immunogenicity of poliovirus B and T cell epitopes presented by hybrid porcine parvovirus particles
    • Sedlik, C., Sarraseca, J., Rueda, P., Leclerc, C., and Casal, I. (1995) Immunogenicity of poliovirus B and T cell epitopes presented by hybrid porcine parvovirus particles. J. Gen. Virol. 76, 2361-2368.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2361-2368
    • Sedlik, C.1    Sarraseca, J.2    Rueda, P.3    Leclerc, C.4    Casal, I.5
  • 11
    • 0033516507 scopus 로고    scopus 로고
    • Display of epitopes on the surface of tobacco mosaic virus: Impact of charge and isoelectric point of the epitope on virus-host interactions
    • Bendahmane, M., Koo, M., Karrer, E., and Beachy R. N. (1999) Display of epitopes on the surface of tobacco mosaic virus: impact of charge and isoelectric point of the epitope on virus-host interactions. J. Mol. Biol. 290, 9-20.
    • (1999) J. Mol. Biol. , vol.290 , pp. 9-20
    • Bendahmane, M.1    Koo, M.2    Karrer, E.3    Beachy, R.N.4
  • 12
    • 0033543951 scopus 로고    scopus 로고
    • Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles
    • Rueda, P., Hurtado, A., del Barrio, M., et al. (1999) Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles. Virology 263, 89-99.
    • (1999) Virology , vol.263 , pp. 89-99
    • Rueda, P.1    Hurtado, A.2    Del Barrio, M.3
  • 13
    • 0344199395 scopus 로고    scopus 로고
    • New chimaeric hepatitis B virus core particles carrying hantavirus (serotype Puumala) epitopes: Immunogenicity and protection against virus challenge
    • Ulrich, R., Koletzki, D., Lachmann, S. (1999) New chimaeric hepatitis B virus core particles carrying hantavirus (serotype Puumala) epitopes: immunogenicity and protection against virus challenge. J. Biotechnol. 73, 141-153.
    • (1999) J. Biotechnol. , vol.73 , pp. 141-153
    • Ulrich, R.1    Koletzki, D.2    Lachmann, S.3
  • 14
    • 0342323856 scopus 로고    scopus 로고
    • Formation of immunogenic virus-like particles by inserting epitopes into surface-exposed regions of hamster polyomavirus major capsid protein
    • Gedvilaite, A., Frommel, C., Sasnauskas, K., et al. (2000) Formation of immunogenic virus-like particles by inserting epitopes into surface-exposed regions of hamster polyomavirus major capsid protein. Virology 273, 21-35.
    • (2000) Virology , vol.273 , pp. 21-35
    • Gedvilaite, A.1    Frommel, C.2    Sasnauskas, K.3
  • 15
    • 0033964311 scopus 로고    scopus 로고
    • Expression of TetC fusion proteins from Salmonella in a gaseous environment that models conditions found in mammalian tissues
    • Heal, K. G., McConkey, G. A., Hormaeche, C. E., Hollingdale, M. R., Khan, C. M., and Taylor-Robinson, A. W. (2000) Expression of TetC fusion proteins from Salmonella in a gaseous environment that models conditions found in mammalian tissues. Biotechniques 28, 228-230, 232.
    • (2000) Biotechniques , vol.28 , pp. 228-230
    • Heal, K.G.1    McConkey, G.A.2    Hormaeche, C.E.3    Hollingdale, M.R.4    Khan, C.M.5    Taylor-Robinson, A.W.6
  • 16
    • 0034712983 scopus 로고    scopus 로고
    • Genetic manipulation of equine arteritis virus using full-length cDNA clones: Separation of overlapping genes and expression of a foreign epitope
    • de Vries, A. A., Glaser, A. L., Raamsman, M. J., et al. (2000) Genetic manipulation of equine arteritis virus using full-length cDNA clones: separation of overlapping genes and expression of a foreign epitope. Virology 270, 84-97.
    • (2000) Virology , vol.270 , pp. 84-97
    • De Vries, A.A.1    Glaser, A.L.2    Raamsman, M.J.3
  • 17
    • 0034899070 scopus 로고    scopus 로고
    • Delivery of multiple epitopes by recombinant detoxified adenylate cyclase of Bordetella pertussis induces protective antiviral immunity
    • Fayolle, C., Osickova, A., Osicka, R., et al. (2001) Delivery of multiple epitopes by recombinant detoxified adenylate cyclase of Bordetella pertussis induces protective antiviral immunity. J. Virol. 75, 7330-7338.
    • (2001) J. Virol. , vol.75 , pp. 7330-7338
    • Fayolle, C.1    Osickova, A.2    Osicka, R.3
  • 19
    • 0036892173 scopus 로고    scopus 로고
    • A modified hepatitis B virus core particle containing multiple epitopes of the Plasmodium falciparum circumsporozoite protein provides a highly immunogenic malaria vaccine in preclinical analyses in rodent and primate hosts
    • Birkett, A., Lyons, K., Schmidt, A., et al. (2002) A modified hepatitis B virus core particle containing multiple epitopes of the Plasmodium falciparum circumsporozoite protein provides a highly immunogenic malaria vaccine in preclinical analyses in rodent and primate hosts. Infect. Immun. 70, 6860-6870.
    • (2002) Infect. Immun. , vol.70 , pp. 6860-6870
    • Birkett, A.1    Lyons, K.2    Schmidt, A.3
  • 20
    • 0034703817 scopus 로고    scopus 로고
    • Immunogenicity of a foreign peptide expressed within a capsid protein of an attenuated coxsackievirus
    • Halim, S. S., Ostrowski, S. E., Lee, W. T., and Ramsingh, A. I. (2000) Immunogenicity of a foreign peptide expressed within a capsid protein of an attenuated coxsackievirus. Vaccine 19, 958-965.
    • (2000) Vaccine , vol.19 , pp. 958-965
    • Halim, S.S.1    Ostrowski, S.E.2    Lee, W.T.3    Ramsingh, A.I.4
  • 21
    • 0036785519 scopus 로고    scopus 로고
    • Newcastle disease virus (NDV) marker vaccine: An immunodominant epitope on the nucleoprotein gene of NDV can be deleted or replaced by a foreign epitope
    • Mebatsion, T., Koolen, M. J., de Vaan, L. T., et al. (2002) Newcastle disease virus (NDV) marker vaccine: an immunodominant epitope on the nucleoprotein gene of NDV can be deleted or replaced by a foreign epitope. J. Virol. 76, 10,138-10,146.
    • (2002) J. Virol. , vol.76
    • Mebatsion, T.1    Koolen, M.J.2    De Vaan, L.T.3
  • 22
    • 3142764760 scopus 로고    scopus 로고
    • Insertion of green fluorescent protein into nonstructural protein 5A allows direct visualization of functional hepatitis C virus replication complexes
    • Moradpour, D., Evans, M. J., Gosert, R., et al. (2004) Insertion of green fluorescent protein into nonstructural protein 5A allows direct visualization of functional hepatitis C virus replication complexes. J. Virol. 78, 7400-7409.
    • (2004) J. Virol. , vol.78 , pp. 7400-7409
    • Moradpour, D.1    Evans, M.J.2    Gosert, R.3
  • 23
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey F. A., Heinz, F. X., Mandl, C., Kunz, C., and Harrison, S. C. (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
  • 24
    • 0034905041 scopus 로고    scopus 로고
    • The machinery for flavivirus fusion with host cell membranes
    • Heinz, F. X. and Allison, S. L. (2001) The machinery for flavivirus fusion with host cell membranes. Curr. Opin. Microbiol. 4, 450-455.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 450-455
    • Heinz, F.X.1    Allison, S.L.2
  • 25
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis, Y., Ogata, S., Clements, D., and Harrison, S. C. (2003) A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. USA 100, 6986-6991.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 26
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • Kuhn, R. J., Zhang, W., Rossmann, M. G., et al. (2002) Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717-725.
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3
  • 27
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • Allison, S. L., Schalich, J., Stiasny K., Mandl, C. W., and Heinz, F. X. (2001) Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol. 75, 4268-4275.
    • (2001) J. Virol. , vol.75 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 28
    • 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. and Roehrig, J. T. (2001) 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, 7769-7773.
    • (2001) J. Virol. , vol.75 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 29
    • 0036891872 scopus 로고    scopus 로고
    • Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein
    • Beasley, D. W. and Barrett, A. D. (2002) Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein. J. Virol. 76, 13,097-14,100.
    • (2002) J. Virol. , vol.76
    • Beasley, D.W.1    Barrett, A.D.2
  • 30
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • Modis, Y., Ogata, S., Clements, D., and Harrison, S. C. (2005) Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79, 1223-1231.
    • (2005) J. Virol. , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 31
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • Stiasny K., Allison, S. L., Marchler-Bauer, A., Kunz, C., and Heinz, F. X. (1996) Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J. Virol. 70, 8142-8147.
    • (1996) J. Virol. , vol.70 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 32
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • Bressanelli, S., Stiasny, K., Allison, S. L., et al. (2004) Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J. 23, 728-738.
    • (2004) EMBO J. , vol.23 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3
  • 33
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D., and Harrison, S. C. (2004) Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319.
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 34
    • 4444338894 scopus 로고    scopus 로고
    • Conformational changes of the flavivirus E glycoprotein
    • Zhang, Y., Zhang, W., Ogata, S., et al. (2004) Conformational changes of the flavivirus E glycoprotein. Structure 12, 1607-1618.
    • (2004) Structure , vol.12 , pp. 1607-1618
    • Zhang, Y.1    Zhang, W.2    Ogata, S.3
  • 35
    • 0023518540 scopus 로고
    • A strategy for the rapid multiple alignment of protein sequences. Confidence levels from tertiary structure comparisons
    • Barton, G. J. and Sternberg, M. J. (1987) A strategy for the rapid multiple alignment of protein sequences. Confidence levels from tertiary structure comparisons. J. Mol. Biol. 198, 327-337.
    • (1987) J. Mol. Biol. , vol.198 , pp. 327-337
    • Barton, G.J.1    Sternberg, M.J.2
  • 36
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 37
    • 0022336792 scopus 로고
    • Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm
    • Braun, W. and Go, N. (1985) Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm. J. Mol. Biol. 186, 611-626.
    • (1985) J. Mol. Biol. , vol.186 , pp. 611-626
    • Braun, W.1    Go, N.2
  • 38
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A., and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 39
    • 0036304601 scopus 로고    scopus 로고
    • Surface expression of an immunodominant malaria protein B cell epitope by yellow fever virus
    • Bonaldo, M. C., Garratt, R. C., Caufour, P. S., et al. (2002) Surface expression of an immunodominant malaria protein B cell epitope by yellow fever virus. J. Mol. Biol. 315, 873-885.
    • (2002) J. Mol. Biol. , vol.315 , pp. 873-885
    • Bonaldo, M.C.1    Garratt, R.C.2    Caufour, P.S.3
  • 40
    • 0035813032 scopus 로고    scopus 로고
    • Construction, characterization and immunogenicity of recombinant yellow fever 17D-dengue type 2 viruses
    • Caufour, P. S., Motta, M. C., Yamamura, A. M., et al. (2001) Construction, characterization and immunogenicity of recombinant yellow fever 17D-dengue type 2 viruses. Virus Res. 279, 1-14.
    • (2001) Virus Res. , vol.279 , pp. 1-14
    • Caufour, P.S.1    Motta, M.C.2    Yamamura, A.M.3
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystogr. 26, 283-291.
    • (1993) J. Appl. Crystogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 42
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J. U., Luthy R., and Eisenberg, D. (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science 253, 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 43
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., Bowie, J. U., and Eisenberg, D. (1992) Assessment of protein models with three-dimensional profiles. Nature 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 44
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • Eisenberg, D., Luthy, R., and Bowie, J. U. (1997) VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol. 277, 396-404.
    • (1997) Methods Enzymol. , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 45
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. (1990) WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56, 29.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 46
    • 0027542118 scopus 로고
    • Quality-control of proteins models-directional atomic contact analysis
    • Vriend, G. and Sander, C. (1993) Quality-control of proteins models-directional atomic contact analysis. J. Appl. Crystallogr. 26, 47-60.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 47-60
    • Vriend, G.1    Sander, C.2
  • 47
    • 0029794372 scopus 로고    scopus 로고
    • Multiple specificities in the murine CD4+ and CD8+ T-cell response to dengue virus
    • Rothman, A. L., Kurane, I., and Ennis, F. A. (1996) Multiple specificities in the murine CD4+ and CD8+ T-cell response to dengue virus. J. Virol. 70, 6540-6546.
    • (1996) J. Virol. , vol.70 , pp. 6540-6546
    • Rothman, A.L.1    Kurane, I.2    Ennis, F.A.3
  • 48
    • 0034022803 scopus 로고    scopus 로고
    • Definition of an epitope on Japanese encephalitis virus (JEV) envelope protein recognized by JEV-specific murine CD8+ cytotoxic T lymphocytes
    • Takada, K., Masaki, H., Konishi, E., Takahashi, M., and Kurane, I. (2000) Definition of an epitope on Japanese encephalitis virus (JEV) envelope protein recognized by JEV-specific murine CD8+ cytotoxic T lymphocytes. Arch. Virol. 145, 523-534.
    • (2000) Arch. Virol. , vol.145 , pp. 523-534
    • Takada, K.1    Masaki, H.2    Konishi, E.3    Takahashi, M.4    Kurane, I.5
  • 49
    • 0036343564 scopus 로고    scopus 로고
    • Human cytotoxic T lymphocyte responses to live attenuated 17D yellow fever vaccine: Identification of HLA-B35-restricted CTL epitopes on non-structural proteins NS1, NS2b, NS3, and the structural protein E
    • Co, M. D., Terajima, M., Cruz, J., Ennis, F. A., and Rothman, A. L. (2002) Human cytotoxic T lymphocyte responses to live attenuated 17D yellow fever vaccine: identification of HLA-B35-restricted CTL epitopes on non-structural proteins NS1, NS2b, NS3, and the structural protein E. Virology 293, 151-163.
    • (2002) Virology , vol.293 , pp. 151-163
    • Co, M.D.1    Terajima, M.2    Cruz, J.3    Ennis, F.A.4    Rothman, A.L.5
  • 50
    • 0036343116 scopus 로고    scopus 로고
    • Yellow fever virus 17D envelope and NS3 proteins are major targets of the antiviral T cell response in mice
    • van der Most, R. G., Harrington, L. E., Giuggio, V., Mahar, P. L., and Ahmed, R. (2002) Yellow fever virus 17D envelope and NS3 proteins are major targets of the antiviral T cell response in mice. Virology 296, 117-124.
    • (2002) Virology , vol.296 , pp. 117-124
    • Van Der Most, R.G.1    Harrington, L.E.2    Giuggio, V.3    Mahar, P.L.4    Ahmed, R.5
  • 51
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A., and Thornton, J. M. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 52
    • 0025116324 scopus 로고
    • Flavivirus genome organization, expression, and replication
    • Chambers, T. J., Hahn, C. S., Galler, R., and Rice, C. M. (1990) Flavivirus genome organization, expression, and replication. Annu. Rev. Microbiol. 44, 649-688.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 649-688
    • Chambers, T.J.1    Hahn, C.S.2    Galler, R.3    Rice, C.M.4
  • 53
    • 4644372800 scopus 로고    scopus 로고
    • Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus
    • Volk, D. E., Beasley D. W., Kallick, D. A., Holbrook, M. R., Barrett A. D., and Gorenstein, D. G. (2004) Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus. J. Biol. Chem. 279, 38,755-38,761.
    • (2004) J. Biol. Chem. , vol.279
    • Volk, D.E.1    Beasley, D.W.2    Kallick, D.A.3    Holbrook, M.R.4    Barrett, A.D.5    Gorenstein, D.G.6
  • 54
    • 0242268520 scopus 로고    scopus 로고
    • Neuroadapted yellow fever virus 17D: Determinants in the envelope protein govern neuroinvasiveness for SCID mice
    • Nickells, M. and Chambers, T. J. (2003) Neuroadapted yellow fever virus 17D: determinants in the envelope protein govern neuroinvasiveness for SCID mice. J. Virol. 77, 12,232-12,242.
    • (2003) J. Virol. , vol.77
    • Nickells, M.1    Chambers, T.J.2
  • 55
    • 0022981913 scopus 로고
    • Loops in globular proteins: A novel category of secondary structure
    • Leszczynski, J. F. and Rose, G. D. (1986) Loops in globular proteins: a novel category of secondary structure. Science 234, 849-855.
    • (1986) Science , vol.234 , pp. 849-855
    • Leszczynski, J.F.1    Rose, G.D.2
  • 56
    • 2142827156 scopus 로고    scopus 로고
    • Dengue: Defining protective versus pathologic immunity
    • Rothman, A. L. (2004) Dengue: defining protective versus pathologic immunity. J. Clin. Investig. 113, 946-951.
    • (2004) J. Clin. Investig. , vol.113 , pp. 946-951
    • Rothman, A.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.